An enzyme that catalyzes the oxidation of cholesterol in the presence of molecular oxygen to 4-cholesten-3-one and hydrogen peroxide. The enzyme is not specific for cholesterol, but will also oxidize other 3-hydroxysteroids. EC 1.1.3.6.
Drugs that inhibit 3-OXO-5-ALPHA-STEROID 4-DEHYDROGENASE. They are commonly used to reduce the production of DIHYDROTESTOSTERONE.
An oxidoreductase that catalyzes the conversion of 3-oxo-delta4 steroids into their corresponding 5alpha form. It plays an important role in the conversion of TESTOSTERONE into DIHYDROTESTOSTERONE and PROGESTERONE into DIHYDROPROGESTERONE.
Steroidal compounds in which one or more carbon atoms in the steroid ring system have been substituted with nitrogen atoms.
An orally active 3-OXO-5-ALPHA-STEROID 4-DEHYDROGENASE inhibitor. It is used as a surgical alternative for treatment of benign PROSTATIC HYPERPLASIA.
An enzyme that catalyzes the reduction of TESTOSTERONE to 5-ALPHA DIHYDROTESTOSTERONE.
Inability to empty the URINARY BLADDER with voiding (URINATION).
A subclass of enzymes which includes all dehydrogenases acting on carbon-carbon bonds. This enzyme group includes all the enzymes that introduce double bonds into substrates by direct dehydrogenation of carbon-carbon single bonds.
Increase in constituent cells in the PROSTATE, leading to enlargement of the organ (hypertrophy) and adverse impact on the lower urinary tract function. This can be caused by increased rate of cell proliferation, reduced rate of cell death, or both.
Oxidoreductases that are specific for the reduction of NITRATES.
Enzymes that catalyze the reversible reduction of alpha-carboxyl group of 3-hydroxy-3-methylglutaryl-coenzyme A to yield MEVALONIC ACID.
Ribonucleotide Reductases are enzymes that catalyze the conversion of ribonucleotides to deoxyribonucleotides, which is a crucial step in DNA synthesis and repair, utilizing a radical mechanism for this conversion.
A FLAVOPROTEIN oxidoreductase that occurs both as a soluble enzyme and a membrane-bound enzyme due to ALTERNATIVE SPLICING of a single mRNA. The soluble form is present mainly in ERYTHROCYTES and is involved in the reduction of METHEMOGLOBIN. The membrane-bound form of the enzyme is found primarily in the ENDOPLASMIC RETICULUM and outer mitochondrial membrane, where it participates in the desaturation of FATTY ACIDS; CHOLESTEROL biosynthesis and drug metabolism. A deficiency in the enzyme can result in METHEMOGLOBINEMIA.
A group of enzymes that oxidize diverse nitrogenous substances to yield nitrite. (Enzyme Nomenclature, 1992) EC 1.
Catalyzes the oxidation of GLUTATHIONE to GLUTATHIONE DISULFIDE in the presence of NADP+. Deficiency in the enzyme is associated with HEMOLYTIC ANEMIA. Formerly listed as EC 1.6.4.2.
An enzyme that utilizes NADH or NADPH to reduce FLAVINS. It is involved in a number of biological processes that require reduced flavin for their functions such as bacterial bioluminescence. Formerly listed as EC 1.6.8.1 and EC 1.5.1.29.
A FLAVOPROTEIN enzyme that catalyzes the oxidation of THIOREDOXINS to thioredoxin disulfide in the presence of NADP+. It was formerly listed as EC 1.6.4.5
A flavoprotein that catalyzes the reduction of heme-thiolate-dependent monooxygenases and is part of the microsomal hydroxylating system. EC 1.6.2.4.
An enzyme that catalyzes the oxidation and reduction of FERREDOXIN or ADRENODOXIN in the presence of NADP. EC 1.18.1.2 was formerly listed as EC 1.6.7.1 and EC 1.6.99.4.
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)
Cytochrome reductases are enzymes that catalyze the transfer of electrons from donor molecules to cytochromes in electron transport chains, playing a crucial role in cellular respiration and energy production within cells.
Plasma glycoprotein member of the serpin superfamily which inhibits TRYPSIN; NEUTROPHIL ELASTASE; and other PROTEOLYTIC ENZYMES.
