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.
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.
The rate dynamics in chemical or physical systems.
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 large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
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.
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.
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)
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
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.
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.
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.
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.
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)
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.
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.
Alcohol oxidoreductases with substrate specificity for LACTIC ACID.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.
Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.
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.
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.
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.
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.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
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).
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.
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)
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.
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
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.

Human brain short chain L-3-hydroxyacyl coenzyme A dehydrogenase is a single-domain multifunctional enzyme. Characterization of a novel 17beta-hydroxysteroid dehydrogenase. (1/334)

Human brain short chain L-3-hydroxyacyl-CoA dehydrogenase (SCHAD) was found to catalyze the oxidation of 17beta-estradiol and dihydroandrosterone as well as alcohols. Mitochondria have been demonstrated to be the proper location of this NAD+-dependent dehydrogenase in cells, although its primary structure is identical to an amyloid beta-peptide binding protein reportedly associated with the endoplasmic reticulum (ERAB). This fatty acid beta-oxidation enzyme was identified as a novel 17beta-hydroxysteroid dehydrogenase responsible for the inactivation of sex steroid hormones. The catalytic rate constant of the purified enzyme was estimated to be 0.66 min-1 with apparent Km values of 43 and 50 microM for 17beta-estradiol and NAD+, respectively. The catalytic efficiency of this enzyme for the oxidation of 17beta-estradiol was comparable with that of peroxisomal 17beta-hydroxysteroid dehydrogenase type 4. As a result, the human SCHAD gene product, a single-domain multifunctional enzyme, appears to function in two different pathways of lipid metabolism. Because the catalytic functions of human brain short chain L-3-hydroxyacyl-CoA dehydrogenase could weaken the protective effects of estrogen and generate aldehydes in neurons, it is proposed that a high concentration of this enzyme in brain is a potential risk factor for Alzheimer's disease.  (+info)

Unique multifunctional HSD17B4 gene product: 17beta-hydroxysteroid dehydrogenase 4 and D-3-hydroxyacyl-coenzyme A dehydrogenase/hydratase involved in Zellweger syndrome. (2/334)

Six types of human 17beta-hydroxysteroid dehydrogenases catalyzing the conversion of estrogens and androgens at position C17 have been identified so far. The peroxisomal 17beta-hydroxysteroid dehydrogenase type 4 (17beta-HSD 4, gene name HSD17B4) catalyzes the oxidation of estradiol with high preference over the reduction of estrone. The highest levels of 17beta-HSD 4 mRNA transcription and specific activity are found in liver and kidney followed by ovary and testes. A 3 kb mRNA codes for an 80 kDa (737 amino acids) protein featuring domains which are not present in the other 17beta-HSDs. The N-terminal domain of 17beta-HSD 4 reveals only 25% amino acid similarity with the other types of 17beta-HSDs. The 80 kDa protein is N-terminally cleaved to a 32 kDa enzymatically active fragment. Both the 80 kDa and the N-terminal 32 kDa (amino acids 1-323) protein are able to perform the dehydrogenase reaction not only with steroids at the C17 position but also with D-3-hydroxyacyl-coenzyme A (CoA). The enzyme is not active with L-stereoisomers. The central part of the 80 kDa protein (amino acids 324-596) catalyzes the 2-enoyl-acyl-CoA hydratase reaction with high efficiency. The C-terminal part of the 80 kDa protein (amino acids 597-737) facilitates the transfer of 7-dehydrocholesterol and phosphatidylcholine between membranes in vitro. The HSD17B4 gene is stimulated by progesterone, and ligands of PPARalpha (peroxisomal proliferator activated receptor alpha) such as clofibrate, and is down-regulated by phorbol esters. Mutations in the HSD17B4 lead to a fatal form of Zellweger syndrome.  (+info)

Enoyl-CoA hydratase deficiency: identification of a new type of D-bifunctional protein deficiency. (3/334)

D-bifunctional protein is involved in the peroxisomal beta-oxidation of very long chain fatty acids, branched chain fatty acids and bile acid intermediates. In line with the central role of D-bifunctional protein in the beta-oxidation of these three types of fatty acids, all patients with D-bifunctional protein deficiency so far reported in the literature show elevated levels of very long chain fatty acids, branched chain fatty acids and bile acid inter-mediates. In contrast, we now report two novel patients with D-bifunctional protein deficiency who both have normal levels of bile acid intermediates. Complementation analysis and D-bifunctional protein activity measurements revealed that both patients had an isolated defect in the enoyl-CoA hydratase domain of D-bifunctional protein. Subsequent mutation analysis showed that both patients are homozygous for a missense mutation (N457Y), which is located in the enoyl-CoA hydratase coding part of the D-bifunctional protein gene. Expression of the mutant protein in the yeast Saccharomyces cerevisiae confirmed that the N457Y mutation is the disease-causing mutation. Immunoblot analysis of patient fibroblast homogenates showed that the protein levels of full-length D-bifunctional protein were strongly reduced while the enoyl-CoA hydratase component produced after processing within the peroxisome was undetectable, which indicates that the mutation leads to an unstable protein.  (+info)

17beta-hydroxysteroid dehydrogenase (HSD)/17-ketosteroid reductase (KSR) family; nomenclature and main characteristics of the 17HSD/KSR enzymes. (4/334)

A number of enzymes possessing 17beta-hydroxysteroid dehydrogenase/17-ketosteroid reductase (17HSD/KSR) activities have been described and cloned, but their nomenclature needs specification. To clarify the present situation, descriptions of the eight cloned 17HSD/KSRs are given and guidelines for the classification of novel 17HSD/KSR enzymes are presented.  (+info)

Aromatase and sex steroid receptors in human vena cava. (5/334)

Among sex steroids, especially estrogen metabolism has been considered to play a role in the function and pathology of human veins. We investigated the expression and activity of the estrogen-producing enzyme aromatase and estrogen receptor (ER) in human vena cava to assess possible in situ biosynthesis of estrogens and their modes of action. We first examined aromatase expression by immunohistochemistry in human inferior vena cava obtained from 29 autopsy cases (11 males, 18 females, 63.6 +/- 3.0 years old). We then semiquantitated the level of aromatase mRNA by reverse transcriptase-polymerase chain reaction in 24 cases and aromatase activity by 3H-water assay in 15 cases to examine whether or not and in which cell types aromatase was expressed. We also studied alternative use of multiple exon 1s of its gene and immunolocalization of 17beta-hydroxysteroid dehydrogenase type I (17beta-HSD I), which converts estrone produced by aromatase to estradiol, a biologically active estrogen and ER. Aromatase and 17beta-HSD I immunoreactivity were both detected in smooth muscle cells (SMC) of the media in all the cases and in endothelial cells (EC) in 20 and 22 cases, respectively. ER immunoreactivity was detected in SMC of vena cava in 21 cases. The amount of aromatase mRNA was significantly greater in the cases utilizing 1c (I.3) or 1d (P.II) of exon 1 (9 cases, 191.1 +/- 26.3 attomol/ng total RNA) than those utilizing 1b (I.4) as the promoter (14 cases, 50.6 +/- 13.0 attomol/ng total RNA) (p < 0.01). Significant correlation (p < 0.05) was observed between the amount of aromatase mRNA and aromatase activity in 15 cases examined. No significant correlation was detected between the amount of aromatase mRNA or aromatase labeling index and the ER status. These results suggest that estrone and estradiol are produced in the human vena cava and that their production is mediated by aromatase and 17beta-HSD I, respectively but not all of these locally synthesized estrogens may not work directly in situ.  (+info)

Structure and activity of the murine type 5 17beta-hydroxysteroid dehydrogenase gene(1). (6/334)

17beta-Hydroxysteroid dehydrogenases (17beta-HSDs) play a crucial role in the control of active sex steroid intracellular levels. Seven types of 17beta-HSD have been described. In this study, we report the cloning and characterization of the mouse type 5 17beta-HSD belonging to the aldo-keto reductase superfamily, in contrast with types 1, 2, 3, 4, 6, and 7 17beta-HSD which belong to the short-chain alcohol dehydrogenase family. The gene spans 16 kb and contains 9 exons separated by 8 introns. Primer extension analysis identified a major transcription start site beginning 50 nucleotides upstream from the ATG initiation codon. Northern blot analysis showed a high mRNA expression level in the liver and a weaker signal in the kidney. To determine more precisely the substrate specificity of the enzyme, we established a stable cell line expressing mouse type 5 17beta-HSD in transformed human embryonic kidney (293) cells. The transfected cell line preferentially catalyzes the transformation of 4-androstenedione (4-dione) and androstanedione (A-dione) into testosterone (T) and dihydrotestosterone (DHT), respectively. This data is somewhat in contradiction with a previous study that described the enzyme as estradiol 17beta-dehydrogenase. Our results indicate that the rate of transformation of estradiol (E(2)) to estrone (E(1)) represents only 1% of the rate of transformation of 4-dione to T. Mouse type 5 17beta-HSD shares 76% amino acid sequence identity with human type 5 17beta-HSD; 71%, 76%, 76% with rat 3alpha-HSD and human types 1 and 3 3alpha-HSDs, respectively; and 71%, 69% and 77% with mouse, rat and human 20alpha-HSD, respectively.  (+info)

