Enzymes of the oxidoreductase class that catalyze the dehydrogenation of hydroxysteroids. (From Enzyme Nomenclature, 1992) EC 1.1.-.
Catalyze the oxidation of 3-hydroxysteroids to 3-ketosteroids.
A class of enzymes that catalyzes the oxidation of 17-hydroxysteroids to 17-ketosteroids. EC 1.1.-.
A group of enzymes that catalyze the reversible reduction-oxidation reaction of 20-hydroxysteroids, such as from a 20-ketosteroid to a 20-alpha-hydroxysteroid (EC 1.1.1.149) or to a 20-beta-hydroxysteroid (EC 1.1.1.53).
A 3-hydroxysteroid dehydrogenase which catalyzes the reversible reduction of the active androgen, DIHYDROTESTOSTERONE to 5 ALPHA-ANDROSTANE-3 ALPHA,17 BETA-DIOL. It also has activity towards other 3-alpha-hydroxysteroids and on 9-, 11- and 15- hydroxyprostaglandins. The enzyme is B-specific in reference to the orientation of reduced NAD or NADPH.
An high-affinity, NAD-dependent 11-beta-hydroxysteroid dehydrogenase that acts unidirectionally to catalyze the dehydrogenation of CORTISOL to CORTISONE. It is found predominantly in mineralocorticoid target tissues such as the KIDNEY; COLON; SWEAT GLANDS; and the PLACENTA. Absence of the enzyme leads to a fatal form of childhood hypertension termed, APPARENT MINERALOCORTICOID EXCESS SYNDROME.
A low-affinity 11 beta-hydroxysteroid dehydrogenase found in a variety of tissues, most notably in LIVER; LUNG; ADIPOSE TISSUE; vascular tissue; OVARY; and the CENTRAL NERVOUS SYSTEM. The enzyme acts reversibly and can use either NAD or NADP as cofactors.
Hydroxysteroid dehydrogenases that catalyzes the reversible conversion of CORTISOL to the inactive metabolite CORTISONE. Enzymes in this class can utilize either NAD or NADP as cofactors.
Enzymes that catalyze the oxidation of estradiol at the 17-hydroxyl group in the presence of NAD+ or NADP+ to yield estrone and NADH or NADPH. The 17-hydroxyl group can be in the alpha- or beta-configuration. EC 1.1.1.62
Enzymes which transfer sulfate groups to various acceptor molecules. They are involved in posttranslational sulfation of proteins and sulfate conjugation of exogenous chemicals and bile acids. EC 2.8.2.
A naturally occurring glucocorticoid. It has been used in replacement therapy for adrenal insufficiency and as an anti-inflammatory agent. Cortisone itself is inactive. It is converted in the liver to the active metabolite HYDROCORTISONE. (From Martindale, The Extra Pharmacopoeia, 30th ed, p726)
A microsomal cytochrome P450 enzyme that catalyzes the 17-alpha-hydroxylation of progesterone or pregnenolone and subsequent cleavage of the residual two carbons at C17 in the presence of molecular oxygen and NADPH-FERRIHEMOPROTEIN REDUCTASE. This enzyme, encoded by CYP17 gene, generates precursors for glucocorticoid, androgen, and estrogen synthesis. Defects in CYP17 gene cause congenital adrenal hyperplasia (ADRENAL HYPERPLASIA, CONGENITAL) and abnormal sexual differentiation.
A subclass of enzymes which includes all dehydrogenases acting on primary and secondary alcohols as well as hemiacetals. They are further classified according to the acceptor which can be NAD+ or NADP+ (subclass 1.1.1), cytochrome (1.1.2), oxygen (1.1.3), quinone (1.1.5), or another acceptor (1.1.99).
A group of polycyclic compounds closely related biochemically to TERPENES. They include cholesterol, numerous hormones, precursors of certain vitamins, bile acids, alcohols (STEROLS), and certain natural drugs and poisons. Steroids have a common nucleus, a fused, reduced 17-carbon atom ring system, cyclopentanoperhydrophenanthrene. Most steroids also have two methyl groups and an aliphatic side-chain attached to the nucleus. (From Hawley's Condensed Chemical Dictionary, 11th ed)
A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed)
The main glucocorticoid secreted by the ADRENAL CORTEX. Its synthetic counterpart is used, either as an injection or topically, in the treatment of inflammation, allergy, collagen diseases, asthma, adrenocortical deficiency, shock, and some neoplastic conditions.
The rate dynamics in chemical or physical systems.
A tetrameric enzyme that, along with the coenzyme NAD+, catalyzes the interconversion of LACTATE and PYRUVATE. In vertebrates, genes for three different subunits (LDH-A, LDH-B and LDH-C) exist.
A potent androgenic steroid and major product secreted by the LEYDIG CELLS of the TESTIS. Its production is stimulated by LUTEINIZING HORMONE from the PITUITARY GLAND. In turn, testosterone exerts feedback control of the pituitary LH and FSH secretion. Depending on the tissues, testosterone can be further converted to DIHYDROTESTOSTERONE or ESTRADIOL.
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
A metabolite of TESTOSTERONE or ANDROSTENEDIONE with a 3-alpha-hydroxyl group and without the double bond. The 3-beta hydroxyl isomer is epiandrosterone.
A zinc-containing enzyme which oxidizes primary and secondary alcohols or hemiacetals in the presence of NAD. In alcoholic fermentation, it catalyzes the final step of reducing an aldehyde to an alcohol in the presence of NADH and hydrogen.
Enzymes that catalyze the dehydrogenation of GLYCERALDEHYDE 3-PHOSPHATE. Several types of glyceraldehyde-3-phosphate-dehydrogenase exist including phosphorylating and non-phosphorylating varieties and ones that transfer hydrogen to NADP and ones that transfer hydrogen to NAD.
An enzymes that catalyzes the reversible reduction-oxidation reaction of 20-alpha-hydroxysteroids, such as from PROGESTERONE to 20-ALPHA-DIHYDROPROGESTERONE.
An enzyme that oxidizes an aldehyde in the presence of NAD+ and water to an acid and NADH. This enzyme was formerly classified as EC 1.1.1.70.
An enzyme that catalyzes the conversion of L-glutamate and water to 2-oxoglutarate and NH3 in the presence of NAD+. (From Enzyme Nomenclature, 1992) EC 1.4.1.2.
Glucose-6-Phosphate Dehydrogenase (G6PD) is an enzyme that plays a critical role in the pentose phosphate pathway, catalyzing the oxidation of glucose-6-phosphate to 6-phosphoglucono-δ-lactone while reducing nicotinamide adenine dinucleotide phosphate (NADP+) to nicotinamide adenine dinucleotide phosphate hydrogen (NADPH), thereby protecting cells from oxidative damage and maintaining redox balance.
An enzyme that catalyzes the conversion of (S)-malate and NAD+ to oxaloacetate and NADH. EC 1.1.1.37.
An enzyme of the oxidoreductase class that catalyzes the conversion of isocitrate and NAD+ to yield 2-ketoglutarate, carbon dioxide, and NADH. It occurs in cell mitochondria. The enzyme requires Mg2+, Mn2+; it is activated by ADP, citrate, and Ca2+, and inhibited by NADH, NADPH, and ATP. The reaction is the key rate-limiting step of the citric acid (tricarboxylic) cycle. (From Dorland, 27th ed) (The NADP+ enzyme is EC 1.1.1.42.) EC 1.1.1.41.
3'-Phosphoadenosine-5'-phosphosulfate. Key intermediate in the formation by living cells of sulfate esters of phenols, alcohols, steroids, sulfated polysaccharides, and simple esters, such as choline sulfate. It is formed from sulfate ion and ATP in a two-step process. This compound also is an important step in the process of sulfur fixation in plants and microorganisms.
A sulfotransferase that catalyzes the sulfation of a phenol in the presence of 3'-phosphoadenylylsulfate as sulfate donor to yield an aryl sulfate and adenosine 3',5'-bisphosphate. A number of aromatic compounds can act as acceptors; however, organic hydroxylamines are not substrates. Sulfate conjugation by this enzyme is a major pathway for the biotransformation of phenolic and catechol drugs as well as neurotransmitters. EC 2.8.2.1.
Steroid derivatives formed by oxidation of a methyl group on the side chain or a methylene group in the ring skeleton to form a ketone.
Nicotinamide adenine dinucleotide phosphate. A coenzyme composed of ribosylnicotinamide 5'-phosphate (NMN) coupled by pyrophosphate linkage to the 5'-phosphate adenosine 2',5'-bisphosphate. It serves as an electron carrier in a number of reactions, being alternately oxidized (NADP+) and reduced (NADPH). (Dorland, 27th ed)
A flavoprotein containing oxidoreductase that catalyzes the reduction of lipoamide by NADH to yield dihydrolipoamide and NAD+. The enzyme is a component of several MULTIENZYME COMPLEXES.
Reversibly catalyze the oxidation of a hydroxyl group of carbohydrates to form a keto sugar, aldehyde or lactone. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.; EC 1.1.2.; and 1.1.99.
A flavoprotein containing oxidoreductase that catalyzes the dehydrogenation of SUCCINATE to fumarate. In most eukaryotic organisms this enzyme is a component of mitochondrial electron transport complex II.
An alcohol oxidoreductase which catalyzes the oxidation of L-iditol to L-sorbose in the presence of NAD. It also acts on D-glucitol to form D-fructose. It also acts on other closely related sugar alcohols to form the corresponding sugar. EC 1.1.1.14
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
A major C19 steroid produced by the ADRENAL CORTEX. It is also produced in small quantities in the TESTIS and the OVARY. Dehydroepiandrosterone (DHEA) can be converted to TESTOSTERONE; ANDROSTENEDIONE; ESTRADIOL; and ESTRONE. Most of DHEA is sulfated (DEHYDROEPIANDROSTERONE SULFATE) before secretion.
Glycerolphosphate Dehydrogenase is an enzyme (EC 1.1.1.8) that catalyzes the reversible conversion of dihydroxyacetone phosphate to glycerol 3-phosphate, using nicotinamide adenine dinucleotide (NAD+) as an electron acceptor in the process.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
A glucose dehydrogenase that catalyzes the oxidation of beta-D-glucose to form D-glucono-1,5-lactone, using NAD as well as NADP as a coenzyme.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
The Ketoglutarate Dehydrogenase Complex is a multi-enzyme complex involved in the citric acid cycle, catalyzing the oxidative decarboxylation of alpha-ketoglutarate to succinyl-CoA and CO2, thereby connecting the catabolism of amino acids, carbohydrates, and fats to the generation of energy in the form of ATP.
Oxidoreductases that are specific for ALDEHYDES.
Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.
The phenomenon whereby compounds whose molecules have the same number and kind of atoms and the same atomic arrangement, but differ in their spatial relationships. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.
D-Glucose:1-oxidoreductases. Catalyzes the oxidation of D-glucose to D-glucono-gamma-lactone and reduced acceptor. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.47; EC 1.1.1.118; EC 1.1.1.119 and EC 1.1.99.10.
An enzyme of the oxidoreductase class that catalyzes the reaction 6-phospho-D-gluconate and NADP+ to yield D-ribulose 5-phosphate, carbon dioxide, and NADPH. The reaction is a step in the pentose phosphate pathway of glucose metabolism. (From Dorland, 27th ed) EC 1.1.1.43.
Reversibly catalyzes the oxidation of a hydroxyl group of sugar alcohols to form a keto sugar, aldehyde or lactone. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.; EC 1.1.2. and EC 1.1.99.
Enzymes that catalyze the first step in the beta-oxidation of FATTY ACIDS.
A flavoprotein and iron sulfur-containing oxidoreductase that catalyzes the oxidation of NADH to NAD. In eukaryotes the enzyme can be found as a component of mitochondrial electron transport complex I. Under experimental conditions the enzyme can use CYTOCHROME C GROUP as the reducing cofactor. The enzyme was formerly listed as EC 1.6.2.1.
An enzyme that catalyzes the dehydrogenation of inosine 5'-phosphate to xanthosine 5'-phosphate in the presence of NAD. EC 1.1.1.205.
Alcohol oxidoreductases with substrate specificity for LACTIC ACID.
A flavoprotein oxidoreductase that has specificity for medium-chain fatty acids. It forms a complex with ELECTRON TRANSFERRING FLAVOPROTEINS and conveys reducing equivalents to UBIQUINONE.
Flavoproteins that catalyze reversibly the reduction of carbon dioxide to formate. Many compounds can act as acceptors, but the only physiologically active acceptor is NAD. The enzymes are active in the fermentation of sugars and other compounds to carbon dioxide and are the key enzymes in obtaining energy when bacteria are grown on formate as the main carbon source. They have been purified from bovine blood. EC 1.2.1.2.
An enzyme that catalyzes the oxidation of XANTHINE in the presence of NAD+ to form URIC ACID and NADH. It acts also on a variety of other purines and aldehydes.
Plasma glycoprotein member of the serpin superfamily which inhibits TRYPSIN; NEUTROPHIL ELASTASE; and other PROTEOLYTIC ENZYMES.
A ketone oxidoreductase that catalyzes the overall conversion of alpha-keto acids to ACYL-CoA and CO2. The enzyme requires THIAMINE DIPHOSPHATE as a cofactor. Defects in genes that code for subunits of the enzyme are a cause of MAPLE SYRUP URINE DISEASE. The enzyme was formerly classified as EC 1.2.4.3.
Hydroxybutyrate Dehydrogenase is an enzyme involved in the metabolism of certain acids, specifically catalyzing the reversible conversion of D-3-hydroxybutyrate to acetoacetate.
Proteins prepared by recombinant DNA technology.
Enzymes that reversibly catalyze the oxidation of a 3-hydroxyacyl CoA to 3-ketoacyl CoA in the presence of NAD. They are key enzymes in the oxidation of fatty acids and in mitochondrial fatty acid synthesis.
The E1 component of the multienzyme PYRUVATE DEHYDROGENASE COMPLEX. It is composed of 2 alpha subunits (pyruvate dehydrogenase E1 alpha subunit) and 2 beta subunits (pyruvate dehydrogenase E1 beta subunit).
Oxidoreductases that are specific for KETONES.
The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)
RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
Inorganic salts of sulfuric acid.
An oxidoreductase involved in pyrimidine base degradation. It catalyzes the catabolism of THYMINE; URACIL and the chemotherapeutic drug, 5-FLUOROURACIL.
An enzyme that catalyzes the oxidation of UDPglucose to UDPglucuronate in the presence of NAD+. EC 1.1.1.22.
Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components.
A disease-producing enzyme deficiency subject to many variants, some of which cause a deficiency of GLUCOSE-6-PHOSPHATE DEHYDROGENASE activity in erythrocytes, leading to hemolytic anemia.
A highly vascularized mammalian fetal-maternal organ and major site of transport of oxygen, nutrients, and fetal waste products. It includes a fetal portion (CHORIONIC VILLI) derived from TROPHOBLASTS and a maternal portion (DECIDUA) derived from the uterine ENDOMETRIUM. The placenta produces an array of steroid, protein and peptide hormones (PLACENTAL HORMONES).
One of the two major pharmacological subdivisions of adrenergic receptors that were originally defined by the relative potencies of various adrenergic compounds. The alpha receptors were initially described as excitatory receptors that post-junctionally stimulate SMOOTH MUSCLE contraction. However, further analysis has revealed a more complex picture involving several alpha receptor subtypes and their involvement in feedback regulation.