An enzyme of the oxidoreductase class that catalyzes the reaction 7,8-dihyrofolate and NADPH to yield 5,6,7,8-tetrahydrofolate and NADPH+, producing reduced folate for amino acid metabolism, purine ring synthesis, and the formation of deoxythymidine monophosphate. Methotrexate and other folic acid antagonists used as chemotherapeutic drugs act by inhibiting this enzyme. (Dorland, 27th ed) EC 1.5.1.3.
A flavoprotein amine oxidoreductase that catalyzes the reversible conversion of 5-methyltetrahydrofolate to 5,10-methylenetetrahydrofolate. This enzyme was formerly classified as EC 1.1.1.171.
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.
An NAD-dependent enzyme that catalyzes the oxidation of nitrite to nitrate. It is a FLAVOPROTEIN that contains IRON and MOLYBDENUM and is involved in the first step of nitrate assimilation in PLANTS; FUNGI; and BACTERIA. It was formerly classified as EC 1.6.6.1.
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)
Reductases that catalyze the reaction of peptide-L-methionine -S-oxide + thioredoxin to produce peptide-L-methionine + thioredoxin disulfide + H(2)O.
One of the two major pharmacological subdivisions of adrenergic receptors that were originally defined by the relative potencies of various adrenergic compounds. The alpha receptors were initially described as excitatory receptors that post-junctionally stimulate SMOOTH MUSCLE contraction. However, further analysis has revealed a more complex picture involving several alpha receptor subtypes and their involvement in feedback regulation.
The rate dynamics in chemical or physical systems.
An enzyme of the oxidoreductase class that catalyzes the formation of 2'-deoxyribonucleotides from the corresponding ribonucleotides using NADPH as the ultimate electron donor. The deoxyribonucleoside diphosphates are used in DNA synthesis. (From Dorland, 27th ed) EC 1.17.4.1.
Compounds that inhibit HMG-CoA reductases. They have been shown to directly lower cholesterol synthesis.
NAD(P)H:(quinone acceptor) oxidoreductases. A family that includes three enzymes which are distinguished by their sensitivity to various inhibitors. EC 1.6.99.2 (NAD(P)H DEHYDROGENASE (QUINONE);) is a flavoprotein which reduces various quinones in the presence of NADH or NADPH and is inhibited by dicoumarol. EC 1.6.99.5 (NADH dehydrogenase (quinone)) requires NADH, is inhibited by AMP and 2,4-dinitrophenol but not by dicoumarol or folic acid derivatives. EC 1.6.99.6 (NADPH dehydrogenase (quinone)) requires NADPH and is inhibited by dicoumarol and folic acid derivatives but not by 2,4-dinitrophenol.
Hypoxia-inducible factor 1, alpha subunit is a basic helix-loop-helix transcription factor that is regulated by OXYGEN availability and is targeted for degradation by VHL TUMOR SUPPRESSOR PROTEIN.
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 oxidoreductases that act on NADH or NADPH. In general, enzymes using NADH or NADPH to reduce a substrate are classified according to the reverse reaction, in which NAD+ or NADP+ is formally regarded as an acceptor. This subclass includes only those enzymes in which some other redox carrier is the acceptor. (Enzyme Nomenclature, 1992, p100) EC 1.6.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
An enzyme that catalyzes the reduction of 6,7-dihydropteridine to 5,6,7,8-tetrahydropteridine in the presence of NADP+. Defects in the enzyme are a cause of PHENYLKETONURIA II. Formerly listed as EC 1.6.99.7.
A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).
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.
A subtype of thioredoxin reductase found primarily in the CYTOSOL.
An NAD-dependent enzyme that catalyzes the oxidation of acyl-[acyl-carrier protein] to trans-2,3-dehydroacyl-[acyl-carrier protein]. It has a preference for acyl groups with a carbon chain length between 4 to 16.