Determination of cDNA, gene structure and chromosomal localization of the novel human 17beta-hydroxysteroid dehydrogenase type 7(1). (7/334)

We have identified human 17beta-hydroxysteroid dehydrogenase type 7 (17beta-HSD 7). The novel human cDNA encodes a 37 kDa protein that shows 78 and 74% amino acid identity with rat and mouse 17beta-HSD 7, respectively. These enzymes are responsible for estradiol production in the corpus luteum during pregnancy, but are also present in placenta and several steroid target tissues (breast, testis and prostate) as revealed by RT-PCR. The human 17beta-HSD 7 gene (HSD17B7) consists of nine exons and eight introns, spanning 21. 8 kb and maps to chromosome 10p11.2 close to susceptibility loci for tumor progression, obesity and diabetes. The HSD17B7 promoter (1.2 kb) reveals binding sites for brain-specific and lymphoid transcription factors corresponding to additional expression domains in hematopoietic tissues and the developing brain as identified by in silico Northern blot.  (+info)

In vivo and in vitro expression of steroid-converting enzymes in human breast tumours: associations with interleukin-6. (8/334)

Enzymes modulating local steroid availability play an important role in the progression of human breast cancer. These include isoforms of 17beta-hydroxysteroid dehydrogenase (17-HSD), aromatase and steroid sulphatase (STS). The aim of this study was to investigate the expression, by reverse transcription polymerase chain reaction, of 17-HSD types I-IV, aromatase and steroid STS in a series of 51 human breast tumour biopsies and 22 primary cultures of epithelial and stromal cells derived from these tumours, giving a profile of the steroid-regulating network for individual tumours. Correlations between enzyme expression profiles and expression of the interleukin (IL)-6 gene were also sought. All except one tumour expressed at least one isoform of 17-HSD, either alone or in combination with aromatase and STS. Expression of 17-HSD isoforms I-IV were observed in nine tumours. Of the 15 tumours which expressed three isoforms, a combination of 17-HSD II, III and IV was most common (6/15 samples). The majority of tumours (n = 17) expressed two isoforms of 17-HSD with combinations of 17-HSD II and IV predominant (7/17 samples). Eight tumours expressed a single isoform and of these, 17-HSD I was in the majority (5/8 samples). In primary epithelial cultures, enzyme expression was ranked: HSD I (86%) > STS (77%) > HSD II (59%) > HSD IV (50%) = aromatase (50%) > HSD III (32%). Incidence of enzyme expression was generally reduced in stromal cultures which were ranked: HSD I (68%) > STS (67%) > aromatase (48%) > HSD II (43%) > HSD IV (28%) > HSD III (19%). Expression of IL-6 was associated with tumours that expressed > or = 3 steroid-converting enzymes. These tumours were of higher grade and tended to come from patients with family history of breast cancer. In conclusion, we propose that these enzymes work in tandem with cytokines thereby providing sufficient quantities of bioactive oestrogen from less active precursors which stimulates tumour growth.  (+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.

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).