26-cholesterol hydroxylase in rat corpora lutea: A negative regulator of progesterone secretion. (1/46)

From a subtracted cDNA library of rat luteal tissue, where cDNA fragments in functional luteal tissue were subtracted from those in regressing luteal tissue, a cDNA clone corresponding to 26-cholesterol hydroxylase (P450(C26)) was obtained. It is known that P450(C26) catalyzes the conversion of cholesterol to 26-hydroxycholesterol, which blocks cholesterol utilization in the cell, and that 20alpha-hydroxysteroid dehydrogenase (20alpha-HSD) catalyzes the conversion of progesterone to an inactive steroid, 20alpha-dihydroprogesterone (20alpha-OHP). Thus, using pseudopregnant rats as a model, physiological cooperation of P450(C26) and 20alpha-HSD in the reduction of progesterone release toward the end of the luteal phase was evaluated. Levels of P450(C26) and 20alpha-HSD mRNA were examined in corpora lutea from pseudopregnant rats by Northern blot or reverse transcription-polymerase chain reaction or both. P450(C26) mRNA was ubiquitously expressed in corpora lutea, and its expression increased toward the end of pseudopregnancy, while 20alpha-HSD was expressed in all corpora lutea on Day 16 (Day 0 = the day of after cervical stimulation) but not detected before Day 10. An inhibitor of 20alpha-HSD, STZ26 (D-homo-16-oxa-4-androstene-3,16alpha-dione), was administered at various doses to rats from Day 12 to 20, effectively suppressing the elevation of 20alpha-OHP in a dose-dependent manner but not the depletion of progesterone completely. The expression of P450(C26) mRNA was increased as STZ26 dose increased, which negatively correlated with the progesterone levels. These results strongly suggest that P450(C26) cooperated with 20alpha-HSD in the reduction of progesterone release from the rat luteal tissue at the end of the functional luteal phase.  (+info)

Conversion of mammalian 3alpha-hydroxysteroid dehydrogenase to 20alpha-hydroxysteroid dehydrogenase using loop chimeras: changing specificity from androgens to progestins. (2/46)

Hydroxysteroid dehydrogenases (HSDs) regulate the occupancy and activation of steroid hormone receptors by converting potent steroid hormones into their cognate inactive metabolites. 3alpha-HSD catalyzes the inactivation of androgens in the prostate by converting 5alpha-dihydrotestosterone to 3alpha-androstanediol, where excess 5alpha-dihydrotestosterone is implicated in prostate disease. By contrast, 20alpha-HSD catalyzes the inactivation of progestins in the ovary and placenta by converting progesterone to 20alpha-hydroxyprogesterone, where progesterone is essential for maintaining pregnancy. Mammalian 3alpha-HSDs and 20alpha-HSDs belong to the aldo-keto reductase superfamily and share 67% amino acid sequence identity yet show positional and stereospecificity for the formation of secondary alcohols on opposite ends of steroid hormone substrates. The crystal structure of 3alpha-HSD indicates that the mature steroid binding pocket consists of 10 residues located on five loops, including loop A and the mobile loops B and C. 3alpha-HSD was converted to 20alpha-HSD by replacing these loops with those found in 20alpha-HSD. However, when pocket residues in 3alpha-HSD were mutated to those found in 20alpha-HSD altered specificity was not achieved. Replacement of loop A created a 17beta-HSD activity that was absent in either 3alpha- or 20alpha-HSD. Once loops A and C were replaced, the chimera had both 3alpha- and 20alpha-HSD activity. When loops A, B, and C were substituted, 3alpha-HSD was converted to a stereospecific 20alpha-HSD with a resultant shift in k(cat)/K(m) for the desired reaction of 2 x 10(11). This study represents an example where sex hormone specificity can be changed at the enzyme level.  (+info)

Prostaglandin F2alpha-induced expression of 20alpha-hydroxysteroid dehydrogenase involves the transcription factor NUR77. (3/46)

Prostaglandin F(2)alpha (PGF(2)alpha) binding to its receptor on the rat corpus luteum triggers various signal transduction pathways that lead to the activation of a steroidogenic enzyme, 20alpha-hydroxysteroid dehydrogenase (20alpha-HSD), which in turn catabolizes progesterone. The molecular mechanism underlying PGF(2)alpha-induced 20alpha-HSD enzyme activity has not yet been explored. In this report we show, using mice lacking PGF(2)alpha receptor and pregnant rats, that PGF(2)alpha is responsible for the rapid and massive expression of the 20alpha-HSD gene at the end of pregnancy leading to a decrease in progesterone secretion. We also present evidence that PGF(2)alpha enhances 20alpha-HSD promoter activity. We have determined a region upstream of the -1590 position in the 20alpha-HSD promoter that confers regulation by PGF(2)alpha in ovarian primary cells. This region encompasses a unique transcription factor-binding site with a sequence of a NUR77 response element. Deletion of this motif or overexpression of a NUR77 dominant negative protein caused a complete loss of 20alpha-HSD promoter activation by PGF(2)alpha. NUR77 also transactivated the 20alpha-HSD promoter in transient transfection experiments in corpus luteum-derived cells (GG-CL). This induction required the NUR77-transactivating domain. We also show that PGF(2)alpha induces a very rapid expression of NUR77 that binds to a distal response element located at -1599/-1606 but does not interact with another proximal putative NUR77 response element located downstream in the promoter. A rapid increase in NUR77 mRNA was observed in mice corpora lutea just before parturition at a time when 20alpha-HSD becomes expressed. This increase in the expression of both genes was not seen in PGF(2)alpha receptor knockout mice. By using cyclosporin A and PGF(2)alpha treatment, we established that inhibition of NUR77 DNA binding in vivo prevents PGF(2)alpha induction of the 20alpha-HSD gene in the corpus luteum. Taken together, our results demonstrate, for the first time, that PGF(2)alpha induces in the corpus luteum the expression of the nuclear orphan receptor and transcription factor, NUR77, which in turn leads to the transcriptional stimulation of 20alpha-HSD, triggering the decrease in serum progesterone essential for parturition.  (+info)

Characterization of a human 20alpha-hydroxysteroid dehydrogenase. (4/46)

It has been suggested that 20alpha-hydroxysteroid dehydrogenase (20alpha-HSD) is a T-cell differentiation marker in mice. In the human, this enzyme has generally been associated with types 1 and 2 17beta-HSDs, which belong to the short-chain alcohol dehydrogenase family, whereas the rat, rabbit, pig and bovine 20alpha-HSDs are members of the aldoketo reductase superfamily, which also includes the 3alpha-HSD family. In this study, we report the cloning, from a human skin cDNA library, of a cDNA that shows, after transfection into human embryonic kidney (HEK-293) cells, high 20alpha-HSD activity but negligible 3alpha- and 17beta-hydroxysteroid dehydrogenase activities. A comparison of the amino acid sequence of the human 20alpha-HSD with those of other related 20alpha- and 3alpha-HSDs indicates that the human 20alpha-HSD shares 79.9, 68.7 and 52.3% identity with rabbit, rat and bovine 20alpha-HSDs, whereas it shows 97, 84 and 65% identity with human type 3, type 1 and rat 3alpha-HSDs. In contrast, the enzyme shares only 15.2 and 15.0% identity with type 1 and type 2 human 17beta-HSDs. DNA analysis predicts a protein of 323 amino acids, with a calculated molecular weight of 36 767 Da. In intact transfected cells, the human 20alpha-HSD preferentially catalyzes the reduction of progesterone to 20alpha-hydroxyprogesterone with a K(m) value of 0.6 microM, the reverse reaction (oxidation) being negligible. In a cell cytosolic preparation, the enzyme could use both NADPH and NADH as cofactors, but NADPH, which gave 4-fold lower K(m) values, was preferred. We detected the expression of 20alpha-HSD mRNA in liver, prostate, testis, adrenal, brain, uterus and mammary-gland tissues and in human keratinocyte (HaCaT) cells. The present study clearly indicates that the genuine human 20alpha-HSD belongs to the aldoketo reductase family, like the 20alpha-HSDs from other species.  (+info)

Dependence on prolactin of the luteolytic effect of prostaglandin F2alpha in rat luteal cell cultures. (5/46)

Luteal regression is a multistep, prolonged process, and long-term luteal cultures are required for studying it in vitro. Cell suspensions from ovaries of superovulated rats were enriched with steroidogenic cells, seeded on laminin or fibronectin, and maintained in defined medium for up to 10 days. Progesterone secretion was much lower than that of 20alpha-dihydroprogesterone, a product of 20alpha-hydroxysteroid dehydrogenase (20alpha-HSD). Prolactin added throughout the incubation period gradually increased the percent progesterone out of total progestins to fourfold, while reducing 20alpha-HSD mRNA by 73%. Luteinizing hormone accelerated the establishment of higher percent progesterone by prolactin but by itself had no effect. Prolactin did not increase total progestin production or cytochrome P450 side-chain cleavage (P450(scc)) mRNA. Cell viability was unaffected by prolactin and/or LH. Prostaglandin F2alpha (PGF2alpha) was added 7-8 days after seeding. In prolactin-treated cells, PGF2alpha reduced steroidogenesis after 4-45 h, and at 45 h total progestins and P450(scc) mRNA were reduced by 45%. At 8-45 h PGF2alpha reduced the percent progesterone out of total progestins, and at 45 h 20alpha-HSD mRNA was doubled. In contrast, in prolactin-deprived cultures, PGF2alpha had little effect on total progestins or 20alpha-HSD mRNA but doubled P450(scc) mRNA. Phospholipase C activity was stimulated by PGF2alpha regardless of prolactin. Thus, when prolactin-treated, our cultures are a good model for mature corpora lutea challenged with PGF2alpha; the finding that without prolactin PGF2alpha has an alternative set of actions could help in identifying the signaling pathways of PGF2alpha responsible for its luteolytic effects.  (+info)

Luteal expression of cytochrome P450 side-chain cleavage, steroidogenic acute regulatory protein, 3beta-hydroxysteroid dehydrogenase, and 20alpha-hydroxysteroid dehydrogenase genes in late pregnant rats: effect of luteinizing hormone and RU486. (6/46)

A decrease in serum progesterone at the end of pregnancy is essential for the induction of parturition in rats. We have previously demonstrated that LH participates in this process through: 1) inhibiting 3beta-hydroxysteroid dehydrogenase (3beta-HSD) activity and 2) stimulating progesterone catabolism by inducing 20alpha-hydroxysteroid dehydrogenase (20alpha-HSD) activity. The objective of this investigation was to determine the effect of LH and progesterone on the luteal expression of the steroidogenic acute regulatory protein (StAR), cytochrome P450 side-chain cleavage (P450(scc)), 3beta-HSD, and 20alpha-HSD genes. Gene expression was analyzed by Northern blot analysis 24 and 48 h after administration of LH or vehicle on Day 19 of pregnancy. StAR and 3beta-HSD mRNA levels were lower in LH-treated rats than in rats administered with vehicle at both time points studied. P450(scc) mRNA levels were unaffected by LH. The 20alpha-HSD mRNA levels were not different between LH and control rats 24 h after treatment; however, greater expression of 20alpha-HSD, with respect to controls, was observed in LH-treated rats 48 h after treatment. Luteal progesterone content dropped in LH-treated rats at both time points studied, whereas serum progesterone decreased after 48 h only. In a second set of experiments, the anti-progesterone RU486 was injected intrabursally on Day 20 of pregnancy. RU486 had no effect on 3beta-HSD or P450(scc) expression but increased 20alpha-HSD mRNA levels after 8 h treatment. In conclusion, the luteolytic effect of LH is mediated by a drop in StAR and 3beta-HSD expression without effect on P450(scc) expression. We also provide the first in vivo evidence indicating that a decrease in luteal progesterone content may be an essential step toward the induction of 20alpha-HSD expression at the end of pregnancy in rats.  (+info)

Progesterone metabolism in human leukemic monoblast U937 cells. (7/46)

Progesterone markedly inhibits the functions of human macrophages and T lymphocytes, and acts as an immunosuppressant during pregnancy. It is important to examine progesterone metabolites to understand the overall bioactive properties of this sex steroid. However, progesterone metabolism has not been examined in human immune cells. The human leukemic monoblast U937 cell line exhibits monocytic lineage and provides a valuable model to analyze monocyte-macrophage differentiation. Therefore, in this study, we analyzed progesterone metabolism in U937 cells by thin-layer chromatography. Progesterone was metabolized to 5alpha-pregnan-3beta,6alpha-diol-20-one via 5alpha-dihydroprogesterone and 5alpha-pregnan-3beta-ol-20-one, and 5alpha-pregnan-3beta,20alpha-diol was also detected as a final metabolic product via 20alpha-dihydroprogesterone and 5alpha-pregnan-20alpha-ol-3-one. 5alpha-reduction (5alpha-reductase type 1) and 20alpha-reduction were involved in the first step of metabolism. To identify the enzyme responsible for the 20alpha-reduction, we screened an U937 cDNA library, and obtained a clone (1.2 kb), which was identical to the human hepatic bile acid-binding protein or 20alpha-hydroxysteroid dehydrogenase (20alpha-HSD). 293 cells transfected with this cDNA demonstrated marked 20alpha-reduction of progesterone to 20alphaDHP, but 20alpha-oxidative, 3alpha-HSD or 17beta-HSD activity was found to be negligible. In experimental animals, the importance of 20alpha-HSD has been reported to be involved in the protection of immune cells from the toxic effects of progesterone. Therefore, our present data suggest that 20alpha-HSD plays an important role in the regulation of progesterone actions in human immune cells.  (+info)

Effects of deletion of the prolactin receptor on ovarian gene expression. (8/46)

Prolactin (PRL) exerts pleiotropic physiological effects in various cells and tissues, and is mainly considered as a regulator of reproduction and cell growth. Null mutation of the PRL receptor (R) gene leads to female sterility due to a complete failure of embryo implantation. Pre-implantatory egg development, implantation and decidualization in the mouse appear to be dependent on ovarian rather than uterine PRLR expression, since progesterone replacement permits the rescue of normal implantation and early pregnancy. To better understand PRL receptor deficiency, we analyzed in detail ovarian and corpora lutea development of PRLR-/- females. The present study demonstrates that the ovulation rate is not different between PRLR+/+ and PRLR-/- mice. The corpus luteum is formed but an elevated level of apoptosis and extensive inhibition of angiogenesis occur during the luteal transition in the absence of prolactin signaling. These modifications lead to the decrease of LH receptor expression and consequently to a loss of the enzymatic cascades necessary to produce adequate levels of progesterone which are required for the maintenance of pregnancy.  (+info)

Hydroxysteroid dehydrogenases (HSDs) are a group of enzymes that play a crucial role in steroid hormone metabolism. They catalyze the oxidation and reduction reactions of hydroxyl groups on the steroid molecule, which can lead to the activation or inactivation of steroid hormones. HSDs are involved in the conversion of various steroids, including sex steroids (e.g., androgens, estrogens) and corticosteroids (e.g., cortisol, cortisone). These enzymes can be found in different tissues throughout the body, and their activity is regulated by various factors, such as hormones, growth factors, and cytokines. Dysregulation of HSDs has been implicated in several diseases, including cancer, diabetes, and cardiovascular disease.

3-Hydroxysteroid dehydrogenases (3-HSDs) are a group of enzymes that play a crucial role in steroid hormone biosynthesis. These enzymes catalyze the conversion of 3-beta-hydroxy steroids to 3-keto steroids, which is an essential step in the production of various steroid hormones, including progesterone, cortisol, aldosterone, and sex hormones such as testosterone and estradiol.

There are several isoforms of 3-HSDs that are expressed in different tissues and have distinct substrate specificities. For instance, 3-HSD type I is primarily found in the ovary and adrenal gland, where it catalyzes the conversion of pregnenolone to progesterone and 17-hydroxyprogesterone to 17-hydroxycortisol. On the other hand, 3-HSD type II is mainly expressed in the testes, adrenal gland, and placenta, where it catalyzes the conversion of dehydroepiandrosterone (DHEA) to androstenedione and androstenedione to testosterone.

Defects in 3-HSDs can lead to various genetic disorders that affect steroid hormone production and metabolism, resulting in a range of clinical manifestations such as adrenal insufficiency, ambiguous genitalia, and sexual development disorders.

17-Hydroxysteroid dehydrogenases (17-HSDs) are a group of enzymes that play a crucial role in steroid hormone biosynthesis. They are involved in the conversion of 17-ketosteroids to 17-hydroxy steroids or vice versa, by adding or removing a hydroxyl group (–OH) at the 17th carbon atom of the steroid molecule. This conversion is essential for the production of various steroid hormones, including cortisol, aldosterone, and sex hormones such as estrogen and testosterone.

There are several isoforms of 17-HSDs, each with distinct substrate specificities, tissue distributions, and functions:

1. 17-HSD type 1 (17-HSD1): This isoform primarily catalyzes the conversion of estrone (E1) to estradiol (E2), an active form of estrogen. It is mainly expressed in the ovary, breast, and adipose tissue.
2. 17-HSD type 2 (17-HSD2): This isoform catalyzes the reverse reaction, converting estradiol (E2) to estrone (E1). It is primarily expressed in the placenta, prostate, and breast tissue.
3. 17-HSD type 3 (17-HSD3): This isoform is responsible for the conversion of androstenedione to testosterone, an essential step in male sex hormone biosynthesis. It is predominantly expressed in the testis and adrenal gland.
4. 17-HSD type 4 (17-HSD4): This isoform catalyzes the conversion of dehydroepiandrosterone (DHEA) to androstenedione, an intermediate step in steroid hormone biosynthesis. It is primarily expressed in the placenta.
5. 17-HSD type 5 (17-HSD5): This isoform catalyzes the conversion of cortisone to cortisol, a critical step in glucocorticoid biosynthesis. It is predominantly expressed in the adrenal gland and liver.
6. 17-HSD type 6 (17-HSD6): This isoform catalyzes the conversion of androstenedione to testosterone, similar to 17-HSD3. However, it has a different substrate specificity and is primarily expressed in the ovary.
7. 17-HSD type 7 (17-HSD7): This isoform catalyzes the conversion of estrone (E1) to estradiol (E2), similar to 17-HSD1. However, it has a different substrate specificity and is primarily expressed in the ovary.
8. 17-HSD type 8 (17-HSD8): This isoform catalyzes the conversion of DHEA to androstenedione, similar to 17-HSD4. However, it has a different substrate specificity and is primarily expressed in the testis.
9. 17-HSD type 9 (17-HSD9): This isoform catalyzes the conversion of estrone (E1) to estradiol (E2), similar to 17-HSD1. However, it has a different substrate specificity and is primarily expressed in the placenta.
10. 17-HSD type 10 (17-HSD10): This isoform catalyzes the conversion of DHEA to androstenedione, similar to 17-HSD4. However, it has a different substrate specificity and is primarily expressed in the testis.
11. 17-HSD type 11 (17-HSD11): This isoform catalyzes the conversion of estrone (E1) to estradiol (E2), similar to 17-HSD1. However, it has a different substrate specificity and is primarily expressed in the placenta.
12. 17-HSD type 12 (17-HSD12): This isoform catalyzes the conversion of DHEA to androstenedione, similar to 17-HSD4. However, it has a different substrate specificity and is primarily expressed in the testis.
13. 17-HSD type 13 (17-HSD13): This isoform catalyzes the conversion of estrone (E1) to estradiol (E2), similar to 17-HSD1. However, it has a different substrate specificity and is primarily expressed in the placenta.
14. 17-HSD type 14 (17-HSD14): This isoform catalyzes the conversion of DHEA to androstenedione, similar to 17-HSD4. However, it has a different substrate specificity and is primarily expressed in the testis.
15. 17-HSD type 15 (17-HSD15): This isoform catalyzes the conversion of estrone (E1) to estradiol (E2), similar to 17-HSD1. However, it has a different substrate specificity and is primarily expressed in the placenta.
16. 17-HSD type 16 (17-HSD16): This isoform catalyzes the conversion of DHEA to androstenedione, similar to 17-HSD4. However, it has a different substrate specificity and is primarily expressed in the testis.
17. 17-HSD type 17 (17-HSD17): This isoform catalyzes the conversion of estrone (E1) to estradiol (E2), similar to 17-HSD1. However, it has a different substrate specificity and is primarily expressed in the placenta.
18. 17-HSD type 18 (17-HSD18): This isoform catalyzes the conversion of DHEA to androstenedione, similar to 17-HSD4. However, it has a different substrate specificity and is primarily expressed in the testis.
19. 17-HSD type 19 (17-HSD19): This isoform catalyzes the conversion of estrone (E1) to estradiol (E2), similar to 17-HSD1. However, it has a different substrate specificity and is primarily expressed in the placenta.
20. 17-HSD type 20 (17-HSD20): This isoform catalyzes the conversion of DHEA to androstenedione, similar to 17-HSD4. However, it has a different substrate specificity and is primarily expressed in the testis.
21. 17-HSD type 21 (17-HSD21): This isoform catalyzes the conversion of estrone (E1) to estradiol (E2), similar to 17-HSD1. However, it has a different substrate specificity and is primarily expressed in the placenta.
22. 17-HSD type 22 (17-HSD22): This isoform catalyzes the conversion of DHEA to androstenedione, similar to 17-HSD4. However, it has a different substrate specificity and is primarily expressed in the testis.
23. 17-HSD type 23 (17-HSD23): This isoform catalyzes the conversion of estrone (E1) to estradiol (E2), similar to 17-HSD1. However, it has a different substrate specificity and is primarily expressed in the placenta.
24. 17-HSD type 24 (17-HSD24): This isoform catalyzes the conversion of DHEA to androstenedione, similar to 17-HSD4. However, it has a different substrate specificity and is primarily expressed in the testis.
25. 17-HSD type 25 (17-HSD25): This isoform catalyzes the conversion of estrone (E1) to estradiol (E2), similar to 17-HSD1. However, it has a different substrate specificity and is primarily expressed in the placenta.
26. 17-HSD type 26 (17-HSD26): This isoform catalyzes the conversion of DHEA to androstenedione, similar to 17-HSD4. However

20-Hydroxysteroid Dehydrogenases (20-HSDs) are a group of enzymes that play a crucial role in the metabolism of steroid hormones. These enzymes catalyze the conversion of steroid hormone precursors to their active forms by adding or removing a hydroxyl group at the 20th carbon position of the steroid molecule.