Reversion of the differentiated phenotype and maturation block in Sertoli cells in pathological human testis. (1/92)

To study the relationship between abnormal Sertoli cell differentiation and spermatogenic impairment, we examined the expression of Sertoli cell markers normally lost at puberty, cytokeratin 18 (CK18), anti-Mullerian hormone (AMH) and M2A antigen, in three children (aged 1-2 years), 50 adults (aged 19-45 years) with obstructive or non-obstructive azoospermia or oligozoospermia, and six patients (aged 1-18 years) with 5 alpha-reductase deficiency. There was CK18 and/or AMH expression, but never M2A antigen expression, associated with spermatogonial arrest or Sertoli cell-only (SCO) syndrome in infertile men. Loss of M2A antigen suggests the transition of Sertoli cells to an adult phenotype, while CK18 and/or AMH expression may be a manifestation of de-differentiation of Sertoli cells. In 5 alpha-reductase deficiency, there was a sequential loss of CK18, M2A antigen and AMH around puberty, associated with partial spermatogenesis. The persistence of immature Sertoli cells expressing M2A antigen was associated with prepubertal seminiferous cords and SCO syndrome. Therefore, 5 alpha-reductase deficiency may prevent the maturation of Sertoli cells, resulting in impairment of spermatogenesis, and loss of M2A antigen expression coincides with a critical step in the Sertoli cell maturation. High follicle stimulating hormone concentrations due to failure of normal Sertoli cell differentiation indicate a normal development pattern of the hypothalamic-pituitary-gonadal axis.  (+info)

Selective serotonin reuptake inhibitors directly alter activity of neurosteroidogenic enzymes. (2/92)

The neurosteroid 3alpha-hydroxysteroid-5alpha-pregnan-20-one (allopregnanolone) acts as a positive allosteric modulator of gamma-aminobutyric acid at gamma-aminobutyric acid type A receptors and hence is a powerful anxiolytic, anticonvulsant, and anesthetic agent. Allopregnanolone is synthesized from progesterone by reduction to 5alpha-dihydroprogesterone, mediated by 5alpha-reductase, and by reduction to allopregnanolone, mediated by 3alpha-hydroxysteroid dehydrogenase (3alpha-HSD). Previous reports suggested that some selective serotonin reuptake inhibitors (SSRIs) could alter concentrations of allopregnanolone in human cerebral spinal fluid and in rat brain sections. We determined whether SSRIs directly altered the activities of either 5alpha-reductase or 3alpha-HSD, using an in vitro system containing purified recombinant proteins. Although rats appear to express a single 3alpha-HSD isoform, the human brain contains several isoforms of this enzyme, including a new isoform we cloned from human fetal brains. Our results indicate that the SSRIs fluoxetine, sertraline, and paroxetine decrease the K(m) of the conversion of 5alpha-dihydroprogesterone to allopregnanolone by human 3alpha-HSD type III 10- to 30-fold. Only sertraline inhibited the reverse oxidative reaction. SSRIs also affected conversions of androgens to 3alpha- and 3alpha, 17beta-reduced or -oxidized androgens mediated by 3alpha-HSD type II(Brain). Another antidepressant, imipramine, was without any effect on allopregnanolone or androstanediol production. The region-specific expression of 3alpha-HSD type II(Brain) and 3alpha-HSD type III mRNAs suggest that SSRIs will affect neurosteroid production in a region-specific manner. Our results may thus help explain the rapid alleviation of the anxiety and dysphoria associated with late luteal phase dysphoria disorder and major unipolar depression by these SSRIs.  (+info)

2,3,7,8-tetrachlorodibenzo-p-dioxin inhibits luminal cell differentiation and androgen responsiveness of the ventral prostate without inhibiting prostatic 5alpha-dihydrotestosterone formation or testicular androgen production in rat offspring. (3/92)