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

"HSD17B3 hydroxysteroid 17-beta dehydrogenase 3 [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2017-03- ... Retrieved 2017-03-17. Lee P. A.; Houk C. P.; Ahmed S. F.; Hughes I. A. (2006). "Consensus statement on management of intersex ... 17-β-Hydroxysteroid dehydrogenase III deficiency is a cause of 46,XY disorder of sex development (46,XY DSD) that presents in ... 17β-Hydroxysteroid dehydrogenase III deficiency is caused by mutations found in the 17β-HSD III (17BHSD3) gene.17β-HSD III ...
Has 3α-HSDTooltip 3α-hydroxysteroid dehydrogenase and 20α-HSDTooltip 20α-hydroxysteroid dehydrogenase activity in addition to ... Aka JA, Mazumdar M, Chen CQ, Poirier D, Lin SX (April 2010). "17beta-hydroxysteroid dehydrogenase type 1 stimulates breast ... Talalay P, Dobson MM (December 1953). "Purification and properties of a beta-hydroxysteroid dehydrogenase". The Journal of ... ISBN 978-0-12-803608-2. Moeller G, Adamski J (2009). "Integrated view on 17beta-hydroxysteroid dehydrogenases". Mol. Cell. ...
... alpha-hydroxysteroid+dehydrogenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology v t ... alpha-hydroxysteroid dehydrogenase (EC 1.1.1.209, 3(17)alpha-hydroxysteroid dehydrogenase) is an enzyme with systematic name 3( ... alpha-hydroxysteroid dehydrogenase of female rabbit kidney cytosol. Purification and characterization of multiple forms of the ... alpha-hydroxysteroid dehydrogenases of female rabbit kidney and liver". The Journal of Biological Chemistry. 257 (16): 9450-6. ...
This enzyme is also called 16alpha-hydroxy steroid dehydrogenase. Meigs RA, Ryan KJ (1966). "16-alpha-hydroxysteroid ... In enzymology, a 16alpha-hydroxysteroid dehydrogenase (EC 1.1.1.147) is an enzyme that catalyzes the chemical reaction a ... The systematic name of this enzyme class is 16alpha-hydroxysteroid:NAD(P)+ 16-oxidoreductase. ... H+ The 3 substrates of this enzyme are 16alpha-hydroxysteroid, NAD+, and NADP+, whereas its 4 products are 16-oxosteroid, NADH ...
20-hydroxysteroid dehydrogenase, dehydrogenase, 20beta-hydroxy steroid, Delta4-3-ketosteroid hydrogenase, 20beta-hydroxysteroid ... dehydrogenase, 3alpha,20beta-hydroxysteroid:NAD+-oxidoreductase, NADH-20beta-hydroxysteroid dehydrogenase, and 20beta-HSD. This ... In enzymology, a 3alpha(or 20beta)-hydroxysteroid dehydrogenase (EC 1.1.1.53) is an enzyme that catalyzes the chemical reaction ... Edwards CA, Orr JC (1978). "Comparison of the 3α- and 20β-Hydroxysteroid Dehydrogenase Activities of the Cortisone Reductase of ...
Steroidogenic enzyme 11β-Hydroxysteroid dehydrogenase type 1 11β-Hydroxysteroid dehydrogenase type 2 Cortisone reductase ... Effect of Hyperlipidemia on 11β-hydroxysteroid-dehydrogenase Hyperlipidemia has a great effect on 11β-hydroxysteroid- ... 11β-Hydroxysteroid dehydrogenase (HSD-11β or 11β-HSD) enzymes catalyze the conversion of inert 11 keto-products (cortisone) to ... The dehydrogenase activity of a HSD-11β converts a 11beta-hydroxysteroid to the corresponding 11-oxosteroid by reducing NADP+ ...
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 ... In enzymology, a 20-α-hydroxysteroid dehydrogenase (EC 1.1.1.149) is an enzyme that catalyzes the chemical reaction 17alpha, ... Hershkovitz L, Beuschlein F, Klammer S, Krup M, Weinstein Y (March 2007). "Adrenal 20alpha-hydroxysteroid dehydrogenase in the ...
17beta-hydroxy steroid dehydrogenase, 3alpha(17beta)-HSD, and 3alpha(17beta)-hydroxysteroid dehydrogenase (NAD+). This enzyme ... hydroxysteroid dehydrogenase distinct from 3α-hydroxysteroid dehydrogenase in hamster liver". Biochem. J. 266 (2): 583-9. PMC ... In enzymology, a 3alpha(17beta)-hydroxysteroid dehydrogenase (NAD+) (EC 1.1.1.239) is an enzyme that catalyzes the chemical ... The systematic name of this enzyme class is 3alpha(or 17beta)-hydroxysteroid:NAD+ oxidoreductase. Other names in common use ...
Poirier D (2009). "Advances in development of inhibitors of 17beta hydroxysteroid dehydrogenases". Anticancer Agents Med Chem. ... "Spironolactone-related inhibitors of type II 17beta-hydroxysteroid dehydrogenase: chemical synthesis, receptor binding ... Soubhye J, Alard IC, van Antwerpen P, Dufrasne F (2015). "Type 2 17hydroxysteroid dehydrogenase as a novel target for the ... 34 (5): 405-17. doi:10.2165/00003088-199834050-00005. PMID 9592622. S2CID 25200595. Shlomo Melmed (2016). Williams Textbook of ...
It acts as a pH indicator in the range 6.5-8.9.[citation needed] Umbelliferone is a potent inhibitor of type 3 17β- ... hydroxysteroid dehydrogenase, the primary enzyme responsible for the conversion of 4-androstene-3,17-dione to testosterone, ... ISBN 978-81-88237-33-3. Poirier, Donald (Mar 2003). "Inhibitors of 17 beta-hydroxysteroid dehydrogenases". Curr Med Chem. 10 (6 ...
Roe CR, Kaplan NO (1969). "Purification and substrate specificities of bacterial hydroxysteroid dehydrogenases". Biochemistry. ... Other names in common use include etiocholanolone 3alpha-dehydrogenase, etiocholanolone 3alpha-dehydrogenase, and 3alpha- ... hydroxy-5beta-steroid dehydrogenase. This enzyme participates in androgen and estrogen metabolism. ... In enzymology, a 3alpha-hydroxy-5beta-androstane-17-one 3alpha-dehydrogenase (EC 1.1.1.152) is an enzyme that catalyzes the ...
Corticosteroid 11-β-dehydrogenase isozyme 2 also known as 11-β-hydroxysteroid dehydrogenase 2 is an enzyme that in humans is ... "Entrez Gene: HSD11B2 hydroxysteroid (11-beta) dehydrogenase 2". Geerling, Joel C.; Arthur D. Loewy (September 2009). " ... 2005). "11beta-hydroxysteroid dehydrogenase type 1: a tissue-specific regulator of glucocorticoid response". Endocr. Rev. 25 (5 ... 1998). "A new compound heterozygous mutation in the 11 beta-hydroxysteroid dehydrogenase type 2 gene in a case of apparent ...
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; ... DCX Succinic semialdehyde dehydrogenase deficiency; 271980; ALDH5A1 Succinyl-CoA:3-oxoacid CoA transferase deficiency; 245050; ... PLI Alpha-ketoglutarate dehydrogenase deficiency; 203740; OGDH Alpha-methylacetoacetic aciduria; 203750; ACAT1 Alpha- ...
17 (6): 754-9. doi:10.1210/jcem-17-6-754. PMID 13428841. Wein AJ, Kavoussi LR, Novick AC, Partin AW, Peters CA (25 August 2011 ... 17α-Hydroxyprogesterone caproate is a depot progestogen which is entirely free of side actions. The dose required to induce ... However, a higher 17-OHP level was observable at the completion of OMP administration (week 2). Sitruk-Ware R (2002). " ... 231 (17): 3557-67. doi:10.1007/s00213-014-3599-x. PMC 4135022. PMID 24846476. Bäckström T, Haage D, Löfgren M, Johansson IM, ...
17beta-hydroxysteroid dehydrogenase 4 and D-3-hydroxyacyl-coenzyme A dehydrogenase/hydratase involved in Zellweger syndrome". ... Green VL, Speirs V, Landolt AM, Foy PM, Atkin SL (April 1999). "17Beta-hydroxysteroid dehydrogenase type 1, 2, 3, and 4 ... Dong Y, Qiu QQ, Debear J, Lathrop WF, Bertolini DR, Tamburini PP (October 1998). "17Beta-hydroxysteroid dehydrogenases in human ... "Structure of the gene for the human 17beta-hydroxysteroid dehydrogenase type IV". Mammalian Genome. 9 (12): 1036-41. doi: ...
1998). "Characterization of Ke 6, a new 17beta-hydroxysteroid dehydrogenase, and its expression in gonadal tissues". J. Biol. ... 2007). "Transcriptional regulation of the human type 8 17beta-hydroxysteroid dehydrogenase gene by C/EBPbeta". J. Steroid ... 2006). "Expression of aromatase and 17beta-hydroxysteroid dehydrogenase types 1, 7 and 12 in breast cancer. An ... "Entrez Gene: HSD17B8 hydroxysteroid (17-beta) dehydrogenase 8". Kikuti YY, Tamiya G, Ando A, et al. (1997). "Physical mapping ...
Aka JA, Mazumdar M, Chen CQ, Poirier D, Lin SX (Apr 2010). "17beta-hydroxysteroid dehydrogenase type 1 stimulates breast cancer ... "Structural basis of the multispecificity demonstrated by 17beta-hydroxysteroid dehydrogenase types 1 and 5". Molecular and ... "Entrez Gene: HSD17B1 Hydroxysteroid (17-beta) dehydrogenase 1". Saloniemi T, Jokela H, Strauss L, Pakarinen P, Poutanen M (2012 ... This enzyme contains a short-chain dehydrogenase domain that contains a characteristic 3-layer (αβα) sandwich known as a ...