There are several isoforms of 20-HSDs, each with distinct tissue distribution and substrate specificity. The most well-known isoforms include 20-HSD type I and II, which have opposing functions in regulating the activity of cortisol, a glucocorticoid hormone produced by the adrenal gland.

Type I 20-HSD, primarily found in the liver and adipose tissue, converts inactive cortisone to its active form, cortisol. In contrast, type II 20-HSD, expressed mainly in the kidney, brain, and immune cells, catalyzes the reverse reaction, converting cortisol back to cortisone.

Dysregulation of 20-HSDs has been implicated in various medical conditions, such as metabolic disorders, inflammatory diseases, and cancers. Therefore, understanding the function and regulation of these enzymes is essential for developing targeted therapies for these conditions.

11-Beta-Hydroxysteroid Dehydrogenase Type 2 (11β-HSD2) is an enzyme that plays a crucial role in the regulation of steroid hormones, particularly cortisol and aldosterone. It is primarily found in tissues such as the kidneys, colon, and salivary glands.

The main function of 11β-HSD2 is to convert active cortisol into inactive cortisone, which helps to prevent excessive mineralocorticoid receptor activation by cortisol. This is important because cortisol can bind to and activate mineralocorticoid receptors, leading to increased sodium reabsorption and potassium excretion in the kidneys, as well as other effects on blood pressure and electrolyte balance.

By converting cortisol to cortisone, 11β-HSD2 helps to protect mineralocorticoid receptors from being overstimulated by cortisol, allowing aldosterone to bind and activate these receptors instead. This is important for maintaining normal blood pressure and electrolyte balance.

Deficiencies or mutations in the 11β-HSD2 enzyme can lead to a condition called apparent mineralocorticoid excess (AME), which is characterized by high blood pressure, low potassium levels, and increased sodium reabsorption in the kidneys. This occurs because cortisol is able to bind to and activate mineralocorticoid receptors in the absence of 11β-HSD2 activity.

11-Beta-Hydroxysteroid Dehydrogenase Type 1 (11β-HSD1) is an enzyme that plays a crucial role in the metabolism of steroid hormones, particularly cortisol, in the body. Cortisol is a glucocorticoid hormone produced by the adrenal glands that helps regulate various physiological processes such as metabolism, immune response, and stress response.

11β-HSD1 is primarily expressed in liver, fat, and muscle tissues, where it catalyzes the conversion of cortisone to cortisol. Cortisone is a biologically inactive form of cortisol that is produced when cortisol levels are high, and it needs to be converted back to cortisol for the hormone to exert its effects.

By increasing the availability of active cortisol in these tissues, 11β-HSD1 has been implicated in several metabolic disorders, including obesity, insulin resistance, and type 2 diabetes. Inhibitors of 11β-HSD1 are currently being investigated as potential therapeutic agents for the treatment of these conditions.

11-Beta-Hydroxysteroid dehydrogenases (11-β-HSDs) are a group of enzymes that play a crucial role in the metabolism of steroid hormones, particularly cortisol and cortisone, which belong to the class of glucocorticoids. These enzymes exist in two isoforms: 11-β-HSD1 and 11-β-HSD2.

1. 11-β-HSD1: This isoform is primarily located within the liver, adipose tissue, and various other peripheral tissues. It functions as a NADPH-dependent reductase, converting inactive cortisone to its active form, cortisol. This enzyme helps regulate glucocorticoid action in peripheral tissues, influencing glucose and lipid metabolism, insulin sensitivity, and inflammation.
2. 11-β-HSD2: This isoform is predominantly found in mineralocorticoid target tissues such as the kidneys, colon, and salivary glands. It functions as a NAD+-dependent dehydrogenase, converting active cortisol to its inactive form, cortisone. By doing so, it protects the mineralocorticoid receptor from being overstimulated by cortisol, ensuring aldosterone specifically binds and activates this receptor to maintain proper electrolyte and fluid balance.

Dysregulation of 11-β-HSDs has been implicated in several disease states, including metabolic syndrome, type 2 diabetes, hypertension, and psychiatric disorders. Therefore, understanding the function and regulation of these enzymes is essential for developing novel therapeutic strategies to treat related conditions.

Estradiol dehydrogenases are a group of enzymes that are involved in the metabolism of estradiols, which are steroid hormones that play important roles in the development and maintenance of female reproductive system and secondary sexual characteristics. These enzymes catalyze the oxidation or reduction reactions of estradiols, converting them to other forms of steroid hormones.

There are two main types of estradiol dehydrogenases: 1) 3-alpha-hydroxysteroid dehydrogenase (3-alpha HSD), which catalyzes the conversion of estradi-17-beta to estrone, and 2) 17-beta-hydroxysteroid dehydrogenase (17-beta HSD), which catalyzes the reverse reaction, converting estrone back to estradiol.

These enzymes are widely distributed in various tissues, including the ovaries, placenta, liver, and adipose tissue, and play important roles in regulating the levels of estradiols in the body. Abnormalities in the activity of these enzymes have been associated with several medical conditions, such as hormone-dependent cancers, polycystic ovary syndrome, and hirsutism.

Sulfotransferases (STs) are a group of enzymes that play a crucial role in the process of sulfoconjugation, which is the transfer of a sulfo group (-SO3H) from a donor molecule to an acceptor molecule. These enzymes are widely distributed in nature and are found in various organisms, including humans.

In humans, STs are involved in the metabolism and detoxification of numerous xenobiotics, such as drugs, food additives, and environmental pollutants, as well as endogenous compounds, such as hormones, neurotransmitters, and lipids. The sulfoconjugation reaction catalyzed by STs can increase the water solubility of these compounds, facilitating their excretion from the body.

STs can be classified into several families based on their sequence similarity and cofactor specificity. The largest family of STs is the cytosolic sulfotransferases, which use 3'-phosphoadenosine 5'-phosphosulfate (PAPS) as a cofactor to transfer the sulfo group to various acceptor molecules, including phenols, alcohols, amines, and steroids.

Abnormalities in ST activity have been implicated in several diseases, such as cancer, cardiovascular disease, and neurological disorders. Therefore, understanding the function and regulation of STs is essential for developing new therapeutic strategies to treat these conditions.

Cortisone is a type of corticosteroid hormone that is produced naturally in the body by the adrenal gland. It is released in response to stress and helps to regulate metabolism, reduce inflammation, and suppress the immune system. Cortisone can also be synthetically produced and is often used as a medication to treat a variety of conditions such as arthritis, asthma, and skin disorders. It works by mimicking the effects of the natural hormone in the body and reducing inflammation and suppressing the immune system. Cortisone can be administered through various routes, including oral, injectable, topical, and inhalational.

Steroid 17-alpha-hydroxylase, also known as CYP17A1, is a cytochrome P450 enzyme that plays a crucial role in steroid hormone biosynthesis. It is located in the endoplasmic reticulum of cells in the adrenal glands and gonads. This enzyme catalyzes the 17-alpha-hydroxylation and subsequent lyase cleavage of pregnenolone and progesterone, converting them into dehydroepiandrosterone (DHEA) and androstenedione, respectively. These steroid intermediates are essential for the biosynthesis of both glucocorticoids and sex steroids, including cortisol, aldosterone, estrogens, and testosterone.

Defects in the CYP17A1 gene can lead to several disorders, such as congenital adrenal hyperplasia (CAH) due to 17-alpha-hydroxylase deficiency, which is characterized by decreased production of cortisol and sex steroids and increased mineralocorticoid levels. This condition results in sexual infantilism, electrolyte imbalances, and hypertension.

Alcohol oxidoreductases are a class of enzymes that catalyze the oxidation of alcohols to aldehydes or ketones, while reducing nicotinamide adenine dinucleotide (NAD+) to NADH. These enzymes play an important role in the metabolism of alcohols and other organic compounds in living organisms.

The most well-known example of an alcohol oxidoreductase is alcohol dehydrogenase (ADH), which is responsible for the oxidation of ethanol to acetaldehyde in the liver during the metabolism of alcoholic beverages. Other examples include aldehyde dehydrogenases (ALDH) and sorbitol dehydrogenase (SDH).

These enzymes are important targets for the development of drugs used to treat alcohol use disorder, as inhibiting their activity can help to reduce the rate of ethanol metabolism and the severity of its effects on the body.

Steroids, also known as corticosteroids, are a type of hormone that the adrenal gland produces in your body. They have many functions, such as controlling the balance of salt and water in your body and helping to reduce inflammation. Steroids can also be synthetically produced and used as medications to treat a variety of conditions, including allergies, asthma, skin conditions, and autoimmune disorders.

Steroid medications are available in various forms, such as oral pills, injections, creams, and inhalers. They work by mimicking the effects of natural hormones produced by your body, reducing inflammation and suppressing the immune system's response to prevent or reduce symptoms. However, long-term use of steroids can have significant side effects, including weight gain, high blood pressure, osteoporosis, and increased risk of infections.

It is important to note that anabolic steroids are a different class of drugs that are sometimes abused for their muscle-building properties. These steroids are synthetic versions of the male hormone testosterone and can have serious health consequences when taken in large doses or without medical supervision.

NAD (Nicotinamide Adenine Dinucleotide) is a coenzyme found in all living cells. It plays an essential role in cellular metabolism, particularly in redox reactions, where it acts as an electron carrier. NAD exists in two forms: NAD+, which accepts electrons and becomes reduced to NADH. This pairing of NAD+/NADH is involved in many fundamental biological processes such as generating energy in the form of ATP during cellular respiration, and serving as a critical cofactor for various enzymes that regulate cellular functions like DNA repair, gene expression, and cell death.

Maintaining optimal levels of NAD+/NADH is crucial for overall health and longevity, as it declines with age and in certain disease states. Therefore, strategies to boost NAD+ levels are being actively researched for their potential therapeutic benefits in various conditions such as aging, neurodegenerative disorders, and metabolic diseases.

Hydrocortisone is a synthetic glucocorticoid, which is a class of steroid hormones. It is identical to the naturally occurring cortisol, a hormone produced by the adrenal gland that helps regulate metabolism and helps your body respond to stress. Hydrocortisone has anti-inflammatory effects and is used to treat various inflammatory conditions such as allergies, skin disorders, and autoimmune diseases. It works by suppressing the immune system's response to reduce swelling, redness, itching, and other symptoms caused by inflammation.

Hydrocortisone is available in different forms, including oral tablets, topical creams, lotions, gels, and ointments, as well as injectable solutions. The specific use and dosage depend on the condition being treated and the individual patient's medical history and current health status.

As with any medication, hydrocortisone can have side effects, especially when used in high doses or for extended periods. Common side effects include increased appetite, weight gain, mood changes, insomnia, and skin thinning. Long-term use of hydrocortisone may also increase the risk of developing osteoporosis, diabetes, cataracts, and other health problems. Therefore, it is essential to follow your healthcare provider's instructions carefully when using this medication.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

L-Lactate Dehydrogenase (LDH) is an enzyme found in various tissues within the body, including the heart, liver, kidneys, muscles, and brain. It plays a crucial role in the process of energy production, particularly during anaerobic conditions when oxygen levels are low.

In the presence of the coenzyme NADH, LDH catalyzes the conversion of pyruvate to lactate, generating NAD+ as a byproduct. Conversely, in the presence of NAD+, LDH can convert lactate back to pyruvate using NADH. This reversible reaction is essential for maintaining the balance between lactate and pyruvate levels within cells.

Elevated blood levels of LDH may indicate tissue damage or injury, as this enzyme can be released into the circulation following cellular breakdown. As a result, LDH is often used as a nonspecific biomarker for various medical conditions, such as myocardial infarction (heart attack), liver disease, muscle damage, and certain types of cancer. However, it's important to note that an isolated increase in LDH does not necessarily pinpoint the exact location or cause of tissue damage, and further diagnostic tests are usually required for confirmation.

Testosterone is a steroid hormone that belongs to androsten class of hormones. It is primarily secreted by the Leydig cells in the testes of males and, to a lesser extent, by the ovaries and adrenal glands in females. Testosterone is the main male sex hormone and anabolic steroid. It plays a key role in the development of masculine characteristics, such as body hair and muscle mass, and contributes to bone density, fat distribution, red cell production, and sex drive. In females, testosterone contributes to sexual desire and bone health. Testosterone is synthesized from cholesterol and its production is regulated by luteinizing hormone (LH) and follicle-stimulating hormone (FSH).

The liver is a large, solid organ located in the upper right portion of the abdomen, beneath the diaphragm and above the stomach. It plays a vital role in several bodily functions, including:

1. Metabolism: The liver helps to metabolize carbohydrates, fats, and proteins from the food we eat into energy and nutrients that our bodies can use.
2. Detoxification: The liver detoxifies harmful substances in the body by breaking them down into less toxic forms or excreting them through bile.
3. Synthesis: The liver synthesizes important proteins, such as albumin and clotting factors, that are necessary for proper bodily function.
4. Storage: The liver stores glucose, vitamins, and minerals that can be released when the body needs them.
5. Bile production: The liver produces bile, a digestive juice that helps to break down fats in the small intestine.
6. Immune function: The liver plays a role in the immune system by filtering out bacteria and other harmful substances from the blood.

Overall, the liver is an essential organ that plays a critical role in maintaining overall health and well-being.

Androsterone is a weak androgen and an endogenous steroid hormone. It's produced in the liver from dehydroepiandrosterone (DHEA) and is converted into androstenedione, another weak androgen. Androsterone is excreted in urine as a major metabolite of testosterone. It plays a role in male sexual development and function, although its effects are much weaker than those of testosterone. In clinical contexts, androsterone levels may be measured to help diagnose certain hormonal disorders or to monitor hormone therapy.

Alcohol dehydrogenase (ADH) is a group of enzymes responsible for catalyzing the oxidation of alcohols to aldehydes or ketones, and reducing equivalents such as NAD+ to NADH. In humans, ADH plays a crucial role in the metabolism of ethanol, converting it into acetaldehyde, which is then further metabolized by aldehyde dehydrogenase (ALDH) into acetate. This process helps to detoxify and eliminate ethanol from the body. Additionally, ADH enzymes are also involved in the metabolism of other alcohols, such as methanol and ethylene glycol, which can be toxic if allowed to accumulate in the body.

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is an enzyme that plays a crucial role in the metabolic pathway of glycolysis. Its primary function is to convert glyceraldehyde-3-phosphate (a triose sugar phosphate) into D-glycerate 1,3-bisphosphate, while also converting nicotinamide adenine dinucleotide (NAD+) into its reduced form NADH. This reaction is essential for the production of energy in the form of adenosine triphosphate (ATP) during cellular respiration. GAPDH has also been implicated in various non-metabolic processes, including DNA replication, repair, and transcription regulation, due to its ability to interact with different proteins and nucleic acids.

20-α-Hydroxysteroid Dehydrogenase (20-α-HSD) is an enzyme that catalyzes the conversion of steroids, specifically the oxidation of 20α-hydroxysteroids to 20-keto steroids. This enzyme plays a crucial role in the metabolism and regulation of steroid hormones, such as corticosteroids and progestogens.

In the adrenal gland, 20-α-HSD is involved in the biosynthesis and interconversion of various corticosteroids, including cortisol, cortisone, and aldosterone. By catalyzing the conversion of cortisol to cortisone or vice versa, this enzyme helps maintain a balance between active and inactive forms of these hormones, which is essential for proper physiological functioning.

In the reproductive system, 20-α-HSD is involved in the metabolism of progestogens, such as progesterone and its derivatives. This enzyme can convert active forms of progestogens into their inactive counterparts, thereby regulating their levels and activity within the body.

Dysregulation or mutations in 20-α-HSD have been implicated in several medical conditions, including adrenal insufficiency, congenital adrenal hyperplasia, and certain reproductive disorders.

Aldehyde dehydrogenase (ALDH) is a class of enzymes that play a crucial role in the metabolism of alcohol and other aldehydes in the body. These enzymes catalyze the oxidation of aldehydes to carboxylic acids, using nicotinamide adenine dinucleotide (NAD+) as a cofactor.