In utero and lactational exposure to a single maternal dose of 1 microg 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD)/kg causes some overt toxicity and impairs prostate growth in male offspring. As similar effects on the ventral prostate can be caused by decreased testosterone production during perinatal development, we determined whether intratesticular testosterone content, testicular responsiveness to gonadotropin stimulation, or plasma testosterone concentrations were reduced in fetal and newborn rats. Because these endpoints were not affected, the ability of TCDD exposure to inhibit synthesis of the proximal androgen in prostate development, 5alpha-dihydrotestosterone (DHT), from the circulating precursor testosterone and 5alpha-androstane-3alpha,17ss-diol (3alpha-Diol), was studied on postnatal days (PNDs) 14, 21, and 32. The ability of the ventral prostate to form DHT from 3alpha-Diol was slightly impaired on PND 14, but this transient effect was not statistically significant, and recovery was evident by PND 21. Subsequent experiments used organ culture to study the effects of in vivo TCDD exposure on androgen metabolism, androgen responsiveness, androgen receptor expression, and luminal epithelial cell differentiation after in vitro exposure to graded androgen concentrations. In utero and lactational TCDD exposure had no effect on DHT formation in organ culture, but transiently reduced the androgen -induced expression of prostatic-binding protein subunit C3, decreased ventral prostate epithelial cell androgen receptor expression, and inhibited the formation of androgen responsive luminal epithelial cells. These results suggest that TCDD exposure impairs prostate growth and androgen responsiveness by inhibiting prostatic epithelial cell differentiation.  (+info)

Sebocytes are the key regulators of androgen homeostasis in human skin. (4/92)

The mRNA expression patterns of the androgen receptor and the androgen metabolizing enzymes 3beta-hydroxysteroid dehydrogenase/Delta(5-4)-isomerase, 17beta-hydroxysteroid dehydrogenase, 5alpha-reductase, and 3alpha-hydroxysteroid dehydrogenase were investigated in three different cell populations originating from human skin, SZ95 sebocytes, HaCaT keratinocytes, and MeWo melanoma cells, by means of reverse transcription polymerase chain reaction. Restriction analysis of cDNA fragments was performed to identify isozymes of 3beta-hydroxysteroid dehydrogenase/Delta(5-4)-isomerase and 3alpha-hydroxysteroid dehydrogenase. In addition, 3H-dihydroepiandrosterone and 3H-testosterone were used as substrates to determine the metabolic activity of these enzymes in SZ95 sebocytes, primary sebocyte cultures, and HaCaT keratinocytes. Furthermore, the effects of the selective 5alpha-reductase type 1 and 2 inhibitors, 4,7beta-dimethyl-4-aza-5alpha-cholestan-3-one and dihydrofinasteride, respectively, and of the 3beta-hydroxysteroid dehydrogenase/Delta(5-4)-isomerase inhibitor cyproterone acetate on androgen metabolism were investigated. Androgen receptor mRNA was detected in SZ95 sebocytes and HaCaT keratinocytes but not in MeWo melanoma cells, whereas 3beta-hydroxysteroid dehydrogenase/Delta(5-4)-isomerase isotype 1 mRNA and metabolic activity were only found in SZ95 sebocytes. The enzyme activity could be inhibited by cyproterone acetate. Type 2 17beta-hydroxysteroid dehydrogenase, type 1 5alpha-reductase, and 3alpha-hydroxysteroid dehydrogenase mRNA were expressed in all three cell populations tested, whereas type 3 17beta-hydroxysteroid dehydrogenase mRNA could only be detected in SZ95 sebocytes. The major metabolic steps of testosterone in SZ95 sebocytes, primary sebocyte cultures, and HaCaT keratinocytes were its conversion to androstenedione by 17beta-hydroxysteroid dehydrogenase and further to 5alpha-androstanedione by 5alpha-reductase. The type 1 5alpha-reductase selective inhibitor 4,7beta-dimethyl-4-aza-5alpha-cholestan-3-one, but not the type 2 selective inhibitor dihydrofinasteride, inhibited 5alpha-reductase at low concentrations in SZ95 sebocytes and HaCaT keratinocytes. 5alpha-androstanedione was degraded to androsterone by 3alpha-hydroxysteroid dehydrogenase, which exhibited a stronger activity in HaCaT keratinocytes than in SZ95 sebocytes and in primary sebocyte cultures. Lower levels of 5alpha-dihydrotestosterone and 5alpha-androstanediol were also detected in all cells tested. Our investigations show that specific enzyme expression and activity in cultured sebocytes and keratinocytes seem to allocate different duties to these cells in vitro. Sebocytes are able to synthesize testosterone from adrenal precursors and to inactivate it in order to maintain androgen homeostasis, whereas keratinocytes are responsible for androgen degradation.  (+info)