"Deleterious missense mutations and silent polymorphism in the human 17beta-hydroxysteroid dehydrogenase 3 gene (HSD17B3)". The ... "Phenotypic variability in 17beta-hydroxysteroid dehydrogenase-3 deficiency and diagnostic pitfalls". Clinical Endocrinology. 67 ... "Entrez Gene: HSD17B3 hydroxysteroid (17-beta) dehydrogenase 3". "Testosterone 17-beta-dehydrogenase deficiency - Conditions - ... short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative". Chemico-Biological Interactions. 178 (1-3): ...
"Cloning and expression of a novel tissue specific 17beta-hydroxysteroid dehydrogenase". Endocrine Research. 24 (3-4): 663-7. ... "Entrez Gene: HSD17B11 hydroxysteroid (17-beta) dehydrogenase 11". Li KX, Smith RE, Krozowski ZS (1999). " ... Haeseleer F, Palczewski K (2000). Short-chain dehydrogenases/reductases in retina. Methods in Enzymology. Vol. 316. pp. 372-83 ... short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative". Chemico-Biological Interactions. 178 (1-3): ...
Peltoketo H, Nokelainen P, Piao YS, Vihko R, Vihko P (Aug 1999). "Two 17beta-hydroxysteroid dehydrogenases (17HSDs) of ... Ohnesorg T, Adamski J (2005). "Promoter analyses of human and mouse 17beta-hydroxysteroid dehydrogenase type 7". J. Steroid ... 2003). "Production, purification, and functional analysis of recombinant human and mouse 17beta-hydroxysteroid dehydrogenase ... gene structure and chromosomal localization of the novel human 17beta-hydroxysteroid dehydrogenase type 7(1)". FEBS Lett. 460 ( ...
"Characterization of type 12 17beta-hydroxysteroid dehydrogenase, an isoform of type 3 17beta-hydroxysteroid dehydrogenase ... 2006). "Systemic distribution and tissue localizations of human 17beta-hydroxysteroid dehydrogenase type 12". J. Steroid ... 2005). "Platelets express steroidogenic 17beta-hydroxysteroid dehydrogenases. Distinct profiles predict the essential ... "Entrez Gene: HSD17B12 hydroxysteroid (17-beta) dehydrogenase 12". Maruyama K, Sugano S (1994). "Oligo-capping: a simple method ...
... reductase Δ5-3β-hydroxysteroid dehydrogenase 3β-hydroxy-5-ene steroid dehydrogenase 3β-hydroxy steroid dehydrogenase/isomerase ... steroid-Δ5-3β-ol dehydrogenase 3β-HSDH 5-ene-3β-hydroxysteroid dehydrogenase 3β-hydroxy-5-ene-steroid dehydrogenase 3β-HSD is ... 3β-Hydroxysteroid dehydrogenase/Δ5-4 isomerase (3β-HSD) (EC 1.1.1.145) is an enzyme that catalyzes the biosynthesis of the ... Steroidogenic enzyme 3α-Hydroxysteroid dehydrogenase Cravioto MD, Ulloa-Aguirre A, Bermudez JA, Herrera J, Lisker R, Mendez JP ...
... possesses the combined activities of the 3-β-hydroxysteroid dehydrogenase/Δ-5-4 isomerase and 20-α-hydroxysteroid dehydrogenase ... In enzymology, a 3-β(or 20-α)-hydroxysteroid dehydrogenase (EC 1.1.1.210) is an enzyme that catalyzes the chemical reaction 5α- ... Sharaf MA, Sweet F (September 1982). "Dual activity at an enzyme active site: 3 beta,20 alpha-hydroxysteroid oxidoreductase ... androstan-3β,17β-diol + NADP+ ⇌ {\displaystyle \rightleftharpoons } 17β-hydroxy-5α-androstan-3-one + NADPH + H+ This enzyme ...
In enzymology, a 3alpha-hydroxysteroid dehydrogenase (A-specific) (EC 1.1.1.213) is an enzyme that catalyzes the chemical ... Tomkins GM (1956). "A mammalian 3alpha-hydroxysteroid dehydrogenase". J. Biol. Chem. 218 (1): 437-447. PMID 13278351. Portal: ... more specifically it is part of the group of hydroxysteroid dehydrogenases. The systematic name of this enzyme class is 3alpha- ... transfer from pyridine nucleotides catalyzed by delta-4-3-oxosteroid 5-beta-reductase and 3-alpha-hydroxysteroid dehydrogenase ...
Penning TM, Sharp RB (1987). "Prostaglandin dehydrogenase activity of purified rat liver 3 alpha-hydroxysteroid dehydrogenase ... In enzymology, a 3alpha-hydroxysteroid dehydrogenase (B-specific) (EC 1.1.1.50) is an enzyme that catalyzes the chemical ... Marcus PI; Talalay P (1956). "Induction and purification of alpha- and beta-hydroxysteroid dehydrogenases". J. Biol. Chem. 218 ... more specifically it is part of the group of hydroxysteroid dehydrogenases. The systematic name of this enzyme class is 3alpha- ...
Steroidogenic enzyme 3α-hydroxysteroid dehydrogenase type 3 3β-Hydroxysteroid dehydrogenase GRCh38: Ensembl release 89: ... 3-alpha hydroxysteroid dehydrogenase, type I; dihydrodiol dehydrogenase 4)". Rizner TL, Lin HK, Peehl DM, Steckelbroeck S, ... 3α-Hydroxysteroid dehydrogenase (3α-HSD or aldo-keto reductase family 1 member C4) is an enzyme that in humans is encoded by ... Khanna M, Qin KN, Cheng KC (June 1995). "Distribution of 3 alpha-hydroxysteroid dehydrogenase in rat brain and molecular ...
Baker ME (Feb 2001). "Evolution of 17beta-hydroxysteroid dehydrogenases and their role in androgen, estrogen and retinoid ... 2001). "Further characterization of human microsomal 3alpha-hydroxysteroid dehydrogenase". Arch. Biochem. Biophys. 386 (1): 1- ... 2007). "Role of microsomal retinol/sterol dehydrogenase-like short-chain dehydrogenases/reductases in the oxidation and ... and 3alpha-hydroxysteroid dehydrogenases from rat and human prostate". J. Biol. Chem. 272 (25): 15959-66. doi:10.1074/jbc. ...
... glucose-6-phosphate dehydrogenase (G6PD) deficiency, congenital adrenal hyperplasia, methyl coenzyme dehydrogenase deficiency ... glucose-6-phosphate dehydrogenase deficiency, and fragile X syndrome (FXS), which is an inherited genetic condition with ... glucose-6-phosphate dehydrogenase) deficiency are the most common in the Arab population. Familial transthyretin amyloidosis ... glucose-6-phosphate dehydrogenase deficiency, alpha-thalassemia, molecular characterization, recessive osteoperosis, ...
Hastings C, Hansson V (August 1981). "Kinetic properties of the soluble 3 alpha-hydroxysteroid dehydrogenase from rat testis ... 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 ... 5α-Pregnan-17α-ol-3,20-dione is produced by 5α-reduction of 17-OHP. The reaction is catalyzed by SRD5A1 and possibly, SRD5A2 ... 5α-Pregnan-17α-ol-3,20-dione, also known as 17α-hydroxy-dihydroprogesterone (17‐OH-DHP) is an endogenous steroid, a metabolite ...
17β-Hydroxysteroid dehydrogenase type 14 also known as 17β-HSD type 14 or 17βHSD14 is an enzyme that in humans is encoded by ... 17βHSD14 catalyzes the stereospecific oxidation and reduction of the 17β carbon atom of androgens and estrogens using NAD(P)(H ... 257-. ISBN 978-1-118-84985-9. Sivik T, Vikingsson S, Gréen H, Jansson A (2012). "Expression patterns of 17β-hydroxysteroid ... dehydrogenase 14 in human tissues". Hormone and Metabolic Research. 44 (13): 949-56. doi:10.1055/s-0032-1321815. PMID 22864907 ...
"HSD17B3 hydroxysteroid 17-beta dehydrogenase 3 [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2017-03- ... Retrieved 2017-03-17. Lee P. A.; Houk C. P.; Ahmed S. F.; Hughes I. A. (2006). "Consensus statement on management of intersex ... 17-β-Hydroxysteroid dehydrogenase III deficiency is a cause of 46,XY disorder of sex development (46,XY DSD) that presents in ... 17β-Hydroxysteroid dehydrogenase III deficiency is caused by mutations found in the 17β-HSD III (17BHSD3) gene.17β-HSD III ...
17-beta hydroxysteroid dehydrogenase 3 deficiency is a condition that affects male sexual development. Explore symptoms, ... 17beta-Hydroxysteroid dehydrogenase-3 deficiency: from pregnancy to adolescence. J Endocrinol Invest. 2009 Sep;32(8):666-70. ... The 17beta-hydroxysteroid dehydrogenase type 3 deficiency: a case report of an 18-year patient and review of the literature. ... due to 17beta-hydroxysteroid dehydrogenase type 3 deficiency. J Steroid Biochem Mol Biol. 2017 Jan;165(Pt A):79-85. doi: ...
hepatic retinol/retinal dehydrogenase. short chain dehydrogenase/reductase family 16C member 3. short-chain dehydrogenase/ ... hydroxysteroid 17-beta dehydrogenase 13provided by HGNC. Primary source. HGNC:HGNC:18685 See related. Ensembl:ENSG00000170509 ... DltE; Short-chain dehydrogenase [General function prediction only]. * NM_178135.5 → NP_835236.2 17-beta-hydroxysteroid ... HSD17B13 hydroxysteroid 17-beta dehydrogenase 13 [ Homo sapiens (human) ] Gene ID: 345275, updated on 23-Nov-2023 ...