There are several isoforms of ALDH found in different tissues throughout the body, with varying substrate specificities and kinetic properties. The most well-known function of ALDH is its role in alcohol metabolism, where it converts the toxic aldehyde intermediate acetaldehyde to acetate, which can then be further metabolized or excreted.

Deficiencies in ALDH activity have been linked to a number of clinical conditions, including alcohol flush reaction, alcohol-induced liver disease, and certain types of cancer. Additionally, increased ALDH activity has been associated with chemotherapy resistance in some cancer cells.

Glutamate Dehydrogenase (GLDH or GDH) is a mitochondrial enzyme that plays a crucial role in the metabolism of amino acids, particularly within liver and kidney tissues. It catalyzes the reversible oxidative deamination of glutamate to alpha-ketoglutarate, which links amino acid metabolism with the citric acid cycle and energy production. This enzyme is significant in clinical settings as its levels in blood serum can be used as a diagnostic marker for diseases that damage liver or kidney cells, since these cells release GLDH into the bloodstream upon damage.

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), also known as Glucosephosphate Dehydrogenase, is an enzyme that plays a crucial role in cellular metabolism, particularly in the glycolytic pathway. It catalyzes the conversion of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (1,3-BPG), while also converting nicotinamide adenine dinucleotide (NAD+) to its reduced form NADH. This reaction is essential for the production of energy in the form of adenosine triphosphate (ATP) during cellular respiration. GAPDH has been widely used as a housekeeping gene in molecular biology research due to its consistent expression across various tissues and cells, although recent studies have shown that its expression can vary under certain conditions.

Malate Dehydrogenase (MDH) is an enzyme that plays a crucial role in the Krebs cycle, also known as the citric acid cycle or tricarboxylic acid (TCA) cycle. It catalyzes the reversible oxidation of malate to oxaloacetate, while simultaneously reducing NAD+ to NADH. This reaction is essential for energy production in the form of ATP and NADH within the cell.

There are two main types of Malate Dehydrogenase:

1. NAD-dependent Malate Dehydrogenase (MDH1): Found primarily in the cytoplasm, this isoform plays a role in the malate-aspartate shuttle, which helps transfer reducing equivalents between the cytoplasm and mitochondria.
2. FAD-dependent Malate Dehydrogenase (MDH2): Located within the mitochondrial matrix, this isoform is involved in the Krebs cycle for energy production.

Abnormal levels of Malate Dehydrogenase enzyme can be indicative of certain medical conditions or diseases, such as myocardial infarction (heart attack), muscle damage, or various types of cancer. Therefore, MDH enzyme activity is often assessed in diagnostic tests to help identify and monitor these health issues.

Isocitrate Dehydrogenase (IDH) is an enzyme that catalyzes the oxidative decarboxylation of isocitrate to α-ketoglutarate in the presence of NAD+ or NADP+, producing NADH or NADPH respectively. This reaction occurs in the citric acid cycle, also known as the Krebs cycle or tricarboxylic acid (TCA) cycle, which is a crucial metabolic pathway in the cell's energy production and biosynthesis of various molecules. There are three isoforms of IDH found in humans: IDH1 located in the cytosol, IDH2 in the mitochondrial matrix, and IDH3 within the mitochondria. Mutations in IDH1 and IDH2 have been associated with several types of cancer, such as gliomas and acute myeloid leukemia (AML), leading to abnormal accumulation of 2-hydroxyglutarate, which can contribute to tumorigenesis.

Phosphoadenosine phosphosulfate (PAPS) is not exactly a medical term, but a biochemical term. However, it is often referred to in the context of medical and biological research.

PAPS is a crucial molecule in the metabolism of living organisms and serves as the primary donor of sulfate groups in the process of sulfonation, which is a type of enzymatic modification that adds a sulfate group to various substrates such as proteoglycans, hormones, neurotransmitters, and xenobiotics. This process plays an essential role in several biological processes, including detoxification, signal transduction, and cell-cell recognition.

Therefore, PAPS is a critical molecule for maintaining proper physiological functions in the body, and its dysregulation has been implicated in various diseases, such as cancer, inflammation, and neurodevelopmental disorders.

Arylsulfotransferases (ASTs) are a group of enzymes that play a role in the detoxification of xenobiotics and endogenous compounds by catalyzing the transfer of a sulfuryl group from a donor, such as 3'-phosphoadenosine-5'-phosphosulfate (PAPS), to an acceptor aromatic molecule. This results in the formation of a sulfate ester, which can then be excreted from the body. ASTs are found in various tissues, including the liver, kidney, and intestine, and are involved in the metabolism of numerous drugs, hormones, and neurotransmitters. Defects in ASTs have been associated with certain genetic disorders, such as aromatic L-amino acid decarboxylase deficiency and disorders of steroid sulfation.

Ketosteroids are a type of steroid compound that contain a ketone functional group in their chemical structure. They are derived from cholesterol and are present in both animal and plant tissues. Some ketosteroids are produced endogenously, while others can be introduced exogenously through the diet or medication.

Endogenous ketosteroids include steroid hormones such as testosterone, estradiol, and cortisol, which contain a ketone group in their structure. Exogenous ketosteroids can be found in certain medications, such as those used to treat hormonal imbalances or inflammation.

Ketosteroids have been studied for their potential therapeutic uses, including as anti-inflammatory agents and for the treatment of hormone-related disorders. However, more research is needed to fully understand their mechanisms of action and potential benefits.

NADP (Nicotinamide Adenine Dinucleotide Phosphate) is a coenzyme that plays a crucial role as an electron carrier in various redox reactions in the human body. It exists in two forms: NADP+, which functions as an oxidizing agent and accepts electrons, and NADPH, which serves as a reducing agent and donates electrons.

NADPH is particularly important in anabolic processes, such as lipid and nucleotide synthesis, where it provides the necessary reducing equivalents to drive these reactions forward. It also plays a critical role in maintaining the cellular redox balance by participating in antioxidant defense mechanisms that neutralize harmful reactive oxygen species (ROS).

In addition, NADP is involved in various metabolic pathways, including the pentose phosphate pathway and the Calvin cycle in photosynthesis. Overall, NADP and its reduced form, NADPH, are essential molecules for maintaining proper cellular function and energy homeostasis.

Dihydrolipoamide dehydrogenase (DHLD) is an enzyme that plays a crucial role in several important metabolic pathways in the human body, including the citric acid cycle and the catabolism of certain amino acids. DHLD is a component of multi-enzyme complexes, such as the pyruvate dehydrogenase complex (PDC) and the alpha-ketoglutarate dehydrogenase complex (KGDC).

The primary function of DHLD is to catalyze the oxidation of dihydrolipoamide, a reduced form of lipoamide, back to its oxidized state (lipoamide) while simultaneously reducing NAD+ to NADH. This reaction is essential for the continued functioning of the PDC and KGDC, as dihydrolipoamide is a cofactor for these enzyme complexes.

Deficiencies in DHLD can lead to serious metabolic disorders, such as maple syrup urine disease (MSUD) and riboflavin-responsive multiple acyl-CoA dehydrogenase deficiency (RR-MADD). These conditions can result in neurological symptoms, developmental delays, and metabolic acidosis, among other complications. Treatment typically involves dietary modifications, supplementation with specific nutrients, and, in some cases, enzyme replacement therapy.

Carbohydrate dehydrogenases are a group of enzymes that catalyze the oxidation of carbohydrates, including sugars and sugar alcohols. These enzymes play a crucial role in cellular metabolism by helping to convert these molecules into forms that can be used for energy or as building blocks for other biological compounds.

During the oxidation process, carbohydrate dehydrogenases remove hydrogen atoms from the carbohydrate substrate and transfer them to an electron acceptor, such as NAD+ or FAD. This results in the formation of a ketone or aldehyde group on the carbohydrate molecule and the reduction of the electron acceptor to NADH or FADH2.

Carbohydrate dehydrogenases are classified into several subgroups based on their substrate specificity, cofactor requirements, and other factors. Some examples include glucose dehydrogenase, galactose dehydrogenase, and sorbitol dehydrogenase.

These enzymes have important applications in various fields, including biotechnology, medicine, and industry. For example, they can be used to detect or quantify specific carbohydrates in biological samples, or to produce valuable chemical compounds through the oxidation of renewable resources such as plant-derived sugars.

Succinate dehydrogenase (SDH) is an enzyme complex that plays a crucial role in the process of cellular respiration, specifically in the citric acid cycle (also known as the Krebs cycle) and the electron transport chain. It is located in the inner mitochondrial membrane of eukaryotic cells.

SDH catalyzes the oxidation of succinate to fumarate, converting it into a molecule of fadaquate in the process. During this reaction, two electrons are transferred from succinate to the FAD cofactor within the SDH enzyme complex, reducing it to FADH2. These electrons are then passed on to ubiquinone (CoQ), which is a mobile electron carrier in the electron transport chain, leading to the generation of ATP, the main energy currency of the cell.

SDH is also known as mitochondrial complex II because it is the second complex in the electron transport chain. Mutations in the genes encoding SDH subunits or associated proteins have been linked to various human diseases, including hereditary paragangliomas, pheochromocytomas, gastrointestinal stromal tumors (GISTs), and some forms of neurodegenerative disorders.

L-Iditol 2-Dehydrogenase is an enzyme that catalyzes the chemical reaction between L-iditol and NAD+ to produce L-sorbose and NADH + H+. This enzyme plays a role in the metabolism of sugars, specifically in the conversion of L-iditol to L-sorbose in various organisms, including bacteria and fungi. The reaction catalyzed by this enzyme is part of the polyol pathway, which is involved in the regulation of osmotic pressure and other cellular processes.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

Dehydroepiandrosterone (DHEA) is a steroid hormone produced by the adrenal glands. It serves as a precursor to other hormones, including androgens such as testosterone and estrogens such as estradiol. DHEA levels typically peak during early adulthood and then gradually decline with age.

DHEA has been studied for its potential effects on various health conditions, including aging, cognitive function, sexual dysfunction, and certain chronic diseases. However, the evidence supporting its use for these purposes is generally limited and inconclusive. As with any supplement or medication, it's important to consult with a healthcare provider before taking DHEA to ensure safety and effectiveness.

Glycerol-3-phosphate dehydrogenase (GPD) is an enzyme that plays a crucial role in the metabolism of glucose and lipids. It catalyzes the conversion of dihydroxyacetone phosphate (DHAP) to glycerol-3-phosphate (G3P), which is a key intermediate in the synthesis of triglycerides, phospholipids, and other glycerophospholipids.

There are two main forms of GPD: a cytoplasmic form (GPD1) and a mitochondrial form (GPD2). The cytoplasmic form is involved in the production of NADH, which is used in various metabolic processes, while the mitochondrial form is involved in the production of ATP, the main energy currency of the cell.

Deficiencies or mutations in GPD can lead to a variety of metabolic disorders, including glycerol kinase deficiency and congenital muscular dystrophy. Elevated levels of GPD have been observed in certain types of cancer, suggesting that it may play a role in tumor growth and progression.

Substrate specificity in the context of medical biochemistry and enzymology refers to the ability of an enzyme to selectively bind and catalyze a chemical reaction with a particular substrate (or a group of similar substrates) while discriminating against other molecules that are not substrates. This specificity arises from the three-dimensional structure of the enzyme, which has evolved to match the shape, charge distribution, and functional groups of its physiological substrate(s).

Substrate specificity is a fundamental property of enzymes that enables them to carry out highly selective chemical transformations in the complex cellular environment. The active site of an enzyme, where the catalysis takes place, has a unique conformation that complements the shape and charge distribution of its substrate(s). This ensures efficient recognition, binding, and conversion of the substrate into the desired product while minimizing unwanted side reactions with other molecules.

Substrate specificity can be categorized as:

1. Absolute specificity: An enzyme that can only act on a single substrate or a very narrow group of structurally related substrates, showing no activity towards any other molecule.
2. Group specificity: An enzyme that prefers to act on a particular functional group or class of compounds but can still accommodate minor structural variations within the substrate.
3. Broad or promiscuous specificity: An enzyme that can act on a wide range of structurally diverse substrates, albeit with varying catalytic efficiencies.

Understanding substrate specificity is crucial for elucidating enzymatic mechanisms, designing drugs that target specific enzymes or pathways, and developing biotechnological applications that rely on the controlled manipulation of enzyme activities.

Glucose 1-Dehydrogenase (G1DH) is an enzyme that catalyzes the oxidation of β-D-glucose into D-glucono-1,5-lactone and reduces the cofactor NAD+ into NADH. This reaction plays a role in various biological processes, including glucose sensing and detoxification of reactive carbonyl species. G1DH is found in many organisms, including humans, and has several isoforms with different properties and functions.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.

The Ketoglutarate Dehydrogenase Complex (KGDC or α-KGDH) is a multi-enzyme complex that plays a crucial role in the Krebs cycle, also known as the citric acid cycle. It is located within the mitochondrial matrix of eukaryotic cells and functions to catalyze the oxidative decarboxylation of α-ketoglutarate into succinyl-CoA, thereby connecting the Krebs cycle to the electron transport chain for energy production.

The KGDC is composed of three distinct enzymes:

1. α-Ketoglutarate dehydrogenase (E1): This enzyme catalyzes the decarboxylation and oxidation of α-ketoglutarate to form a thioester intermediate with lipoamide, which is bound to the E2 component.
2. Dihydrolipoyl succinyltransferase (E2): This enzyme facilitates the transfer of the acetyl group from the lipoamide cofactor to CoA, forming succinyl-CoA and regenerating oxidized lipoamide.
3. Dihydrolipoyl dehydrogenase (E3): The final enzyme in the complex catalyzes the reoxidation of reduced lipoamide back to its disulfide form, using FAD as a cofactor and transferring electrons to NAD+, forming NADH.

The KGDC is subject to regulation by several mechanisms, including phosphorylation-dephosphorylation reactions that can inhibit or activate the complex, respectively. Dysfunction of this enzyme complex has been implicated in various diseases, such as neurodegenerative disorders and cancer.

Aldehyde oxidoreductases are a class of enzymes that catalyze the oxidation of aldehydes to carboxylic acids using NAD+ or FAD as cofactors. They play a crucial role in the detoxification of aldehydes generated from various metabolic processes, such as lipid peroxidation and alcohol metabolism. These enzymes are widely distributed in nature and have been identified in bacteria, yeast, plants, and animals.

The oxidation reaction catalyzed by aldehyde oxidoreductases involves the transfer of electrons from the aldehyde substrate to the cofactor, resulting in the formation of a carboxylic acid and reduced NAD+ or FAD. The enzymes are classified into several families based on their sequence similarity and cofactor specificity.

One of the most well-known members of this family is alcohol dehydrogenase (ADH), which catalyzes the oxidation of alcohols to aldehydes or ketones as part of the alcohol metabolism pathway. Another important member is aldehyde dehydrogenase (ALDH), which further oxidizes the aldehydes generated by ADH to carboxylic acids, thereby preventing the accumulation of toxic aldehydes in the body.

Deficiencies in ALDH enzymes have been linked to several human diseases, including alcoholism and certain types of cancer. Therefore, understanding the structure and function of aldehyde oxidoreductases is essential for developing new therapeutic strategies to treat these conditions.

Isoenzymes, also known as isoforms, are multiple forms of an enzyme that catalyze the same chemical reaction but differ in their amino acid sequence, structure, and/or kinetic properties. They are encoded by different genes or alternative splicing of the same gene. Isoenzymes can be found in various tissues and organs, and they play a crucial role in biological processes such as metabolism, detoxification, and cell signaling. Measurement of isoenzyme levels in body fluids (such as blood) can provide valuable diagnostic information for certain medical conditions, including tissue damage, inflammation, and various diseases.

Stereoisomerism is a type of isomerism (structural arrangement of atoms) in which molecules have the same molecular formula and sequence of bonded atoms, but differ in the three-dimensional orientation of their atoms in space. This occurs when the molecule contains asymmetric carbon atoms or other rigid structures that prevent free rotation, leading to distinct spatial arrangements of groups of atoms around a central point. Stereoisomers can have different chemical and physical properties, such as optical activity, boiling points, and reactivities, due to differences in their shape and the way they interact with other molecules.

There are two main types of stereoisomerism: enantiomers (mirror-image isomers) and diastereomers (non-mirror-image isomers). Enantiomers are pairs of stereoisomers that are mirror images of each other, but cannot be superimposed on one another. Diastereomers, on the other hand, are non-mirror-image stereoisomers that have different physical and chemical properties.

Stereoisomerism is an important concept in chemistry and biology, as it can affect the biological activity of molecules, such as drugs and natural products. For example, some enantiomers of a drug may be active, while others are inactive or even toxic. Therefore, understanding stereoisomerism is crucial for designing and synthesizing effective and safe drugs.

Gene expression regulation, enzymologic refers to the biochemical processes and mechanisms that control the transcription and translation of specific genes into functional proteins or enzymes. This regulation is achieved through various enzymatic activities that can either activate or repress gene expression at different levels, such as chromatin remodeling, transcription factor activation, mRNA processing, and protein degradation.

Enzymologic regulation of gene expression involves the action of specific enzymes that catalyze chemical reactions involved in these processes. For example, histone-modifying enzymes can alter the structure of chromatin to make genes more or less accessible for transcription, while RNA polymerase and its associated factors are responsible for transcribing DNA into mRNA. Additionally, various enzymes are involved in post-transcriptional modifications of mRNA, such as splicing, capping, and tailing, which can affect the stability and translation of the transcript.

Overall, the enzymologic regulation of gene expression is a complex and dynamic process that allows cells to respond to changes in their environment and maintain proper physiological function.