beta-hydroxyacyl dehydrogenase. beta-keto-reductase. epididymis secretory sperm binding protein. hydroxysteroid dehydrogenase 4 ... hydroxysteroid dehydrogenase 4 induces liver cancer proliferation‑associated genes via STAT3 activation. ... hydroxysteroid 17-beta dehydrogenase 4provided by HGNC. Primary source. HGNC:HGNC:5213 See related. Ensembl:ENSG00000133835 MIM ... hydroxyacyl-CoA-like_DH_SDR_c-like; (3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs. PRK05653. Location:6 → 208 ...
Hydroxysteroid (17 beta) Dehydrogenase 4 (HSD17B4) Mouse Monoclonal Antibody [Clone ID: OTI4C4]. ... Recombinant protein of human hydroxysteroid (17-beta) dehydrogenase 4 (HSD17B4), 20 µg ...
Studie über die Genregulation der Expression der 3alpha-Hydroxysteroid-Dehydrogenase im Bakterium Comamonas testosteroni by: ... Carbonyl Reductases and Pluripotent HydroxysteroidDehydrogenases of the Short-Chain Dehydrogenase/ReductaseSuperfamily: ... So konnten Inhibitoren für die 17β-HSDs 1, 2 und 3 entwickelt werden, mit denen nach der in vivo Verabreichung ein „proof of ... 17β-HSDs besitzen die Fähigkeit lokale Konzentrationen von aktiven und inaktiven Hormonderivaten in bestimmten Gewebearten nach ...
β hydroxysteroid dehydrogenase type 6(HSD17B6) in samples from blood, plasma, serum, cell culture supernatant and other ... β hydroxysteroid dehydrogenase type 6(HSD17B6) in samples from blood, plasma, serum, cell culture supernatant and other ... β hydroxysteroid dehydrogenase type 6(HSD17B6) in samples from blood, plasma, serum, cell culture supernatant and other ... β hydroxysteroid dehydrogenase type 6(HSD17B6) in samples from blood, plasma, serum, cell culture supernatant and other ...
3-beta-hydroxysteroid dehydrogenase (3BHSD) deficiency is a rare genetic disorder of steroid biosynthesis that results in ... 3-Beta-Hydroxysteroid Dehydrogenase Deficiency. 3-beta-hydroxysteroid dehydrogenase (3BHSD) is required for the synthesis of ... 3-Beta-Hydroxysteroid Dehydrogenase Deficiency. 3-beta-hydroxysteroid dehydrogenase (3BHSD) is required for the synthesis of ... Type I 3-beta-hydroxysteroid dehydrogenase isoenzyme is normal in patients with type II 3-beta-hydroxysteroid dehydrogenase ...
... dehydrogenase",. author = "Day, {Joanna M.} and Tutill, {Helena J.} and Foster, {Paul A.} and Bailey, {Helen V.} and Heaton, { ... 17β-HSD Type 3 (17β-HSD3) has been seen to be over-expressed in prostate cancer, and catalyses the reduction of androstenedione ... 17β-HSD Type 3 (17β-HSD3) has been seen to be over-expressed in prostate cancer, and catalyses the reduction of androstenedione ... 17β-HSD Type 3 (17β-HSD3) has been seen to be over-expressed in prostate cancer, and catalyses the reduction of androstenedione ...
Crystal structure of a 17beta-hydroxysteroid dehydrogenase (holo form) from fungus Cochliobolus lunatus in complex with NADPH ... Structural studies on the flavonoid inhibition of a fungal 17Beta-Hydroxysteroid dehydrogenase. Cassetta, A., Krastanova, I., ... Crystal structure of a 17beta-hydroxysteroid dehydrogenase (holo form) from fungus Cochliobolus lunatus in complex with NADPH ... short-chain dehydrogenase/reductase) superfamily. It is currently the only fungal 17β-HSD member that has been described and ...
What does hydroxysteroid dehydrogenase do?. Hydroxysteroid dehydrogenases (HSDs) or oxidoreductases catalyze the ... What does 11 beta hydroxysteroid dehydrogenase do?. 11 beta-HSD2 is a high affinity NAD-dependent dehydrogenase that protects ... 11β-Hydroxysteroid dehydrogenase (HSD-11β or 11β-HSD) enzymes catalyze the conversion of inert 11 keto-products (cortisone) to ... What is 17b hydroxysteroid dehydrogenase?. The HSD17B3 gene provides instructions for making an enzyme called 17-beta ...
17b-hydroxysteroid dehydrogenase (HSD) is a steroidogenic enzyme essential for invertebrate spermatogenesis. A homologue of HSD ... 17b-hydroxysteroid dehydrogenase (HSD) is a steroidogenic enzyme essential for invertebrate spermatogenesis. A homologue of HSD ... EST Cloning and Expression of 17β-Hydroxysteroid Dehydrogenase in the Ascidian, Ciona intestinalis Testis. Kang Hee Kho ... EST Cloning and Expression of 17β-Hydroxysteroid Dehydrogenase in the Ascidian, Ciona intestinalis Testis. Kang Hee Kho ...
3-β hydroxysteroid dehydrogenase/isomerase. Steroid metabolism. 17. (26). group_273. Recombinase/resolvase. Mobile genetic ... NADH-dependent dehydrogenase. Putative functions. 26. NA. nmrA. Putative nmrA negative transcriptional regulator family protein ...
STX2171 is a novel selective non-steroidal 17β-HSD3 inhibitor with an IC(50) of ∼200 nM in a whole-cell assay. It inhibits ... 17β-Hydroxysteroid dehydrogenases (17β-HSDs) catalyse the 17-position reduction/oxidation of steroids. 17β-HSD type 3 (17β-HSD3 ... indicating that 17β-HSD3 inhibitors may have application in the treatment of hormone-dependent prostate cancer. ... suggesting that specific inhibitors of 17β-HSD3 may have a role in the treatment of hormone-dependent prostate cancer and ...
Acyl-CoA Dehydrogenase-9 (ACAD9) deficiency: ACAD9* , MetaboSeq , Test Requisition. *Barth Syndrome: TAZ* , MetaboSeq , Test ... Short-chain acyl-CoA dehydrogenase (SCAD) deficiency: ACADS* , MetaboSeq , Test Requisition. *Very-long-chain acyl-CoA ... Medium-chain acyl-CoA dehydrogenase (MCAD) deficiency: ACADM , MetaboSeq , Test Requisition. *Multiple Acyl-CoA Dehydrogenation ... Long-chain 3-hydroxyacyl-CoA dehydrogenase (LCHAD) deficiency: HADHA , HADHB* , MetaboSeq , Test Requisition ...
3-beta-hydroxysteroid dehydrogenase [3-beta-HSD]; CYP11A1; CYP17A1; 17-beta-hydroxysteroid dehydrogenase [17-beta-HSD]), and ... 17-alpha-hydroxylase/C17,20-lyase [CYP17A1]; low saccharin: StAR). Moreover, a high-dose saccharin-related decline in ...
Key enzyme: 3-B-Hydroxysteroid Dehydrogenase. * Progesterone converted to 17-a-hydroxyprogesterone. *Key enzyme: 17-Hydroxylase ... 17-a-hydroxyprogesterone converted to 11-Deoxycortisol. *Key enzyme: 21-Hydroxylase. *Most common enzyme deficiency in steroid ... 17-a-hydroxyprogesterone converted to Androstenedione. *Key enzyme: 3-B-Hydroxysteroid Dehydrogenase ... V. Physiology: Step 2 (Cortisol Synthesis from 17-a-hydroxyprogesterone) * ...
It is a conjugated steroid converted by the sulfation of dehydroepiandrosterone (DHEA) at the 3β position via hydroxysteroid ... 17α-hydroxyprogesterone (ng/dL). Target: Both males and females 6 YEARS - 150 YEARS. Code or Value. Value Description. Count. ... 17α-hydroxyprogesterone (nmol/L). Target: Both males and females 6 YEARS - 150 YEARS. Code or Value. Value Description. Count. ... 17α-hydroxyprogesterone Comment Code. Target: Both males and females 6 YEARS - 150 YEARS. Code or Value. Value Description. ...
The enzymatic defects causing female virilization involve 3β-hydroxysteroid dehydrogenase Δ5-Δ4 isomerase (3β-HSD), P450C21 ... 3β-Hydroxylase dehydrogenase is exceptional.. Prenatal diagnosis of these defects is possible in high-risk families and ... 17β-Hydroxysteroid Dehydrogenase (17β-HSD) Deficiency. Type 3 17β-HSD deficiency is a rare autosomal recessive cause of male ... 17α-Hydroxylase Deficiency. Defects in P450C17 lead to male pseudohermaphroditism with various degrees of ambiguous genitalia. ...
Analyses of the mitochondrial hydroxysteroid dehydrogenase (HSD17B10) uncover the RNA-binding specificity of an enigmRBP. RNA- ... A non-enzymatic function of 17beta-hydroxysteroid dehydrogenase type 10 is required for mitochondrial integrity and cell ... Analyses of the mitochondrial hydroxysteroid dehydrogenase (HSD17B10) uncover the RNA-binding specificity of an enigmRBP. ... hydroxysteroid dehydrogenase 17B 10, c11orf68, chromosome 11 open reading frame 68, CRKL, v-crk avian sarcoma virus CT10 ...
to estradiol by 17β-hydroxysteroid dehydrogenase. Smaller amounts of estradiol are also produced by the adrenal cortex. Adrenal ... Estrogen receptor refers to a group of receptors that are activated by the hormone 17β-estradiol . Two types of estrogen ... Estrogen receptor refers to a group of receptors that are activated by the hormone 17β-estradiol . Two types of estrogen ...
hydroxysteroid dehydrogenase-like protein 2 isoform X1 77. - - 59.1. 8 N-acetyltransferase Eis ...
3-beta-hydroxysteroid dehydrogenase type II deficiency. HSD3B2. CNV. Hydrolethalus syndrome. HYLS1. CNV. ... Short chain acyl-CoA dehydrogenase deficiency. ACADS. CNV. Short/branched chain acyl-CoA dehydrogenase deficiency. ACADSB. CNV ... Medium chain acyl-CoA dehydrogenase deficiency. ACADM. CNV. ... Very long chain acyl-CoA dehydrogenase deficiency. ACADVL. CNV ...
2004 Aug;17(8):1125-32. [PubMed:15379426 ] *Michaud DS, Manson JE, Spiegelman D, Barbieri RL, Sepkovic DW, Bradlow HL, ... InChI=1S/C18H22O5S/c1-18-9-8-14-13-5-3-12(23-24(20,21)22)10-11(13)2-4-15(14)16(18)6-7-17(18)19/h3,5,10,14-16H,2,4,6-9H2,1H3,(H, ... InChI=1S/C18H22O5S/c1-18-9-8-14-13-5-3-12(23-24(20,21)22)10-11(13)2-4-15(14)16(18)6-7-17(18)19/h3,5,10,14-16H,2,4,6-9H2,1H3,(H, ... Other potential substrates, such as triiodothyronine (T3), 17-beta-glucuronosyl estradiol, estrone-3-sulfate and ...
... hydroxysteroid dehydrogenase; 5-r, 5-reductase; 3a-, 3-diol, 3-androstenediol, 3-androstenediol; 3a-, 3-diol-G, 3-diol- ... glucuronide, 3-diol-glucuronide; androsterone-G, androsterone glucorunide; ar, aromatase; E1, estrone; E2, estradiol-17. ...
dihydrodiol dehydrogenase (dimeric). Tssr72411. 7. 45474276 to 45474299 23. -. TSS region. transcription start site region ... hydroxysteroid (17-beta) dehydrogenase 14. Tssr66561. 7. 45554915 to 45554922 7. +. TSS region. transcription start site region ... 17. -. TSS region. transcription start site region 72400. Tssr66542. 7. 45461064 to 45461100 36. +. TSS region. transcription ... 17. +. TSS region. transcription start site region 66554. Tssr66555. 7. 45526531 to 45526534 3. +. TSS region. transcription ...
There are two subtypes of 17β-HSD: type 1 catalyzes E1 to E2, and type 2 preferentially catalyzes the oxidation of E2 to E1 [3 ... The enzyme 17β-hydroxysteroid dehydrogenase (17β-HSD) catalyzes reversible inter- conversion of E1 and E2. STS is responsible ... 2012) Overexpression of 17β-Hydroxysteroid Dehydrogenase Type 1 Increases the Exposure of Endometrial Cancer to 17β-Estradiol. ... Although STS and Estrogen sulfotransferase (EST) activities have been examined in estrogen-dependent neoplasms [17] [18] , STS- ...
3β-hydroxysteroid dehydrogenase (3β2-HSD); 17β-HSD = 17β-hydroxysteroid dehydrogenase (17β-HSD); SCC = side-chain cleavage (P- ... 11β = 11β-hydroxylase (P-450c11); 17α = 17α-hydroxylase (P-450c17); 17,20 = 17,20 lyase (P-450c17); 18 = aldosterone synthase ( ... The deficiency completely or partially blocks conversion of 17-hydroxyprogesterone to 11-deoxycortisol, a precursor of cortisol ... Routine newborn screening typically includes measuring serum levels of 17-hydroxyprogesterone. If levels are elevated, the ...
Purification and properties of 3 alpha-hydroxysteroid dehydrogenase from rat brain cytosol. Inhibition by nonsteroidal anti- ... Provera administered in vivo had no effect on either dehydrogenase activity in soluble estradiol receptor-poor carcinomata, ... Examination of a variety of steroidal contraceptives as modulators of the dehydrogenase indicates that ethinylestradiol is a ... whereas both dehydrogenase activities were high in some but not all soluble estradiol receptor-rich tumors [13]. ...
Osteoblastic 11beta-hydroxysteroid dehydrogenase type 1 activity increases with age and glucocorticoid exposure. J Bone Miner ... 11beta-Hydroxysteroid dehydrogenase: a regulator of glucocorticoid response in osteoporosis. J Endocrinol Invest. 2008;31:16-21 ... Expression and functional consequences of 11beta-hydroxysteroid dehydrogenase activity in human bone. Bone. 2000;27:375-81 ... 11beta-Hydroxysteroid dehydrogenase type 1 selective inhibitor BVT.2733 protects osteoblasts against endogenous glucocorticoid ...
  • The autosomal recessive deficiency arises are a result of homozygous or compound heterozygous mutations in HSD17B3 gene which encodes the 17β-hydroxysteroid dehydrogenase III enzyme, impairing of the conversion of 17-keto into 17-hydroxysteroids. (wikipedia.org)
  • The HSD17B3 gene provides instructions for making an enzyme called 17-beta hydroxysteroid dehydrogenase 3. (medlineplus.gov)
  • Mutations in the HSD17B3 gene result in a 17-beta hydroxysteroid dehydrogenase 3 enzyme with little or no activity, reducing production of testosterone from androstenedione. (medlineplus.gov)
  • 17β-HSDs besitzen die Fähigkeit lokale Konzentrationen von aktiven und inaktiven Hormonderivaten in bestimmten Gewebearten nach dem intrakrinen Konzept regulieren zu können.1 Demnach können sie als molekulare Schalter betrachtet werden, die als Prärezeptorregulatoren auf die Funktion von Steroidhormonen wirken, bevor sie an die entsprechenden Rezeptoren angreifen.2,3 Die Blockade dieser Enzyme durch potente und selektive Inhibitoren kann daher ein vielversprechender therapeutischer Ansatz zur Behandlung von steroidhormonabhängigen Erkrankungen sein. (uni-marburg.de)
  • 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)
  • 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)
  • The 17β-HSD (17β-hydroxysteroid dehydrogenase) from the filamentous fungus Cochliobolus lunatus (17β-HSDcl) is a NADP(H)-dependent enzyme that preferentially catalyses the interconversion of inactive 17-oxo-steroids and their active 17β-hydroxy counterparts. (rcsb.org)
  • The enzyme 11-beta-hydroxysteroid dehydrogenase (EC 1.1. (richardvigilantebooks.com)
  • Licorice influences cortisol production by inhibiting the enzyme 11-beta-hydroxysteroid dehydrogenase. (richardvigilantebooks.com)
  • Hydroxysteroid (17β) dehydrogenases (HSD17Bs) form an enzyme family characterized by their ability to catalyze reactions in steroid and lipid metabolism. (richardvigilantebooks.com)
  • 17b-hydroxysteroid dehydrogenase (HSD) is a steroidogenic enzyme essential for invertebrate spermatogenesis. (molcells.org)
  • To address the second, we investigated RNAs bound by the metabolic enzyme hydroxysteroid dehydrogenase 17-β 10 (HSD17B10). (nature.com)
  • The enzyme 17β-hydroxysteroid dehydrogenase (17β-HSD) catalyzes the reversible interconversion of E1 and E2. (scirp.org)
  • 11β-hydroxysteroid dehydrogenase type 1 (11β-HSD1) is a key enzyme that transform cortisone to cortisol, which activates the endogenous glucocorticoid function. (ijbs.com)
  • Abi blocks 17α-hydroxylase/17,20-lyase (CYP17A1), an enzyme required for androgen synthesis. (aacc.org)
  • Consistent with increase in serum T, piperine increased Leydig cell number, cell size, and multiple steroidogenic pathway proteins, including steroidogenic acute regulatory protein, cholesterol side-chain cleavage enzyme, 3β-hydroxysteroid dehydrogenase 1, 17α-hydroxylase/20-lyase, and steroidogenic factor 1 expression levels. (frontiersin.org)
  • Piperine in vitro also increased androgen production and stimulated cholesterol side-chain cleavage enzyme and 17α-hydroxylase/20-lyase activities in immature Leydig cells. (frontiersin.org)
  • Predicted to enable oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor and steroid dehydrogenase activity. (nih.gov)
  • at 100 μM substrate (4-oestrene-3,17-dione)] by occupying the putative steroid-binding site. (rcsb.org)
  • Hydroxysteroid dehydrogenases (HSDs) or oxidoreductases catalyze the interconversion of alcohol and carbonyl functions in a position- and stereospecific manner on the steroid nucleus and side chain, using oxidized (+) or reduced (H) nicotinamide adenine dinucleotide, NAD(H), or NADP(H) as cofactors. (richardvigilantebooks.com)
  • 11β-Hydroxysteroid dehydrogenase (HSD-11β or 11β-HSD) enzymes catalyze the conversion of inert 11 keto-products (cortisone) to active cortisol, or vice versa, thus regulating the access of glucocorticoids to the steroid receptors. (richardvigilantebooks.com)
  • 17α-hydroxyprogesterone (17-OHP) is a steroid hormone that is primarily produced in the adrenal glands, as well as in ovaries, testes, and placenta. (cdc.gov)
  • It is a conjugated steroid converted by the sulfation of dehydroepiandrosterone (DHEA) at the 3β position via hydroxysteroid sulfotransferase. (cdc.gov)
  • The differential diagnosis is made by the marked accumulation of the steroid above the enzymatic block: 17-OHP for 21-OH deficiency, 11-deoxycortisol for 11-OH deficiency and pregnelonone and other Δ 5 precursors for 3β-HSD deficiency. (health.am)