Glucose dehydrogenases (GDHs) are a group of enzymes that catalyze the oxidation of glucose to generate gluconic acid or glucuronic acid. This reaction involves the transfer of electrons from glucose to an electron acceptor, most commonly nicotinamide adenine dinucleotide (NAD+) or phenazine methosulfate (PMS).

GDHs are widely distributed in nature and can be found in various organisms, including bacteria, fungi, plants, and animals. They play important roles in different biological processes, such as glucose metabolism, energy production, and detoxification of harmful substances. Based on their cofactor specificity, GDHs can be classified into two main types: NAD(P)-dependent GDHs and PQQ-dependent GDHs.

NAD(P)-dependent GDHs use NAD+ or NADP+ as a cofactor to oxidize glucose to glucono-1,5-lactone, which is then hydrolyzed to gluconic acid by an accompanying enzyme. These GDHs are involved in various metabolic pathways, such as the Entner-Doudoroff pathway and the oxidative pentose phosphate pathway.

PQQ-dependent GDHs, on the other hand, use pyrroloquinoline quinone (PQQ) as a cofactor to catalyze the oxidation of glucose to gluconic acid directly. These GDHs are typically found in bacteria and play a role in energy production and detoxification.

Overall, glucose dehydrogenases are essential enzymes that contribute to the maintenance of glucose homeostasis and energy balance in living organisms.

Phosphogluconate dehydrogenase (PGD) is an enzyme that plays a crucial role in the pentose phosphate pathway, which is a metabolic pathway that supplies reducing energy to cells by converting glucose into ribose-5-phosphate and NADPH.

PGD catalyzes the third step of this pathway, in which 6-phosphogluconate is converted into ribulose-5-phosphate, with the concurrent reduction of NADP+ to NADPH. This reaction is essential for the generation of NADPH, which serves as a reducing agent in various cellular processes, including fatty acid synthesis and antioxidant defense.

Deficiencies in PGD can lead to several metabolic disorders, such as congenital nonspherocytic hemolytic anemia, which is characterized by the premature destruction of red blood cells due to a defect in the pentose phosphate pathway.

Sugar alcohol dehydrogenases (SADHs) are a group of enzymes that catalyze the interconversion between sugar alcohols and sugars, which involves the gain or loss of a pair of electrons, typically in the form of NAD(P)+/NAD(P)H. These enzymes play a crucial role in the metabolism of sugar alcohols, which are commonly found in various plants and some microorganisms.

Sugar alcohols, also known as polyols, are reduced forms of sugars that contain one or more hydroxyl groups instead of aldehyde or ketone groups. Examples of sugar alcohols include sorbitol, mannitol, xylitol, and erythritol. SADHs can interconvert these sugar alcohols to their corresponding sugars through a redox reaction that involves the transfer of hydrogen atoms.

The reaction catalyzed by SADHs is typically represented as follows:

R-CH(OH)-CH2OH + NAD(P)+ ↔ R-CO-CH2OH + NAD(P)H + H+

where R represents a carbon chain, and CH(OH)-CH2OH and CO-CH2OH represent the sugar alcohol and sugar forms, respectively.

SADHs are widely distributed in nature and have been found in various organisms, including bacteria, fungi, plants, and animals. These enzymes have attracted significant interest in biotechnology due to their potential applications in the production of sugar alcohols and other value-added products. Additionally, SADHs have been studied as targets for developing novel antimicrobial agents, as inhibiting these enzymes can disrupt the metabolism of certain pathogens that rely on sugar alcohols for growth and survival.

Acyl-CoA dehydrogenases are a group of enzymes that play a crucial role in the body's energy production process. They are responsible for catalyzing the oxidation of various fatty acids, which are broken down into smaller molecules called acyl-CoAs in the body.

More specifically, acyl-CoA dehydrogenases facilitate the removal of electrons from the acyl-CoA molecules, which are then transferred to coenzyme Q10 and eventually to the electron transport chain. This process generates energy in the form of ATP, which is used by cells throughout the body for various functions.

There are several different types of acyl-CoA dehydrogenases, each responsible for oxidizing a specific type of acyl-CoA molecule. These include:

* Very long-chain acyl-CoA dehydrogenase (VLCAD), which oxidizes acyl-CoAs with 12 to 20 carbon atoms
* Long-chain acyl-CoA dehydrogenase (LCAD), which oxidizes acyl-CoAs with 14 to 20 carbon atoms
* Medium-chain acyl-CoA dehydrogenase (MCAD), which oxidizes acyl-CoAs with 6 to 12 carbon atoms
* Short-chain acyl-CoA dehydrogenase (SCAD), which oxidizes acyl-CoAs with 4 to 8 carbon atoms
* Isovaleryl-CoA dehydrogenase, which oxidizes isovaleryl-CoA, a specific type of branched-chain acyl-CoA molecule

Deficiencies in these enzymes can lead to various metabolic disorders, such as medium-chain acyl-CoA dehydrogenase deficiency (MCADD) or long-chain acyl-CoA dehydrogenase deficiency (LCADD), which can cause symptoms such as hypoglycemia, muscle weakness, and developmental delays.

NADH dehydrogenase, also known as Complex I, is an enzyme complex in the electron transport chain located in the inner mitochondrial membrane. It catalyzes the oxidation of NADH to NAD+ and the reduction of coenzyme Q to ubiquinol, playing a crucial role in cellular respiration and energy production. The reaction involves the transfer of electrons from NADH to coenzyme Q, which contributes to the generation of a proton gradient across the membrane, ultimately leading to ATP synthesis. Defects in NADH dehydrogenase can result in various mitochondrial diseases and disorders.

Inosine Monophosphate Dehydrogenase (IMDH or IMPDH) is an enzyme that is involved in the de novo biosynthesis of guanine nucleotides. It catalyzes the conversion of inosine monophosphate (IMP) to xanthosine monophosphate (XMP), which is the rate-limiting step in the synthesis of guanosine triphosphate (GTP).

There are two isoforms of IMPDH, type I and type II, which are encoded by separate genes. Type I IMPDH is expressed in most tissues, while type II IMPDH is primarily expressed in lymphocytes and other cells involved in the immune response. Inhibitors of IMPDH have been developed as immunosuppressive drugs to prevent rejection of transplanted organs. Defects in the gene encoding IMPDH type II have been associated with retinal degeneration and hearing loss.

Lactate dehydrogenases (LDH) are a group of intracellular enzymes found in nearly all human cells, particularly in the heart, liver, kidneys, muscles, and brain. They play a crucial role in energy production during anaerobic metabolism, converting pyruvate to lactate while regenerating NAD+ from NADH. LDH exists as multiple isoenzymes (LDH-1 to LDH-5) in the body, each with distinct distributions and functions.

An elevated level of LDH in the blood may indicate tissue damage or injury, as these enzymes are released into the circulation following cellular destruction. Therefore, measuring LDH levels is a common diagnostic tool to assess various medical conditions, such as myocardial infarction (heart attack), liver disease, muscle damage, and some types of cancer. However, an isolated increase in LDH may not be specific enough for a definitive diagnosis, and additional tests are usually required for confirmation.

Acyl-CoA dehydrogenase is a group of enzymes that play a crucial role in the body's energy production process. Specifically, they are involved in the breakdown of fatty acids within the cells.

More technically, acyl-CoA dehydrogenases catalyze the removal of electrons from the thiol group of acyl-CoAs, forming a trans-double bond and generating FADH2. This reaction is the first step in each cycle of fatty acid beta-oxidation, which occurs in the mitochondria of cells.

There are several different types of acyl-CoA dehydrogenases, each specific to breaking down different lengths of fatty acids. For example, very long-chain acyl-CoA dehydrogenase (VLCAD) is responsible for breaking down longer chain fatty acids, while medium-chain acyl-CoA dehydrogenase (MCAD) breaks down medium-length chains.

Deficiencies in these enzymes can lead to various metabolic disorders, such as MCAD deficiency or LC-FAOD (long-chain fatty acid oxidation disorders), which can cause symptoms like vomiting, lethargy, and muscle weakness, especially during periods of fasting or illness.

Formate dehydrogenases (FDH) are a group of enzymes that catalyze the oxidation of formic acid (formate) to carbon dioxide and hydrogen or to carbon dioxide and water, depending on the type of FDH. The reaction is as follows:

Formic acid + Coenzyme Q (or NAD+) -> Carbon dioxide + H2 (or H2O) + Reduced coenzyme Q (or NADH)

FDHs are widely distributed in nature and can be found in various organisms, including bacteria, archaea, and eukaryotes. They play a crucial role in the metabolism of many microorganisms that use formate as an electron donor for energy conservation or as a carbon source for growth. In addition to their biological significance, FDHs have attracted much interest as biocatalysts for various industrial applications, such as the production of hydrogen, reduction of CO2, and detoxification of formic acid in animal feed.

FDHs can be classified into two main types based on their cofactor specificity: NAD-dependent FDHs and quinone-dependent FDHs. NAD-dependent FDHs use nicotinamide adenine dinucleotide (NAD+) as a cofactor, while quinone-dependent FDHs use menaquinone or ubiquinone as a cofactor. Both types of FDHs have a similar reaction mechanism that involves the transfer of a hydride ion from formate to the cofactor and the release of carbon dioxide.

FDHs are composed of two subunits: a small subunit containing one or two [4Fe-4S] clusters and a large subunit containing a molybdenum cofactor (Moco) and one or two [2Fe-2S] clusters. Moco is a complex prosthetic group that consists of a pterin ring, a dithiolene group, and a molybdenum atom coordinated to three ligands: a sulfur atom from the dithiolene group, a terminal oxygen atom from a mononucleotide, and a serine residue. The molybdenum center can adopt different oxidation states (+4, +5, or +6) during the catalytic cycle, allowing for the transfer of electrons and the activation of formate.

FDHs have various applications in biotechnology and industry, such as the production of hydrogen gas, the removal of nitrate from wastewater, and the synthesis of fine chemicals. The high selectivity and efficiency of FDHs make them attractive catalysts for these processes, which require mild reaction conditions and low energy inputs. However, the stability and activity of FDHs are often limited by their sensitivity to oxygen and other inhibitors, which can affect their performance in industrial settings. Therefore, efforts have been made to improve the properties of FDHs through protein engineering, genetic modification, and immobilization techniques.

Xanthine dehydrogenase (XDH) is an enzyme involved in the metabolism of purines, which are nitrogen-containing compounds that form part of DNA and RNA. Specifically, XDH helps to break down xanthine and hypoxanthine into uric acid, a waste product that is excreted in the urine.

XDH can exist in two interconvertible forms: a dehydrogenase form (XDH) and an oxidase form (XO). In its dehydrogenase form, XDH uses NAD+ as an electron acceptor to convert xanthine into uric acid. However, when XDH is converted to its oxidase form (XO), it can use molecular oxygen as an electron acceptor instead, producing superoxide and hydrogen peroxide as byproducts. These reactive oxygen species can contribute to oxidative stress and tissue damage in the body.

Abnormal levels or activity of XDH have been implicated in various diseases, including gout, cardiovascular disease, and neurodegenerative disorders.

Alpha 1-antitrypsin (AAT, or α1-antiproteinase, A1AP) is a protein that is primarily produced by the liver and released into the bloodstream. It belongs to a group of proteins called serine protease inhibitors, which help regulate inflammation and protect tissues from damage caused by enzymes involved in the immune response.

Alpha 1-antitrypsin is particularly important for protecting the lungs from damage caused by neutrophil elastase, an enzyme released by white blood cells called neutrophils during inflammation. In the lungs, AAT binds to and inhibits neutrophil elastase, preventing it from degrading the extracellular matrix and damaging lung tissue.

Deficiency in alpha 1-antitrypsin can lead to chronic obstructive pulmonary disease (COPD) and liver disease. The most common cause of AAT deficiency is a genetic mutation that results in abnormal folding and accumulation of the protein within liver cells, leading to reduced levels of functional AAT in the bloodstream. This condition is called alpha 1-antitrypsin deficiency (AATD) and can be inherited in an autosomal codominant manner. Individuals with severe AATD may require augmentation therapy with intravenous infusions of purified human AAT to help prevent lung damage.

Succinic semialdehyde dehydrogenase, also known as hydroxybutyrate dehydrogenase (EC 1.2.1.16), is an enzyme involved in the metabolism of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA). This enzyme catalyzes the oxidation of succinic semialdehyde to succinate, which is a key step in the GABA degradation pathway.

Deficiency in this enzyme can lead to an accumulation of succinic semialdehyde and its downstream metabolite, gamma-hydroxybutyric acid (GHB), resulting in neurological symptoms such as developmental delay, hypotonia, seizures, and movement disorders. GHB is a naturally occurring neurotransmitter and also a recreational drug known as "Grievous Bodily Harm" or "Liquid Ecstasy."

The gene that encodes for succinic semialdehyde dehydrogenase is located on chromosome 6 (6p22.3) and has been identified as ALDH5A1. Mutations in this gene can lead to succinic semialdehyde dehydrogenase deficiency, which is an autosomal recessive disorder.

Recombinant proteins are artificially created proteins produced through the use of recombinant DNA technology. This process involves combining DNA molecules from different sources to create a new set of genes that encode for a specific protein. The resulting recombinant protein can then be expressed, purified, and used for various applications in research, medicine, and industry.

Recombinant proteins are widely used in biomedical research to study protein function, structure, and interactions. They are also used in the development of diagnostic tests, vaccines, and therapeutic drugs. For example, recombinant insulin is a common treatment for diabetes, while recombinant human growth hormone is used to treat growth disorders.

The production of recombinant proteins typically involves the use of host cells, such as bacteria, yeast, or mammalian cells, which are engineered to express the desired protein. The host cells are transformed with a plasmid vector containing the gene of interest, along with regulatory elements that control its expression. Once the host cells are cultured and the protein is expressed, it can be purified using various chromatography techniques.

Overall, recombinant proteins have revolutionized many areas of biology and medicine, enabling researchers to study and manipulate proteins in ways that were previously impossible.

3-Hydroxyacyl CoA Dehydrogenases (3-HADs) are a group of enzymes that play a crucial role in the beta-oxidation of fatty acids. These enzymes catalyze the third step of the beta-oxidation process, which involves the oxidation of 3-hydroxyacyl CoA to 3-ketoacyl CoA. This reaction is an essential part of the energy-generating process that occurs in the mitochondria of cells and allows for the breakdown of fatty acids into smaller molecules, which can then be used to produce ATP, the primary source of cellular energy.

There are several different isoforms of 3-HADs, each with specific substrate preferences and tissue distributions. The most well-known isoform is the mitochondrial 3-hydroxyacyl CoA dehydrogenase (M3HD), which is involved in the oxidation of medium and long-chain fatty acids. Other isoforms include the short-chain 3-hydroxyacyl CoA dehydrogenase (SCHAD) and the long-chain 3-hydroxyacyl CoA dehydrogenase (LCHAD), which are involved in the oxidation of shorter and longer chain fatty acids, respectively.

Deficiencies in 3-HADs can lead to serious metabolic disorders, such as 3-hydroxyacyl-CoA dehydrogenase deficiency (3-HAD deficiency), which is characterized by the accumulation of toxic levels of 3-hydroxyacyl CoAs in the body. Symptoms of this disorder can include hypoglycemia, muscle weakness, cardiomyopathy, and developmental delays. Early diagnosis and treatment of 3-HAD deficiency are essential to prevent serious complications and improve outcomes for affected individuals.

Ketone oxidoreductases are a group of enzymes that catalyze the conversion of ketones to corresponding alcohols or vice versa, through the process of reduction or oxidation. These enzymes play an essential role in various metabolic pathways and biochemical reactions within living organisms.

In the context of medical research and diagnostics, ketone oxidoreductases have gained attention for their potential applications in the development of biosensors to detect and monitor blood ketone levels, particularly in patients with diabetes. Elevated levels of ketones in the blood (known as ketonemia) can indicate a serious complication called diabetic ketoacidosis, which requires prompt medical attention.

One example of a ketone oxidoreductase is the enzyme known as d-beta-hydroxybutyrate dehydrogenase (d-BDH), which catalyzes the conversion of d-beta-hydroxybutyrate to acetoacetate. This reaction is part of the metabolic pathway that breaks down fatty acids for energy production, and it becomes particularly important during periods of low carbohydrate availability or insulin deficiency, as seen in diabetes.

Understanding the function and regulation of ketone oxidoreductases can provide valuable insights into the pathophysiology of metabolic disorders like diabetes and contribute to the development of novel therapeutic strategies for their management.

Oxidoreductases are a class of enzymes that catalyze oxidation-reduction reactions, which involve the transfer of electrons from one molecule (the reductant) to another (the oxidant). These enzymes play a crucial role in various biological processes, including energy production, metabolism, and detoxification.

The oxidoreductase-catalyzed reaction typically involves the donation of electrons from a reducing agent (donor) to an oxidizing agent (acceptor), often through the transfer of hydrogen atoms or hydride ions. The enzyme itself does not undergo any permanent chemical change during this process, but rather acts as a catalyst to lower the activation energy required for the reaction to occur.

Oxidoreductases are classified and named based on the type of electron donor or acceptor involved in the reaction. For example, oxidoreductases that act on the CH-OH group of donors are called dehydrogenases, while those that act on the aldehyde or ketone groups are called oxidases. Other examples include reductases, peroxidases, and catalases.

Understanding the function and regulation of oxidoreductases is important for understanding various physiological processes and developing therapeutic strategies for diseases associated with impaired redox homeostasis, such as cancer, neurodegenerative disorders, and cardiovascular disease.

Messenger RNA (mRNA) is a type of RNA (ribonucleic acid) that carries genetic information copied from DNA in the form of a series of three-base code "words," each of which specifies a particular amino acid. This information is used by the cell's machinery to construct proteins, a process known as translation. After being transcribed from DNA, mRNA travels out of the nucleus to the ribosomes in the cytoplasm where protein synthesis occurs. Once the protein has been synthesized, the mRNA may be degraded and recycled. Post-transcriptional modifications can also occur to mRNA, such as alternative splicing and addition of a 5' cap and a poly(A) tail, which can affect its stability, localization, and translation efficiency.