  • Subramaniam P, Clayton PT, Portmann BC, Mieli-Vergani G, Hadzic N. Variable clinical spectrum of the most common inborn error of bile acid metabolism--3beta-hydroxy-Delta 5-C27-steroid dehydrogenase deficiency. (medscape.com)
  • 17β-HSDcl belongs to the SDR (short-chain dehydrogenase/reductase) superfamily. (rcsb.org)
  • 11β-hydroxysteroid dehydrogenase type 1 (11β-HSD1), encoded by Hsd11b1 , is a reductase that can convert inactive cortisone into metabolically active cortisol, but the role of 11β-HSD1 in sepsis-induced myocardial dysfunction remains poorly understood. (jbr-pub.org.cn)
  • A novel proof of concept model was developed to study the efficacy of the compounds in vitro using the androgen receptor positive hormone-dependent prostate cancer cell line, LNCaPwt, and its derivative, LNCaP[17β-HSD3], transfected and selected for stable expression of 17β-HSD3. (bath.ac.uk)
  • It inhibits adione-stimulated proliferation of 17β-HSD3-expressing androgen receptor-positive LNCaP(HSD3) prostate cancer cells in vitro. (ox.ac.uk)
  • An androgen-stimulated LNCaP(HSD3) xenograft proof-of-concept model was developed to study the efficacies of STX2171 and a more established 17β-HSD3 inhibitor, STX1383 (SCH-451659, Schering-Plough), in vivo. (ox.ac.uk)
  • In conclusion, STX2171 and STX1383 significantly lower plasma testosterone levels and inhibit androgen-dependent tumour growth in vivo, indicating that 17β-HSD3 inhibitors may have application in the treatment of hormone-dependent prostate cancer. (ox.ac.uk)
  • New insight into the molecular basis of 3beta-hydroxysteroid dehydrogenase deficiency: identification of eight mutations in the HSD3B2 gene eleven patients from seven new families and comparison of the functional properties of twenty-five mutant enzym. (medscape.com)
  • Molecular biology of the 3beta-hydroxysteroid dehydrogenase/delta5-delta4 isomerase gene family. (medscape.com)
  • Simard J, Moisan AM, Morel Y. Congenital adrenal hyperplasia due to 3beta-hydroxysteroid dehydrogenase/Delta(5)-Delta(4) isomerase deficiency. (medscape.com)
  • Carboxyl-terminal mutations in 3beta-hydroxysteroid dehydrogenase type II cause severe salt-wasting congenital adrenal hyperplasia. (medscape.com)
  • Persistent testicular delta5-isomerase-3beta-hydroxysteroid dehydrogenase (delta5-3beta-HSD) deficiency in the delta5-3beta-HSD form of congenital adrenal hyperplasia. (medscape.com)
  • Analyses of the mitochondrial hydroxysteroid dehydrogenase (HSD17B10) uncover the RNA-binding specificity of an enigmRBP. (nature.com)
  • Androstenedione is created from dehydroepiandrosterone (DHEA) or 17-hydroxyprogesterone. (wikipedia.org)
  • In terms of the diagnosis of 17β-hydroxysteroid dehydrogenase III deficiency the following should be taken into account: Increased androstenedione:testosterone ratio Thyroid dyshormonogenesis Genetic testing The 2006 Consensus statement on the management of intersex disorders states that individuals with 17β-hydroxysteroid dehydrogenase III deficiency have an intermediate risk of germ cell malignancy, at 28%, recommending that gonads be monitored. (wikipedia.org)
  • 17β-HSD Type 3 (17β-HSD3) has been seen to be over-expressed in prostate cancer, and catalyses the reduction of androstenedione (Adione) to testosterone (T), which stimulates prostate tumour growth. (bath.ac.uk)
  • 17β-HSD type 3 (17β-HSD3) catalyses the reduction of the weakly androgenic androstenedione (adione) to testosterone, suggesting that specific inhibitors of 17β-HSD3 may have a role in the treatment of hormone-dependent prostate cancer and benign prostate hyperplasia. (ox.ac.uk)
  • Measurement of androstenedione is useful in the diagnosis of congenital adrenal hyperplasia, in conjunction with other androgenic precursors, such as 17α-hydroxyprogesterone. (cdc.gov)
  • Peripheral type I 3-beta-hydroxysteroid dehydrogenase activity may also increase androstenedione levels. (medscape.com)
  • 17-beta hydroxysteroid dehydrogenase 3 deficiency is a condition that affects male sexual development. (medlineplus.gov)
  • Most people with 17-beta hydroxysteroid dehydrogenase 3 deficiency are born with external genitalia that appear female. (medlineplus.gov)
  • Children with 17-beta hydroxysteroid dehydrogenase 3 deficiency are often raised as girls. (medlineplus.gov)
  • 17-beta hydroxysteroid dehydrogenase 3 deficiency is a rare disorder. (medlineplus.gov)
  • Mutations in the HSD17B3 gene cause 17-beta hydroxysteroid dehydrogenase 3 deficiency. (medlineplus.gov)
  • in the male fetus, resulting in the abnormalities in the external sex organs that occur in 17-beta hydroxysteroid dehydrogenase 3 deficiency. (medlineplus.gov)
  • The additional testosterone results in the development of male secondary sex characteristics in adolescents, including those with 17-beta hydroxysteroid dehydrogenase 3 deficiency. (medlineplus.gov)
  • and have two copies of a mutated gene in each cell are affected by 17-beta hydroxysteroid dehydrogenase 3 deficiency. (medlineplus.gov)
  • 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)
  • 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)
  • What does 11 beta hydroxysteroid dehydrogenase do? (richardvigilantebooks.com)
  • What does 17 beta hydroxysteroid dehydrogenase do? (richardvigilantebooks.com)
  • 17 beta-Hydroxysteroid dehydrogenase (17 beta-HSD) controls the last step in the formation of all androgens and all estrogens. (richardvigilantebooks.com)
  • How does 17-beta hydroxysteroid dehydrogenase 3 affect male sexual development? (richardvigilantebooks.com)
  • Estrone sulfate acts as a long-lived reservoir that can be converted as needed to the more active estradiol (from estrone via 17 beta-hydroxysteroid dehydrogenase). (hmdb.ca)
  • [ 14 ] However, in 3-beta-hydroxysteroid dehydrogenase deficiency, the plasma ratio of 17-hydroxypregnenolone to 17-hydroxyprogesterone is markedly elevated. (medscape.com)
  • Plasma cortisol and aldosterone levels are low in 3-beta-hydroxysteroid dehydrogenase. (medscape.com)
  • Late-onset or nonclassic 3-beta-hydroxysteroid dehydrogenase deficiency: Baseline (unstimulated) measurements of pregnenolone, 17-hydroxypregnenolone, and dehydroepiandrosterone (DHEA) may be unremarkable in patients with late-onset or nonclassic 3-beta-hydroxysteroid dehydrogenase deficiency. (medscape.com)
  • Carriers: Carriers of type II 3-beta-hydroxysteroid dehydrogenase deficiency can have hormone profiles (both stimulated and unstimulated) within the reference range and, therefore, can only be detected by genotype studies. (medscape.com)
  • The impaired testosterone biosynthesis by 17β-hydroxysteroid dehydrogenase III (17β-HSD III), presents as atypical genitalia in affected males. (wikipedia.org)
  • however, in the presence of either 17β-HSD3 inhibitor, adione-dependent tumour growth was significantly inhibited and plasma testosterone levels reduced. (ox.ac.uk)
  • It upregulated the declined level of serum testosterone and the expression of steroidogenic genes such as CYP11A1 and 17β3-HSD with an obvious histologic improvement of the testes with re-establishment of the normal spermatogenic series, Sertoli and Leydig cells. (biomedcentral.com)
  • 17β-Hydroxysteroid dehydrogenase III deficiency is a rare autosomal recessive disorder of sexual development condition that is a cause of 46,XY disorder of sex development (46,XY DSD). (wikipedia.org)
  • The enzymatic defects causing female virilization involve 3β-hydroxysteroid dehydrogenase Δ5-Δ4 isomerase (3β-HSD), P 450 C21 hydroxylase (21-OH), and P 450 C11 hydroxylase (11-OH). (health.am)
  • 17β-Hydroxysteroid dehydrogenase III deficiency is caused by mutations found in the 17β-HSD III (17BHSD3) gene.17β-HSD III deficiency is an autosomal recessive disorder. (wikipedia.org)
  • It is caused by deficiency of 11β-hydroxysteroid dehydrogenase, which results in a defect of the peripheral metabolism of cortisol to cortisone. (richardvigilantebooks.com)
  • It is derived from progesterone via 17α-hydroxylase and is a chemical intermediate in the biosynthesis of several other steroids, including cortisol. (cdc.gov)