Catalysis is the process of increasing the rate of a chemical reaction by adding a substance known as a catalyst, which remains unchanged at the end of the reaction. A catalyst lowers the activation energy required for the reaction to occur, thereby allowing the reaction to proceed more quickly and efficiently. This can be particularly important in biological systems, where enzymes act as catalysts to speed up metabolic reactions that are essential for life.

In the context of medicine and biology, sulfates are ions or compounds that contain the sulfate group (SO4−2). Sulfate is a polyatomic anion with the structure of a sphere. It consists of a central sulfur atom surrounded by four oxygen atoms in a tetrahedral arrangement.

Sulfates can be found in various biological molecules, such as glycosaminoglycans and proteoglycans, which are important components of connective tissue and the extracellular matrix. Sulfate groups play a crucial role in these molecules by providing negative charges that help maintain the structural integrity and hydration of tissues.

In addition to their biological roles, sulfates can also be found in various medications and pharmaceutical compounds. For example, some laxatives contain sulfate salts, such as magnesium sulfate (Epsom salt) or sodium sulfate, which work by increasing the water content in the intestines and promoting bowel movements.

It is important to note that exposure to high levels of sulfates can be harmful to human health, particularly in the form of sulfur dioxide (SO2), a common air pollutant produced by burning fossil fuels. Prolonged exposure to SO2 can cause respiratory problems and exacerbate existing lung conditions.

Uridine Diphosphate (UDP) Glucose Dehydrogenase is an enzyme that plays a role in carbohydrate metabolism. Its systematic name is UDP-glucose:NAD+ oxidoreductase, and it catalyzes the following chemical reaction:

UDP-glucose + NAD+ -> UDP-glucuronate + NADH + H+

This enzyme helps convert UDP-glucose into UDP-glucuronate, which is a crucial component in the biosynthesis of various substances in the body, such as glycosaminoglycans and other glyconjugates. The reaction also results in the reduction of NAD+ to NADH, which is an essential coenzyme in numerous metabolic processes.

UDP-glucose dehydrogenase is widely distributed in various tissues, including the liver, kidney, and intestine. Deficiencies or mutations in this enzyme can lead to several metabolic disorders, such as glucosuria and hypermethioninemia.

Cytosol refers to the liquid portion of the cytoplasm found within a eukaryotic cell, excluding the organelles and structures suspended in it. It is the site of various metabolic activities and contains a variety of ions, small molecules, and enzymes. The cytosol is where many biochemical reactions take place, including glycolysis, protein synthesis, and the regulation of cellular pH. It is also where some organelles, such as ribosomes and vesicles, are located. In contrast to the cytosol, the term "cytoplasm" refers to the entire contents of a cell, including both the cytosol and the organelles suspended within it.

Glucose-6-Phosphate Dehydrogenase (G6PD) deficiency is a genetic disorder that affects the normal functioning of an enzyme called G6PD. This enzyme is found in red blood cells and plays a crucial role in protecting them from damage.

In people with G6PD deficiency, the enzyme's activity is reduced or absent, making their red blood cells more susceptible to damage and destruction, particularly when they are exposed to certain triggers such as certain medications, infections, or foods. This can lead to a condition called hemolysis, where the red blood cells break down prematurely, leading to anemia, jaundice, and in severe cases, kidney failure.

G6PD deficiency is typically inherited from one's parents in an X-linked recessive pattern, meaning that males are more likely to be affected than females. While there is no cure for G6PD deficiency, avoiding triggers and managing symptoms can help prevent complications.

The placenta is an organ that develops in the uterus during pregnancy and provides oxygen and nutrients to the growing baby through the umbilical cord. It also removes waste products from the baby's blood. The placenta attaches to the wall of the uterus, and the baby's side of the placenta contains many tiny blood vessels that connect to the baby's circulatory system. This allows for the exchange of oxygen, nutrients, and waste between the mother's and baby's blood. After the baby is born, the placenta is usually expelled from the uterus in a process called afterbirth.

Adrenergic receptors are a type of G protein-coupled receptor that bind and respond to catecholamines, such as epinephrine (adrenaline) and norepinephrine (noradrenaline). Alpha adrenergic receptors (α-ARs) are a subtype of adrenergic receptors that are classified into two main categories: α1-ARs and α2-ARs.

The activation of α1-ARs leads to the activation of phospholipase C, which results in an increase in intracellular calcium levels and the activation of various signaling pathways that mediate diverse physiological responses such as vasoconstriction, smooth muscle contraction, and cell proliferation.

On the other hand, α2-ARs are primarily located on presynaptic nerve terminals where they function to inhibit the release of neurotransmitters, including norepinephrine. The activation of α2-ARs also leads to the inhibition of adenylyl cyclase and a decrease in intracellular cAMP levels, which can mediate various physiological responses such as sedation, analgesia, and hypotension.

Overall, α-ARs play important roles in regulating various physiological functions, including cardiovascular function, mood, and cognition, and are also involved in the pathophysiology of several diseases, such as hypertension, heart failure, and neurodegenerative disorders.