  • The deficiency completely or partially blocks conversion of 17- hydroxyprogesterone to 11-deoxycortisol, a precursor of cortisol, and conversion of progesterone to deoxycorticosterone, a precursor of aldosterone. (merckmanuals.com)
  • Because cortisol synthesis is decreased, adrenocorticotropic hormone (ACTH) levels increase, which stimulates the adrenal cortex, causing accumulation of cortisol precursors (eg, 17- hydroxyprogesterone ) and excessive production of the adrenal androgens dehydroepiandrosterone (DHEA) and androstenedione. (merckmanuals.com)
  • However, the role of 11β-hydroxysteroid dehydrogenase type 1 (11β-HSD1), which catalyzes the conversion of inactive cortisone into active cortisol, in inflammation remains unclear. (ac.ir)
  • Hirsutism caused by CAH is due to 1 of 3 cortisol biosynthetic defects, ie, 21-hydroxylase deficiency, 3 3 β -hydroxysteroid dehydrogenase, or 11-β -hydroxylase deficiency. (medscape.com)
  • Nuestro objetivo era el investigar la posible asociación entre niveles de cortisol salivar en hijos y depresión materna en tres momentos distintos: 2 días después del parto (N=58), cuatro meses después (N=64) y 36 meses después (N=81). (bvsalud.org)
  • Un test de ANOVA mostró diferencias marginales de efecto moderado en los niveles de cortisol en hijos de madres con DPP comparados con grupo de control. (bvsalud.org)
  • Suponiendo que los hijos de madres con DPP tienen niveles de cortisol ligeramente elevados al nacer, no se observaron estas diferencias en otros momentos. (bvsalud.org)
  • STX2171, a 17β-hydroxysteroid dehydrogenase type 3 inhibitor, is efficacious in vivo in a novel hormone-dependent prostate cancer model. (ox.ac.uk)
  • STX2171 is a novel selective non-steroidal 17β-HSD3 inhibitor with an IC(50) of ∼200 nM in a whole-cell assay. (ox.ac.uk)
  • Anti-inflammatory effect of a selective 11beta-hydroxysteroid dehydrogenase type 1 inhibitor via the stimulation of heme oxygenase-1 in LPS-activated mice and J774.1 murine macrophages. (ac.ir)
  • Its lead clinical compound is an investigational, potentially first-in-class oral 17β-hydroxysteroid dehydrogenase type 1 (HSD17B1) inhibitor in early clinical development for endometriosis, being evaluated for its potential effect on endometriotic lesions. (finbio.net)
  • Measurement of 17-OHP is useful in the diagnosis of congenital adrenal hyperplasia (CAH). (cdc.gov)
  • Se cree que la depresión post-parto (DPP) causa una variedad de problemas del desarrollo, incluyendo alteraciones funcionales en el eje hypotálamo-hipofisario-adrenal (HHA). (bvsalud.org)
  • 17β-Hydroxysteroid dehydrogenases (17β-HSDs) are responsible for the pre-receptor reduction/oxidation of steroids at the 17-position into active/inactive hormones, and the 15 known enzymes vary in their substrate specificity, localisation, and directional activity. (bath.ac.uk)
  • 17β-Hydroxysteroid dehydrogenases (17β-HSDs) catalyse the 17-position reduction/oxidation of steroids. (ox.ac.uk)
  • Specific inhibitors of 17β-HSD3 may have a role in the treatment of hormone-dependent prostate cancer and benign prostate hyperplasia, and also have potential as male anti-fertility agents. (bath.ac.uk)
  • In conclusion, a primary screening assay and proof of concept model have been developed to study the efficacy of 17β-HSD3 inhibitory compounds, which may have a role in the treatment of hormone-dependent cancer. (bath.ac.uk)
  • Anti-inflammatory effects of levalbuterol-induced 11beta-hydroxysteroid dehydrogenase type 1 activity in airway epithelial cells. (ac.ir)
  • Carbenoxolone prevents chemical eye ischemia-reperfusion-induced cell death via 11beta-hydroxysteroid dehydrogenase type 1 inhibition. (ac.ir)
  • 11. Chapman KE, Coutinho AE, Zhang Z, Kipari T, Savill JS, Seckl JR. Changing glucocorticoid action: 11beta-hydroxysteroid dehydrogenase type 1 in acute and chronic inflammation. (ac.ir)
  • Among the remaining half, 11β-hydroxysteroid dehydrogenase type 2 (11βHSD2) deficiency plays an important role. (pucv.cl)
  • 3alpha-Hydroxysteroid dehydrogenase type III deficiency: a novel mechanism for hirsutism. (medscape.com)
  • Herein we report on a 35-year-old man with a rather unusual type of EN. (karger.com)
  • This study was aimed to evaluate the presence of 17β-hydroxysteroid dehydrogenase type 1 (17β-HSD1), aromatase and estrogen receptor alpha (ERα) in the tumor cells and their association with the overall survival in 111 patients diagnosed with primary ovarian tumors. (bioscientifica.com)
  • 7. Chapman K, Holmes M, Seckl J. 11beta-hydroxysteroid dehydrogenases: Intracellular gate-keepers of tissue glucocorticoid action. (ac.ir)
  • A 293-EBNA-based cell line with stable expression of transfected human 17β-HSD3 was created and used to develop a whole cell radiometric TLC-based assay to assess the 17β-HSD3 inhibitory potency of a series of compounds. (bath.ac.uk)
  • d ) Validation of the yeast mRNA interactome using western blotting of input samples and eluate after interactome capture with specific antibodies (ADH1, alcohol dehydrogenase 1, PUB1) or against TAP-tagged proteins (PGK1, phosphoglycerate kinase 1, TDH1, triose phosphate dehydrogenase, TRX2, thioredoxine 2, SHE2, Swi5p-dependent HO Expression 2). (nature.com)
  • No association was observed of 17β-HSD1 expression with the histological subtypes and clinical stages of the tumor. (bioscientifica.com)
  • The expression of 17β-HSD1 in the cells of the serous epithelial ovarian tumors was associated with an improved overall survival, whereas aromatase and ERα were not related to a better survival. (bioscientifica.com)
  • The evaluation of hazard risk factors demonstrated that age and clinical stage showed worse prognosis, and 17β-HSD1 expression displayed a protective effect with a better survival outcome in patients of epithelial ovarian tumors. (bioscientifica.com)
  • Active compounds are selective for 17β-HSD3 over 17β-HSD1 and 17β-HSD2, non-androgenic with low toxicity, and efficacious in both an in vitro proof of concept model and in an in vivo tumour model. (bath.ac.uk)
  • Variants in mitochondrial amidoxime reducing component 1 and hydroxysteroid 17-beta dehydrogenase 13 reduce severity of nonalcoholic fatty liver disease in children and suppress fibrotic pathways through distinct mechanisms. (mpg.de)
  • Positive immunoreactivity for 17β-HSD1 was observed in 74% of the tumors. (bioscientifica.com)
  • In dieser Arbeit wird die Familie der 17β-Hydroxysteroid Dehydrogenasen (17β-HSDs) vorgestellt, die in vitro die Oxidation und/oder Reduktion von Steroidhormonen in Position 17 des Steroidgerüstes katalysieren. (uni-marburg.de)
  • Plasma concentrations of pregnenolone, 17-hydroxypregnenolone, and DHEA are elevated. (medscape.com)
  • Hydroxysteroid dehydrogenases (HSDs) are a group of alcohol oxidoreductases that catalyze the dehydrogenation of hydroxysteroids. (richardvigilantebooks.com)
  • The crystal structures of the 17β-HSDcl apo, holo and coumestrol-inhibited ternary complex, and the active-site Y167F mutant reveal subtle conformational differences in the substrate-binding loop that probably modulate the catalytic activity of 17β-HSDcl. (rcsb.org)
  • When basal values of 17-hydroxyprogesterone are between 7 and 45 nmol/L, an ACTH-stimulated concentration of greater than 45 nmol/L is also diagnostic. (medscape.com)
  • Although elevated basal plasma 17-hydroxyprogesterone levels (as high as 17 nmol/L) may be present during the luteal phase of the menstrual cycle and in PCOS, ACTH-stimulated increments are blunted. (medscape.com)
  • 5. Itoi S, Terao M, Murota H, Katayama I. 11beta-Hydroxysteroid dehydrogenase 1 contributes to the pro-inflammatory response of keratinocytes. (ac.ir)
  • In similar TLC-based assays these compounds were found to be inactive against 17β-HSD1 and 17β-HSD2, indicating selectivity. (bath.ac.uk)
  • The proliferation of the parental cell line was most efficiently stimulated by 5α-dihydrotestosterone (DHT), but the LNCaP[17β-HSD3] cells were equally stimulated by Adione, indicating that 17β-HSD3 efficiently converts Adione to T in this model. (bath.ac.uk)
  • Adione-stimulated proliferation of LNCaP[17β-HSD3] cells was inhibited in the presence of either STX2171 or STX2624. (bath.ac.uk)