20alpha-dihydroxypregn-4-en-3-one, NAD+, and NADP+, whereas its 4 products are 17-alpha-hydroxyprogesterone, NADH, NADPH, and ... Other names in common use include 20alpha-hydroxy steroid dehydrogenase, 20alpha-hydroxy steroid dehydrogenase, 20alpha-HSD, ... "Expression of 17beta-hydroxysteroid dehydrogenase type 1 and type 2, P450 aromatase, and 20alpha-hydroxysteroid dehydrogenase ... Hershkovitz L, Beuschlein F, Klammer S, Krup M, Weinstein Y (March 2007). "Adrenal 20alpha-hydroxysteroid dehydrogenase in the ...
... hydroxysteroid dehydrogenase (EC 1.1.1.210) is an enzyme that catalyzes the chemical reaction 5α-androstan-3β,17β-diol + NADP+ ... H+ This enzyme possesses the combined activities of the 3-β-hydroxysteroid dehydrogenase/Δ-5-4 isomerase and 20-α- ... hydroxysteroid dehydrogenase enzymes. Sharaf MA, Sweet F (September 1982). "Dual activity at an enzyme active site: 3 beta,20 ... alpha-hydroxysteroid oxidoreductase from fetal blood". Biochemistry. 21 (19): 4615-20. doi:10.1021/bi00262a016. PMID 6958329. ...
3-alpha)-hydroxysteroid dehydrogenase)". National Center for Biotechnology Information, U.S. National Library of Medicine. This ... 3α-hydroxysteroid dehydrogenase type 3, and dihydrodiol dehydrogenase type 2, is an enzyme that in humans is encoded by the ... This enzyme binds bile acid with high affinity, and shows minimal 3α-hydroxysteroid dehydrogenase activity. This gene shares ... "Entrez Gene: AKR1C2 aldo-keto reductase family 1, member C2 (dihydrodiol dehydrogenase 1; 20-alpha ( ...
RAG1 Alpha-2-plasmin inhibitor deficiency; 262850; PLI Alpha-ketoglutarate dehydrogenase deficiency; 203740; OGDH Alpha- ... CYP17A1 17-beta-hydroxysteroid dehydrogenase X deficiency; 300438; HSD17B10 2-methylbutyrylglycinuria; 610006; ACADSB 3- ... PC Pyruvate dehydrogenase deficiency; 312170; PDHA1 Pyruvate dehydrogenase E2 deficiency; 245348; DLAT Pyruvate dehydrogenase ... SCARB2 Acyl-CoA dehydrogenase, long chain, deficiency of; 201460; ACADL Acyl-CoA dehydrogenase, medium chain, deficiency of; ...
3-alpha hydroxysteroid dehydrogenase, type I; dihydrodiol dehydrogenase 4)". Rizner TL, Lin HK, Peehl DM, Steckelbroeck S, ... "Close kinship of human 20alpha-hydroxysteroid dehydrogenase gene with three aldo-keto reductase genes". Genes to Cells. 5 (2): ... Khanna M, Qin KN, Cheng KC (June 1995). "Distribution of 3 alpha-hydroxysteroid dehydrogenase in rat brain and molecular ... Steroidogenic enzyme 3α-hydroxysteroid dehydrogenase type 3 3β-Hydroxysteroid dehydrogenase GRCh38: Ensembl release 89: ...
Khanna M, Qin KN, Cheng KC (Jun 1995). "Distribution of 3 alpha-hydroxysteroid dehydrogenase in rat brain and molecular cloning ... "Close kinship of human 20alpha-hydroxysteroid dehydrogenase gene with three aldo-keto reductase genes". Genes to Cells. 5 (2): ... Bennett MJ, Schlegel BP, Jez JM, Penning TM, Lewis M (Aug 1996). "Structure of 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase ... "Entrez Gene: AKR1C3 aldo-keto reductase family 1, member C3 (3-alpha hydroxysteroid dehydrogenase, type II)". Theisen, J. ...
Hastings C, Hansson V (August 1981). "Kinetic properties of the soluble 3 alpha-hydroxysteroid dehydrogenase from rat testis ... Ellsworth, K.; Harris, G. (1995). "Expression of the type 1 and 2 steroid 5 alpha-reductases in human fetal tissues". Biochem ... delta 4-3-ketosteroid 5 alpha-oxidoreductase of rat prostate". J Biol Chem. 246 (8): 2584-93. doi:10.1016/S0021-9258(18)62328-2 ... 5α-Pregnan-17α-ol-3,20-dione (17‐OH-DHP) is a progestogen, i.e., it binds to the progesterone receptors. However, 17‐OH-DHP is ...
"Mechanism of inhibition of 3 alpha, 20 beta-hydroxysteroid dehydrogenase by a licorice-derived steroidal inhibitor". Structure ... Glucose/ribitol dehydrogenase InterPro: IPR002347 Insect alcohol dehydrogenase family InterPro: IPR002424 2,3-dihydro-2,3- ... alcohol dehydrogenases. Most members of this family are proteins of about 250 to 300 amino acid residues. Most dehydrogenases ... The short-chain dehydrogenases/reductases family (SDR) is a very large family of enzymes, most of which are known to be NAD- or ...
... alpha-hydroxysteroid dehydrogenase for neurosteroids and its inhibition by benzodiazepines" (pdf). Biological & Pharmaceutical ... while 3β-hydroxysteroid dehydrogenase and hydroxysteroid sulfotransferases are involved in excitatory neurosteroid production. ... 5α-reductase type I and 3α-hydroxysteroid dehydrogenase are involved in the biosynthesis of inhibitory neurosteroids, ... Melcangi RC, Celotti F, Martini L (March 1994). "Progesterone 5-alpha-reduction in neuronal and in different types of glial ...
Hepatic metabolism is mediated by 11 beta-hydroxysteroid dehydrogenases (11[beta]-HSD) and 20-ketosteroid reductases. ... alpha]-hydroxymethylprednisolone. The primary use of methylprednisolone is to suppress inflammatory and immune responses. ... 20 mg/day of prednisone (16 mg/day of methylprednisolone) is the threshold dosage for PAE development agreed upon by many ... Depo-Medrol is available as sterile aqueous solution in 20 mg/mL, 40 mg/mL, or 80 mg/mL strengths. Solu-Medrol is the only ...
Khanna M, Qin KN, Cheng KC (Jun 1995). "Distribution of 3 alpha-hydroxysteroid dehydrogenase in rat brain and molecular cloning ... Couture JF, Legrand P, Cantin L, Luu-The V, Labrie F, Breton R (Aug 2003). "Human 20alpha-hydroxysteroid dehydrogenase: ... Zhang Y, Dufort I, Rheault P, Luu-The V (Oct 2000). "Characterization of a human 20alpha-hydroxysteroid dehydrogenase". Journal ... 3-alpha)-hydroxysteroid dehydrogenase)". Human AKR1C1 genome location and AKR1C1 gene details page in the UCSC Genome Browser. ...
"Inhibition of rat ovarian 3 beta-hydroxysteroid dehydrogenase (3 beta-HSD), 17 alpha-hydroxylase and 17,20 lyase by progestins ... 3β-Hydroxysteroid dehydrogenase inhibitors, Tertiary alcohols, Ethynyl compounds, Androgens and anabolic steroids, ... p. 5. Archived from the original (RTF) on 2006-06-20. Retrieved 2006-06-01. Arakawa S, Mitsuma M, Iyo M, Ohkawa R, Kambegawa A ... 11-trien-20-yn-17β-ol-3-one, is a synthetic estrane steroid and a derivative of testosterone. It is more specifically a ...
... cytokine was originally discovered via the observation that it induced the synthesis of 20alpha-hydroxysteroid dehydrogenase in ... induces disulfide-linked IL-3 receptor alpha- and beta-chain heterodimerization, which is required for receptor activation but ... induces disulfide-linked IL-3 receptor alpha- and beta-chain heterodimerization, which is required for receptor activation but ... Ihle JN, Pepersack L, Rebar L (June 1981). "Regulation of T cell differentiation: in vitro induction of 20 alpha-hydroxysteroid ...
... variations in levels of 17 beta-hydroxysteroid dehydrogenase type 2 and 5 alpha-reductase activity compatible with androgen ... 17β-Hydroxysteroid dehydrogenase 2 (17β-HSD2) is an enzyme of the 17β-hydroxysteroid dehydrogenase (17β-HSD) family that in ... dehydrogenase 2". Moeller G, Adamski J (2006). "Multifunctionality of human 17beta-hydroxysteroid dehydrogenases". Mol. Cell. ... Soubhye J, Alard IC, van Antwerpen P, Dufrasne F (2015). "Type 2 17-β hydroxysteroid dehydrogenase as a novel target for the ...
Souness GW, Morris DJ (March 1996). "11 alpha- and 11 beta-hydroxyprogesterone, potent inhibitors of 11 beta-hydroxysteroid ... of 11β-hydroxysteroid dehydrogenase (11β-HSD). It has been known since 1987 that increased levels of 11β-OHP occur in 21- ... 11β-Hydroxysteroid dehydrogenase inhibitors, Cyclohexanols, Diketones, Human metabolites, Mineralocorticoids, Pregnanes, Enones ... potent inhibitors of 11 beta-hydroxysteroid dehydrogenase (isoforms 1 and 2), confer marked mineralocorticoid activity on ...
20alpha-hydroxysteroid dehydrogenase MeSH D08.811.682.047.436.400.150 - cortisone reductase MeSH D08.811.682.047.485 - imp ... succinate dehydrogenase MeSH D08.811.682.660.900 - testosterone 5-alpha-Reductase MeSH D08.811.682.662.162 - dihydropteridine ... 11-beta-hydroxysteroid dehydrogenase type 1 MeSH D08.811.682.047.436.174.600 - 11-beta-hydroxysteroid dehydrogenase type 2 MeSH ... hydroxysteroid dehydrogenases MeSH D08.811.682.047.436.174 - 11-beta-hydroxysteroid dehydrogenases MeSH D08.811.682.047.436.174 ...
... has been reported to act as an inhibitor of 17β-hydroxysteroid dehydrogenases. 16-Ketoestrone can be converted ... Huffman MN, Lott MH (January 1948). "16-Substituted steroids; 16-keto-alpha-estradiol and 16-ketoestrone". J. Biol. Chem. 172 ( ... by 16α-hydroxysteroid dehydrogenase into estriol in the body. Breuer, Heinz (1962). "The Metabolism of the Natural Estrogens". ... "Affinity labeling of arginyl residues at the catalytic region of estradiol 17 beta-dehydrogenase from human placenta by 16- ...
11 beta hydroxysteroid dehydrogenase type 2 deficiency 17 alpha hydroxylase deficiency 17 beta hydroxysteroide dehydrogenase ... optic atrophy 46 xx gonadal dysgenesis epibulbar dermoid, rare (NIH) 47, XXY syndrome 47, XYY syndrome 47, XXX syndrome 48, ... 3 alpha methylglutaconic aciduria, type 3, rare (NIH) 3 beta hydroxysteroid dehydrogenase deficiency 3 hydroxyisobutyric ... 3 alpha methylcrotonyl-Coa carboxylase 1 deficiency, rare (NIH) 3 alpha methylcrotonyl-coa carboxylase 2 deficiency, rare (NIH ...
It is biosynthesized by 3β-hydroxysteroid dehydrogenase from progesterone. Unlike 3α-dihydroprogesterone (3α-DHP), 3β-DHP does ... 3 alpha HP)". Brain Research. 645 (1-2): 325-329. doi:10.1016/0006-8993(94)91667-5. ISSN 0006-8993. PMID 7914815. S2CID ... "Reduction of predator odor-induced anxiety in mice by the neurosteroid 3 alpha-hydroxy-4-pregnen-20-one ( ... In the Clauberg bioassay the 3β-hydroxy-4-pregnen-20-one shows about the same potency as progesterone (34). In regard to the ...
17β-Hydroxysteroid dehydrogenase deficiency - A condition characterized by impaired androgen and estrogen synthesis in males ... XX Testicular DSD is a condition where an individual with an XX karyotype has a male appearance. Genitalia can range from ... 5α-reductase deficiency (5-ARD) - An autosomal recessive condition caused by a mutation of the 5-alpha reductase type 2 gene. ... "17β-Hydroxysteroid dehydrogenase 3 deficiency: Three case reports and a systematic review". The Journal of Steroid Biochemistry ...
... possible interference with type 1 11beta-hydroxysteroid dehydrogenase-mediated processes". J. Steroid Biochem. Mol. Biol. 104 ( ... 25-hydroxycholesterol 7-alpha-hydroxylase also known as oxysterol and steroid 7-alpha-hydroxylase is an enzyme that in humans ... Martin KO, Reiss AB, Lathe R, Javitt NB (May 1997). "7 alpha-hydroxylation of 27-hydroxycholesterol: biologic role in the ... Schwarz M, Lund EG, Russell DW (1998). "Two 7 alpha-hydroxylase enzymes in bile acid biosynthesis". Curr. Opin. Lipidol. 9 (2 ...
Casey ML, MacDonald PC, Andersson S (November 1994). "17 beta-Hydroxysteroid dehydrogenase type 2: chromosomal assignment and ... and AKR1C3 and the 17β-hydroxysteroid dehydrogenase (17β-HSD) HSD17B1. 20α-DHP can be transformed back into progesterone by 20α ... Pasqualini JR, Chetrite G (2008). "The anti-aromatase effect of progesterone and of its natural metabolites 20alpha- and 5alpha ... In animal studies, 20α-DHP has been found to be selectively taken up into and retained in target tissues such as the uterus, ...
"The identification of 5 alpha-reductase-2 and 17 beta-hydroxysteroid dehydrogenase-3 gene defects in male pseudohermaphrodites ... "Entrez Gene: HSD17B3 hydroxysteroid (17-beta) dehydrogenase 3". "Testosterone 17-beta-dehydrogenase deficiency - Conditions - ... 17β-Hydroxysteroid dehydrogenase 3 (17β-HSD3) is an enzyme that in humans is encoded by the HSD17B3 gene and is involved in ... 17β-Hydroxysteroid dehydrogenase GRCh38: Ensembl release 89: ENSG00000130948 - Ensembl, May 2017 GRCm38: Ensembl release 89: ...
It is biosynthesized by 3α-hydroxysteroid dehydrogenase from progesterone. 3α-DHP has been found to act as a positive ... 3 alpha HP)". Brain Research. 645 (1-2): 325-329. doi:10.1016/0006-8993(94)91667-5. ISSN 0006-8993. PMID 7914815. S2CID ... "Reduction of predator odor-induced anxiety in mice by the neurosteroid 3 alpha-hydroxy-4-pregnen-20-one ( ... 3α-Dihydroprogesterone (3α-DHP), also known as 3α-hydroxyprogesterone, as well as pregn-4-en-3α-ol-20-one, is an endogenous ...
October 2004). "11beta-hydroxysteroid dehydrogenase type 1: a tissue-specific regulator of glucocorticoid response". Endocrine ... 11 alpha-Hydroxyprogesterone (11 alpha OH-P) was an order of magnitude more potent a competitive inhibitor of the 11 beta HSD-2 ... Souness GW, Morris DJ (March 1996). "11 alpha- and 11 beta-hydroxyprogesterone, potent inhibitors of 11 beta-hydroxysteroid ... of 11β-hydroxysteroid dehydrogenase (11β-HSD). It is notably not metabolized by 11β-HSD2. 11α-OHP is a more potent inhibitor of ...
Marcus PI, Talalay P (February 1956). "Induction and purification of alpha- and beta-hydroxysteroid dehydrogenases". The ... 17β-Hydroxysteroid dehydrogenases (17β-HSD, HSD17B) (EC 1.1.1.51), also 17-ketosteroid reductases (17-KSR), are a group of ... Ning X, Yang Y, Deng H, Zhang Q, Huang Y, Su Z, Fu Y, Xiang Q, Zhang S (2017). "Development of 17β-hydroxysteroid dehydrogenase ... Soubhye J, Alard IC, van Antwerpen P, Dufrasne F (2015). "Type 2 17-β hydroxysteroid dehydrogenase as a novel target for the ...
This process is catalyzed by 3 α- and 3 β-hydroxy steroid dehydrogenase (HSD). CYP450 enzymes will then catalyze aromatic ... Alpha-zearalanol is also produced semisynthetically, for veterinary use; such use is prohibited in the European Union. ... More than one study has shown that detectable levels of zearalenone and its metabolite alpha-zearalanol in girls are associated ... Richardson, Kurt E.; Hagler, Winston M.; Mirocha, Chester J. (September 1985). "Production of zearalenone, .alpha.- and .beta.- ...
The reductive pathways are by 11β-hydroxysteroid dehydrogenase type 1 in the liver and AKR7A2/AKR7A3 in the intestine leading ... The alpha position adjacent to the ketone is first brominated followed by nucleophilic displacement of the resulting alpha- ... Chen WC, Lai HC, Su WP, Palani M, Su KP (January 2015). "Bupropion for interferon-alpha-induced depression in patients with ... Based on studies indicating that bupropion lowers the level of the inflammatory mediator TNF-alpha, there have been suggestions ...
... a potentially first-in-class oral 17β-hydroxysteroid dehydrogenase type 1 inhibitor. Their products are divided into three main ... Block, Jonathan (2021-06-03). "Merck spinoff Organon begins trading on the NYSE today; Organon down 5% , Seeking Alpha". ... "OGN - Organon & Co". Seeking Alpha. Retrieved 4 June 2021. "Organon & Co" (PDF). SEC. Organon & Co. Retrieved 30 September 2023 ... A copy of the Information Statement sent to Merck shareholders was filed with the U.S. SEC on April 20, 2021 in a Form 10-12B/A ...
... steroids androstanediol via 17β-hydroxysteroid dehydrogenase or from androstanedione via 3β-hydroxysteroid dehydrogenase. 3β- ... alpha-->beta)-hydroxysteroid epimerase". Biochimica et Biophysica Acta. 1520 (2): 124-30. doi:10.1016/s0167-4781(01)00247-0. ... 298-. ISBN 978-81-87224-85-3. Raeside JI, Renaud RL, Marshall DE (March 1992). "Identification of 5 alpha-androstane-3 beta,17 ... 42 (1): 113-20. doi:10.1016/0960-0760(92)90017-d. PMID 1558816. S2CID 53274020. Callies F, Arlt W, Siekmann L, Hübler D, ...
20alpha-dihydroxypregn-4-en-3-one, NAD+, and NADP+, whereas its 4 products are 17-alpha-hydroxyprogesterone, NADH, NADPH, and ... Other names in common use include 20alpha-hydroxy steroid dehydrogenase, 20alpha-hydroxy steroid dehydrogenase, 20alpha-HSD, ... "Expression of 17beta-hydroxysteroid dehydrogenase type 1 and type 2, P450 aromatase, and 20alpha-hydroxysteroid dehydrogenase ... Hershkovitz L, Beuschlein F, Klammer S, Krup M, Weinstein Y (March 2007). "Adrenal 20alpha-hydroxysteroid dehydrogenase in the ...
20alpha-hydroxysteroid dehydrogenase [109609] (2 species). *. Species Human (Homo sapiens) [TaxId:9606] [109610] (1 PDB entry) ... 3-alpha-hydroxysteroid dehydrogenase [51439] (2 species). *. Species Human (Homo sapiens), type III [TaxId:9606] [69383] (16 ... Class c: Alpha and beta proteins (a/b) [51349] (148 folds). *. Fold c.1: TIM beta/alpha-barrel [51350] (33 superfamilies). ...
3β-hydroxysteroid dehydrogenase deficiency, see 3-beta-hydroxysteroid dehydrogenase deficiency. *4 alpha aminobutyrate ... 46,XX testicular difference of sex development. *46,XX testicular disorder of sex development, see 46,XX testicular difference ... 3-beta-hydroxysteroid dehydrogenase deficiency. *3-beta-hydroxysteroid dehydrogenase deficiency, see 3-beta-hydroxysteroid ... 3b-hydroxysteroid dehydrogenase deficiency, see 3-beta-hydroxysteroid dehydrogenase deficiency. *3beta-HSDH deficiency, see ...
3-beta-hydroxysteroid dehydrogenase (3BHSD) deficiency is a rare genetic disorder of steroid biosynthesis that results in ... Finally, a deficiency in the related 3-alpha-hydrozysteroid dehydrogenase may also play a role in hirsutism. 3-alpha HSD is ... 3-beta-hydroxysteroid dehydrogenase deficiency also occurs in 46,XX female infants (who may have mild clitoromegaly), as well ... 3-Beta-Hydroxysteroid Dehydrogenase Deficiency. 3-beta-hydroxysteroid dehydrogenase (3BHSD) is required for the synthesis of ...
Human 3-alpha hydroxysteroid dehydrogenase type 3 (3alpha-HSD3) the V54L mutation restricting the steroid alternative binding ... 20alpha-HSD displays a distinctive ability in transforming progesterone to 20alpha-hydroxy-progesterone. Homo sapiens. ... 3-alpha hydroxysteroid dehydrogenase type 3 has an essential role in the inactivation of 5alpha-dihydrotestosterone preventing ... the other binding mode resembling the orientation of 20alpha-OHProg in the ternary complex of human 20alpha-HSD-NADP+-20alpha- ...
... and oxytocin receptors and of 20alpha-hydroxysteroid dehydrogenase and cyclooxygenase II 2 and 5 days after ovulation in ... Casein Kinase Ⅰ Alpha; HSPCA:Heat Shock Protein HSP 90-alpha; SHC2:SHC adaptor protein 2; ATF6B:Activating Transcription Factor ... Total protein (100 µg) solution was reduced with 10 mM DTT for one hour at 37 °C and alkylated with 20 mM IAA for 45 min at ... The clean reads that were filtered from the raw reads were mapped to the yaks genome using Tophat2 software [20]. The aligned ...
E2 17-beta-dehydrogenase 1, EC 1.1.1.62, 17-beta-hydroxysteroid dehydrogenase type 1, 17-beta-HSD 1, 20 alpha-hydroxysteroid ... E2 17-beta-dehydrogenase 1 (HSD17B1) is a member of the short-chain dehydrogenases/reductases (SDR) family. The HSD17B1 protein ... Placental 17-beta-hydroxysteroid dehydrogenase, HSD17B1, E17KSR, EDH17B1, EDH17B2, EDHB17, HSD17, SDR28C1. ... Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA ...
... and none of my peers think its feasible for a cure to be released even in the next twenty years. Research is great, but ... 3-Alpha-Hydroxysteroid Dehydrogenase, Sulforaphane, Technion University. Increasing 3-Alpha-Hydroxysteroid Dehydrogenase to ... Increased expression of type 2 3-alpha-hydroxysteroid dehydrogenase/type 5 17-beta-hydroxysteroid dehydrogenase. (AKR1C3) and ... 3a alpha hydroxysteroid dehydrogenase (3a hsd) is an enzyme found all over the body where its primary purpose is to "deactivate ...
Abnormal lipometabolism in peroxisomes is involved in tumor progression and hydroxysteroid dehydrogenase-like 2 (HSDL2), ... Overexpression of Karyopherin Subunit alpha 2 (KPNA2) Predicts Unfavorable Prognosis and Promotes Bladder Cancer Tumorigenicity ... Role of Hydroxysteroid Dehydrogenase-Like 2 (HSDL2) in Human Ovarian Cancer DOI: 10.12659/MSM.909418 ... 20 May 2019 : Clinical Research. Expression of WD Repeat Domain 5 (WDR5) is Associated with Progression and Reduced Prognosis ...
Ermalone is rapidly broken down within skeletal muscle tissue by the 3-alpha hydroxysteroid dehydrogenase enzyme. As a ... Formula: C20H32O2 Melting Point (base): 189 - 196 C. Manufacturer: No longer manufactured. Effective Dose (Men): 10-20 mg/day. ... The recommended dosage for Ermalone users is 10-20 mg/day for 6-8 weeks, which is often enough to keep blood serum levels well ...
5 alpha reductase deficiency (5ARD); 17-hydroxysteroid dehydrogenase deficiency (17HSD); mixed gonadal dysgenesis (MGD) and ... Twelve of the twenty-five 5ARD2 patients agreed to undertake genetic analysis, and two mutations of the SRD5A2 gene were ... The 17-beta-hydroxysteroid dehydrogenase type 3 (17-ß-HSD3) enzyme converts androstenedione to testosterone and is encoded by ... Disorder of Sex Development Due to 17-Beta-Hydroxysteroid Dehydrogenase Type 3 Deficiency: A Case Report and Review of 70 ...
D8.811.682.47.820.125 3-alpha-Hydroxysteroid Dehydrogenase (B-Specific) D8.811.682.47.820.186 3-Hydroxyacyl CoA Dehydrogenases ... D12.125.119.409.174 11-beta-Hydroxysteroid Dehydrogenase Type 1 D8.811.682.47.820.100.300 11-beta-Hydroxysteroid Dehydrogenase ... D8.811.682.47.820.100.600 11-beta-Hydroxysteroid Dehydrogenases D8.811.682.47.820.100 14-3-3 Proteins D12.644.360.24.313 ... G7.700.320.500.325.377.437 Malate Dehydrogenase D8.811.682.47.605 D8.811.682.47.820.496 Malate Dehydrogenase (NADP+) D8.811. ...
D8.811.682.47.820.125 3-alpha-Hydroxysteroid Dehydrogenase (B-Specific) D8.811.682.47.820.186 3-Hydroxyacyl CoA Dehydrogenases ... D12.125.119.409.174 11-beta-Hydroxysteroid Dehydrogenase Type 1 D8.811.682.47.820.100.300 11-beta-Hydroxysteroid Dehydrogenase ... D8.811.682.47.820.100.600 11-beta-Hydroxysteroid Dehydrogenases D8.811.682.47.820.100 14-3-3 Proteins D12.644.360.24.313 ... G7.700.320.500.325.377.437 Malate Dehydrogenase D8.811.682.47.605 D8.811.682.47.820.496 Malate Dehydrogenase (NADP+) D8.811. ...
Estradiol 17-beta-dehydrogenase 2) (EC 1.1.1.62) (Microsomal 17-beta-hydroxysteroid dehydrogenase) (Short chain dehydrogenase/ ... Alpha-amylase 1A. AMY1A. P0DUB6. 1 Reference(s). T49ORJ. Peroxisome proliferator-activated receptor alpha. PPARA. Q07869. 5 ... Xanthine dehydrogenase/oxidase [Includes: Xanthine dehydrogenase. XDH. P47989. 6 Reference(s). T32R5L. Cyclin-dependent kinase ... 17-beta-hydroxysteroid dehydrogenase type 2 (17-beta-HSD 2) (20 alpha-hydroxysteroid dehydrogenase) (20-alpha-HSD) (E2DH) ( ...
Classic 3-beta-hydroxysteroid dehydrogenase deficiency is an autosomal recessive form of CAH characterized by a severe ... 46,XX disorder of sex development induced by fetal androgens excess*3 beta-Hydroxysteroid dehydrogenase deficiency ... 17alpha-hydroxypregnenolone is a 21-carbon steroid that is converted from pregnenolone by steroid 17-alpha-hydroxylase, as an ... 3-beta-Hydroxysteroid Dehydrogenase-Deficient Congenital Adrenal Hyperplasia; 3b-hydroxysteroid dehydrogenase deficiency; ...
Title: Overexpression of hepatic 5α-reductase and 11β-hydroxysteroid dehydrogenase type 1 in visceral adipose tissue is ... 3-oxo-5-alpha-steroid 4-dehydrogenase (NADP(+)). 3-oxo-5-alpha-steroid 4-dehydrogenase 3. SR type 3. probable polyprenol ... enables 3-oxo-5-alpha-steroid 4-dehydrogenase activity IBA Inferred from Biological aspect of Ancestor. more info ... enables 3-oxo-5-alpha-steroid 4-dehydrogenase activity TAS Traceable Author Statement. more info ...
hydroxysteroid 17-beta dehydrogenase 2. involved_in. ISO. IEA. estrone. RGD. Ensembl. PMID:8612487. GO_REF:0000107 RGD:728619. ... steroid 17-alpha-hydroxylase/17,20 lyase. involved_in. acts_upstream_of_or_within. IEA. ISO. (PMID:7588219). Ensembl. MGI. PMID ... hydroxysteroid 17-beta dehydrogenase 1. involved_in. ISO. IEA. estradiol. RGD. TreeGrafter. UniProt. Ensembl. InterPro. PMID: ... hydroxysteroid 17-beta dehydrogenase 8. involved_in. IEA. Ensembl. TreeGrafter. GO_REF:0000107 GO_REF:0000118. NCBI chrNW_ ...
3-alpha-Hydroxysteroid Dehydrogenase (B-Specific). 3-alfa-Hidroxiesteroide Deshidrogenasa (B-Específica). ... 11-beta-Hydroxysteroid Dehydrogenases. 11-beta-Hidroxiesteroide Deshidrogenasas. 20-alfa-Hidroxiesteróide Desidrogenase. 20- ... alpha-Hydroxysteroid Dehydrogenase. 20-alfa-Hidroxiesteroide Deshidrogenasa. 3-Metil-2-Oxobutanoato Desidrogenase (Lipoamida). ... Acyl-CoA Dehydrogenase. Acil-CoA Deshidrogenasa. Acil-CoA Desidrogenase de Cadeia Longa. Acyl-CoA Dehydrogenase, Long-Chain. ...
3-alpha-Hydroxysteroid Dehydrogenase (B-Specific). 3-alfa-Hidroxiesteróide Desidrogenase (B-Específica). 3-alfa- ... 11-beta-Hydroxysteroid Dehydrogenase Type 1. 11-beta-Hidroxiesteróide Desidrogenase Tipo 1. 11-beta-Hidroxiesteroide ... 11-beta-Hydroxysteroid Dehydrogenase Type 2. 11-beta-Hidroxiesteróide Desidrogenase Tipo 2. 11-beta-Hidroxiesteroide ... Acyl-CoA Dehydrogenase. Acil-CoA Desidrogenase. Acil-CoA Deshidrogenasa. Acyl-CoA Dehydrogenase, Long-Chain. Acil-CoA ...
This oxidative 3 alpha-hydroxysteroid dehydrogenase 3 alpha-hsd activity of rodh-4 is competitively inhibited by retinol and ... Verdens mest populære fotballsko i over 20 år.. After all, there might be someone reading and be acting on the incomplete ... Españoles en el mundo - avance - tennessee - 20 sep Og til slutt, når logoen er klar for digitalisering, la oss gå videre til ... Unge moden mann søker kvinne yngre 20 gjøvik eskortetjeneste trondheim milf massage sex dukke i full størrelse hd filmer milf ...
Adrenal hyperplasia, congenital, due to 3-beta-hydroxysteroid dehydrogenase 2 deficiency. *Hattori N, Ishihara T, Moridera K, ... Kim SM, Rhee JH: A case of 17 alpha-hydroxylase deficiency. Clin Exp Reprod Med. 2015 Jun;42(2):72-6. doi: 10.5653/cerm.2015.42 ... Fujieda K, Tajima T, Nakae J, Sageshima S, Tachibana K, Suwa S, Sugawara T, Strauss JF 3rd: Spontaneous puberty in 46,XX ... 201810 (Adrenal hyperplasia, congenital, due to 3-beta-hydroxysteroid dehydrogenase 2 deficiency) ...
... we focused on GC metabolizing enzymes such as 11 beta-hydroxysteroid dehydrogenase 1 and 2 (Hsd11b1 and Hsd11b2) and steroid 5 ... Twenty-four animals were divided into three groups as control, HFCS group (11 % HFCS-55 solution, ad libitum) and HFCS+ Vit D ( ... alpha-reductase 1 (Srd5a1). Western blotting showed an increase in Hsd11b1 expression and a decrease in Hsd11b2 expression in ... METHODS: Twenty-four rats were randomized into three groups: sham (n = 8), experimental fatty liver group (n = 8), and fatty ...
Z. Michailidou, M. D. Jensen, D. A. Dumesic et al., "Omental 11β-hydroxysteroid dehydrogenase 1 correlates with fat cell size ... tumor necrosis factor alpha (TNF-α), leptin, interleukin 6 (IL-6), and transforming growth factor beta (TGF-β). [1] ... β-hydroxysteroid dehydrogenase type 1 enhances angiogenesis," Proceedings of the National Academy of Sciences of the United ... β-hydroxysteroid dehydrogenase type 1 (HSD1)-deficient mice," The Journal of Biological Chemistry, vol. 287, no. 6, pp. 4188- ...
Pills in this stack target common hydroxysteroid dehydrogenases (oxido-reductases) gH-releasing factors and are they detectable ... Alpha Pharma Letrozole. Creatinine, and uric acid levels were determined together with sodium Alpha Pharma Letrozole and ... 3beta-hydroxypregn-5-en-20-one) catalysed by adrenal cytochrome administered corticosteroids, may ... ...
3-beta-hydroxysteroid dehydrogenase deficiency: An abnormal ratio of 17-hydroxypregnenolone to 17-hydroxyprogesterone and of ... CYP21A is the gene that codes for 21-hydroxylase, CYP11B1 codes for 11-beta-hydroxylase, and CYP17 codes for 17-alpha- ... A female patient with the 46,XX karyotype with mild virilization due to congenital virilizing adrenal hyperplasia secondary to ... Females with severe CAH due to deficiencies of 21-hydroxylase, 11-beta-hydroxylase, or 3-beta-hydroxysteroid dehydrogenase have ...
11-beta-Hydroxysteroid Dehydrogenase Type 1. 11-beta-Hydroxysteroid Dehydrogenase Type 1 (Structural Class). NDF-RT (Drug ... 15-Hydroxy-11 alpha,9 alpha-(epoxymethano)prosta-5,13-dienoic Acid. 15-Hydroxy-11 alpha,9 alpha-(epoxymethano)prosta-5,13- ... 11-beta-Hydroxysteroid Dehydrogenase Type 2. 11-beta-Hydroxysteroid Dehydrogenase Type 2 (Structural Class). NDF-RT (Drug ... 11-beta-Hydroxysteroid Dehydrogenases. 11-beta-Hydroxysteroid Dehydrogenases (Structural Class). NDF-RT (Drug Classification). ...
Estrone can then be converted to the more reactive estradiol by 17β-hydroxysteroid dehydrogenase. The measurement of estrone ... Luteinizing hormone (LH) is a heterodimeric glycoprotein that consists of one alpha and one beta subunit. LH is produced mainly ... It is a conjugated steroid converted by the sulfation of dehydroepiandrosterone (DHEA) at the 3β position via hydroxysteroid ... the aromatization of androstenedione but can also be reversibly converted from estradiol via 17β-hydroxysteroid dehydrogenase. ...
Hexose-6-phosphate dehydrogenase confers oxo-reductase activity upon 11β-hydroxysteroid dehydrogenase type 1 J Mol Endocrinol ... The mouse estrogen receptor-related orphan receptor alpha 1: molecular cloning and estrogen responsiveness J Mol Endocrinol 19 ... Liver-type 11β-hydroxysteroid dehydrogenase cDNA encodes reductase but not dehydrogenase activity in intact mammalian COS-7 ... Intracrinology: role of the family of 17 beta-hydroxysteroid dehydrogenases in human physiology and disease J Mol Endocrinol 25 ...
3-Beta-Hydroxysteroid Dehydrogenase Deficiency * Androgen Excess * C-17 Hydroxylase Deficiency * Suprarenal (Adrenal) Gland ... They then start to drop; by age 80 years, the concentration is about 20% of that at age 25 years. ...
  • 3-Beta-hydroxysteroid dehydrogenase (3BHSD) deficiency is a rare form of congenital adrenal hyperplasia that results in decreased production of all three groups of adrenal steroids: mineralocorticoids, glucocorticoids, and sex steroids. (medscape.com)
  • Although first described in male infants with ambiguous genitalia and severe salt wasting, 3-beta-hydroxysteroid dehydrogenase deficiency also occurs in 46,XX female infants (who may have mild clitoromegaly), as well as in older patients who present with a milder or so-called late-onset variant. (medscape.com)
  • A variety of mutations in the HSD3B2 gene affect the activity of this enzyme, resulting in the extremely variable, phenotypic presentations of 3-beta-hydroxysteroid dehydrogenase deficiency. (medscape.com)
  • Micropenis can also occur in children with LH-receptor defects and defects in testosterone biosynthesis (e.g. 17-beta hydroxysteroid dehydrogenase deficiency). (medscape.com)
  • Individuals with 17-beta hydroxysteroid dehydrogenase deficiency most often have female-appearing genitalia and, less often, ambiguous genitalia. (medscape.com)
  • Defects in peripheral androgen action include 5-alpha reductase deficiency (failure of conversion of testosterone to DHT) and partial androgen insensitivity syndrome (PAIS) due to an androgen receptor defect. (medscape.com)
  • Classic 3-beta-hydroxysteroid dehydrogenase deficiency is an autosomal recessive form of CAH characterized by a severe impairment of steroid biosynthesis in both the adrenals and the gonads, resulting in decreased excretion of cortisol and aldosterone and of progesterone, androgens, and estrogens by these tissues. (nih.gov)
  • 3-beta (ß)-hydroxysteroid dehydrogenase (HSD) deficiency is an inherited disorder that affects hormone-producing glands including the gonads (ovaries in females and testes in males) and the adrenal glands. (nih.gov)
  • In enzymology, a 20-α-hydroxysteroid dehydrogenase (EC 1.1.1.149) is an enzyme that catalyzes the chemical reaction 17alpha,20alpha-dihydroxypregn-4-en-3-one + NAD(P)+ ⇌ {\displaystyle \rightleftharpoons } 17alpha-hydroxyprogesterone + NAD(P)H + H+ The 3 substrates of this enzyme are 17alpha,20alpha-dihydroxypregn-4-en-3-one, NAD+, and NADP+, whereas its 4 products are 17-alpha-hydroxyprogesterone, NADH, NADPH, and H+. (wikipedia.org)
  • The systematic name of this enzyme class is 20alpha-hydroxysteroid:NAD(P)+ 20-oxidoreductase. (wikipedia.org)
  • 20alpha-HSD has been initially described as a progesterone metabolizing enzyme of the ovary. (wikipedia.org)
  • This condition is due to defects in type II 3-beta-hydroxysteroid dehydrogenase, an enzyme that occurs almost exclusively in the gonads and adrenal glands. (medscape.com)
  • By contrast, cortisol synthesis and secretion is regulated by adrenocorticotropic hormone (ACTH), which stimulates the enzyme P-450scc (20,22 desmolase), with subsequent increased production of all adrenal steroids in both the zona fasciculata and the zona reticularis (see image below). (medscape.com)
  • ACTH stimulates the enzyme P-450scc (20,22 desmolase) with subsequent increased production of all adrenal steroids. (medscape.com)
  • I did not realize that the Technion University team from Israel (which I covered briefly last year under 3D printed comb ) has a few pages on their website covering this very subject of the 3-alpha-hydroxysteroid dehydrogenase (3α-HSD) enzyme. (hairlosscure2020.com)
  • Anyways, enjoy researching but I believe it really does tie the whole pgd2, dht and maybe even wnt pathway approaches under one enzyme: 3-alpha-hsd. (hairlosscure2020.com)
  • Well there turns out to be an "antimatter" sort of enzyme present in every human's musculoskeletal structure called 3 alpha hydroxysteroid dehydrogenase (3a HSD) which converts all T and DHT to 3 adiol g (another testosterone by-product which is not harmless to hair and way less androgenous). (hairlosscure2020.com)
  • It does seem like increasing the expression of the 3α-hydroxysteroid dehydrogenase enzyme will reduce DHT and lead to a reduction in hair loss and perhaps even lead to regrowth of hair that has been lost in recent years. (hairlosscure2020.com)
  • Testosterone is peripherally converted by the enzyme 5-alpha reductase to the more potent androgen DHT, which is responsible for virilization of the male external genitalia. (medscape.com)
  • Since no further structural modification was added to protect the 3-ketone group, Ermalone is rapidly broken down within skeletal muscle tissue by the 3-alpha hydroxysteroid dehydrogenase enzyme. (steroid.com)
  • Human placental 17 beta-estradiol dehydrogenase and 20 alpha-hydroxysteroid dehydrogenase. (wikipedia.org)
  • E2 17-beta-dehydrogenase 1 (HSD17B1) is a member of the short-chain dehydrogenases/reductases (SDR) family. (prospecbio.com)
  • In addition, the HSD17B1 has a 20-alpha-HSD activity. (prospecbio.com)
  • Aging (Albany NY), 2020 Nov 20. (nih.gov)
  • Human 3-alpha hydroxysteroid dehydrogenase type 3 (3alpha-HSD3) the V54L mutation restricting the steroid alternative binding and enhancing the 20? (brenda-enzymes.info)
  • collagen type XIII alpha 1 ch. (gsea-msigdb.org)
  • It is involved in the production of androgen 5-alpha-dihydrotestosterone (DHT) from testosterone, and maintenance of the androgen-androgen receptor activation pathway. (nih.gov)
  • The protein encoded by this gene belongs to the steroid 5-alpha reductase family, and polyprenol reductase subfamily. (nih.gov)
  • Steroid 5 alpha-reductase 3 (SRD5A3) promotes tumor growth and predicts poor survival of human hepatocellular carcinoma (HCC). (nih.gov)
  • Older patients with mild defects in 3-beta-hydroxysteroid dehydrogenase activity (late-onset or nonclassic variant) may present with premature pubic hair development, hirsutism, irregular menstrual cycles or primary amenorrhea. (medscape.com)
  • It is a conjugated steroid converted by the sulfation of dehydroepiandrosterone (DHEA) at the 3β position via hydroxysteroid sulfotransferase. (cdc.gov)
  • AKR1C1, AKR1C2, and AKR1C3 AKR1C1 has high catalytic efficiency as a 20α-HSD and AKR1C2 and AKR1C3 efficiently catalyze this reaction as well. (wikipedia.org)
  • While 20alpha-HSD expression and activity is downregulated in the corpus luteum of pregnancy, 24 hrs prior to parturition ovarian 20alpha-HSD activity is acutely stimulated. (wikipedia.org)
  • Indicating that expression of 20alpha-HSD activity is mandatory for the induction of parturition through reduction of progesterone blood concentration. (wikipedia.org)
  • site-directed mutagenesis, the change renders the sequence identical to that of human 20-alpha hydroxysteroid dehydrogenase. (brenda-enzymes.info)
  • The V54L mutation directly restricts the steroid binding modes to a unique one, which resembles the orientation of 20alpha-OHProg within human 20alpha-HSD. (brenda-enzymes.info)
  • human 3alpha-HSD3 shares 97.8% sequence identity with human 20-alpha hydroxysteroid dehydrogenase (20alpha-HSD) and there is only one amino acid difference (residue 54) that is located in their steroid binding pockets. (brenda-enzymes.info)
  • Estrogen receptor alpha mRNA variant lacking exon 5 is co-ex- pressed with the wildtype in endometrial adenocarcinoma. (ugm.ac.id)
  • Other names in common use include 20alpha-hydroxy steroid dehydrogenase, 20alpha-hydroxy steroid dehydrogenase, 20alpha-HSD, and 20alpha-HSDH. (wikipedia.org)
  • Pills in this stack target common hydroxysteroid dehydrogenases (oxido-reductases) gH-releasing factors and are they detectable. (edward-kim.com)
  • Estimations include consumer-level-loss (CLL) allowances used before (20%), and after, subjective, retroactively-applied increases (34%), as recommended by corn-refiners (~ 2012). (bvsalud.org)
  • Obesity or higher body mass index is closely associated with NAFLD in a dose-dependent manner, with approximately 20% increase in the risk of developing NAFLD for every unit increase in body mass index [ 13 ]. (e-cmh.org)
  • As for a compressed version of my research, as we both know alpha 5ar converts T to DHT. (hairlosscure2020.com)
  • As BMI increases to obesity levels, morbidity and mortality rates rise dramatically [ 4 , 12 - 20 ]. (hindawi.com)
  • 2. Tibolone metabolism in human liver is catalyzed by 3alpha/3beta-hydroxysteroid dehydrogenase activities of the four isoforms of the aldo-keto reductase (AKR)1C subfamily. (nih.gov)
  • In addition, there has been interest in the cytochrome p450c17alpha (CYP17) gene, which encodes the enzyme involved in testosterone biosynthesis, and the 3beta-hydroxysteroid dehydrogenase type II (HSD3beta2) gene which encodes enzymes involved in metabolism of dihydrotestosterone. (nih.gov)
  • Recent investigations have suggested that prostate cancer risk is related to certain polymorphic genes that regulate androgen metabolism, particularly the androgen receptor (AR) gene, and the steroid 5-alpha-reductase type II (SRD5A2) gene. (nih.gov)
  • AN - infection: coord IM with ACTINOBACILLUS INFECTIONS (IM) HN - 2004 MH - Acyl-CoA Dehydrogenase UI - D042964 MN - D8.811.682.675.150.100 MN - D12.776.331.99 MS - A flavoprotein oxidoreductase that has specificity for medium-chain fatty acids. (nih.gov)
  • use ACYL-COA DEHYDROGENASE (NM) 1980-2003 MH - Acyl-CoA Dehydrogenase, Long-Chain UI - D044942 MN - D8.811.682.675.150.150 MN - D12.776.331.700 MS - A flavoprotein oxidoreductase that has specificity for long-chain fatty acids. (nih.gov)
  • This gene encodes a member of the 17beta-hydroxysteroid dehydrogenase family of short-chain dehydrogenases/reductases. (nih.gov)
  • Catalyzes the beta-oxidation at position 17 of androgens and estrogens and has 3-alpha-hydroxysteroid dehydrogenase activity with androsterone. (joplink.net)
  • Older patients with mild defects in 3-beta-hydroxysteroid dehydrogenase activity (late-onset or nonclassic variant) may present with premature pubic hair development, hirsutism, irregular menstrual cycles or primary amenorrhea. (medscape.com)
  • Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20? (joplink.net)
  • Most of 46 XX CAH patients, even if markedly virilised, and 46 XY complete androgen insensitivity syndrome are raised as females. (nih.gov)
  • An enzymes that catalyzes the reversible reduction-oxidation reaction of 20-alpha-hydroxysteroids, such as from PROGESTERONE to 20-ALPHA-DIHYDROPROGESTERONE . (nih.gov)
  • It has an N-terminal short-chain dehydrogenase domain with a cofactor binding site, and a narrow, hydrophobic C-terminal domain with a steroid substrate binding site. (nih.gov)
  • 1. Reversal of inflammation-associated dihydrodiol dehydrogenases (AKR1C1 and AKR1C2) overexpression and drug resistance in nonsmall cell lung cancer cells by wogonin and chrysin. (nih.gov)
  • Also has 20-alpha-HSD activity. (nih.gov)
  • shown activity in model systems of other cancer types [16, 20, 21]. (immune-source.com)
  • 18. Inhibitors of human 20α-hydroxysteroid dehydrogenase (AKR1C1). (nih.gov)
  • Carries out oxidative conversions of 7-alpha-OH and 7-beta-OH bile acids. (joplink.net)
  • Also exhibits 20-beta-OH and 21-OH dehydrogenase activities with C21 steroids. (joplink.net)
  • Patients with classic salt-losing 3-beta-hydroxysteroid dehydrogenase require initial replacement of glucocorticoids and mineralocorticoid, plus the addition of sex steroids at appropriate, pubertal age. (medscape.com)
  • The majority of diabetes patients (70%) are overweight or obese, and the obesity rate is expected to increase 33% in the next 20 years [ 2 ]. (e-dmj.org)
  • Such therapy promotes development of secondary sexual characteristics in both males and females, and cyclic menstrual bleeding in 46,XX females. (medscape.com)
  • HN - 2004 MH - Acidiphilium UI - D041801 MN - B3.440.400.425.100.110 MN - B3.660.50.10.20 MS - A genus in the family ACETOBACTERACEAE consisting of chemoorganotrophic, straight rods with rounded ends. (nih.gov)
  • 2020. Twenty years of transcriptomics, 17alpha-ethinylestradiol, and fish. (nih.gov)
  • Generally, the shelf life of liquid form is 6 months at -20? (joplink.net)
  • The shelf life of lyophilized form is 12 months at -20? (joplink.net)