Lifestyle determinants of 5alpha-reductase metabolites in older African-American, white, and Asian-American men. (5/92)

Men with higher endogenous 5alpha-reductase activity may have higher prostate cancer risk. This hypothesis raises two questions: (a) Could racial differences in 5alpha-reductase activity explain the observed racial differences in prostate cancer risk? and (b) Could a man reduce his activity level by modifying his lifestyle? To address these questions, we measured two hormonal indices of 5alpha-reductase activity [serum levels of androstane-3alpha-17beta-diol glucuronide (3alpha-diol G) and androsterone glucuronide (AG)] in healthy, older African-American, white, and Asian-American men, who are at high, intermediate, and low prostate cancer risk, respectively. We also examined associations between these metabolite levels and such lifestyle characteristics as body size and physical activity as well as select aspects of medical history and family history of prostate cancer. Men included in this cross-sectional analysis (n = 1054) had served as control subjects in a population-based case-control study of prostate cancer we conducted in California, Hawaii, and Vancouver, Canada and provided information on certain personal attributes and donated blood between March 1990 and March 1992. In this study, concentrations of 3alpha-diol G declined significantly with age and increased significantly with body mass index. Mean levels of 3alpha-diol G, adjusted for age and body mass index, were 6.1 ng/ml in African-Americans, 6.9 ng/ml in whites and 4.8 ng/ml in Asian-Americans. These differences were statistically significant (African-Americans versus whites: P < 0.01; whites versus Asian-Americans: P < 0.001). Concentrations of AG decreased significantly with age, but only in whites, and were unrelated to any of the reported personal attributes. Mean levels of AG, adjusted for age, were 44.1 ng/ml in African-Americans, 44.9 ng/ml in whites, and 37.5 ng/ml in Asian-Americans (Asian-Americans versus whites, P < 0.001). In conclusion, older African-American and white men have similar levels of these two indices of 5alpha-reductase activity, and these levels are higher than those of older Asian-American men. This difference may be related to the lower prostate cancer risk in Asian-Americans.  (+info)

Dietary soy-phytoestrogens decrease testosterone levels and prostate weight without altering LH, prostate 5alpha-reductase or testicular steroidogenic acute regulatory peptide levels in adult male Sprague-Dawley rats. (6/92)

Nutritional factors, especially phytoestrogens, have been extensively studied for their potential beneficial effects against hormone-dependent and age-related diseases. The present study describes the short-term effects of dietary phytoestrogens on regulatory behaviors (food/water intake, locomotor activity and body weight), prostate weight, prostate 5alpha-reductase enzyme activity, reproductive hormone levels, and testicular steroidogenic acute regulatory peptide (StAR) levels in adult Sprague-Dawley rats. Animals were fed either a phytoestrogen-rich diet containing approximately 600 microg/g isoflavones (as determined by HPLC) or a phytoestrogen-free diet. After 5 weeks of consuming these diets, plasma phytoestrogen levels were 35 times higher in animals fed the phytoestrogen-rich vs phytoestrogen-free diets. Body and prostate weights were significantly decreased in animals fed the phytoestrogen-rich diet vs the phytoestrogen-free fed animals; however, no significant change in prostate 5alpha-reductase enzyme activity was observed between the treatment groups. Locomotor activity levels were higher in the phytoestrogen-rich vs the phytoestrogen-free animals during the course of the treatment interval. Plasma testosterone and androstenedione levels were significantly lower in the animals fed the phytoestrogen-rich diet compared with animals fed the phytoestrogen-free diet. However, there were no significant differences in plasma LH or estradiol levels between the diet groups. Testicular StAR levels were not significantly different between the phytoestrogen-rich vs the phytoestrogen-free fed animals. These results indicated that consumption of dietary phytoestrogens resulting in very high plasma isoflavone levels over a relatively short period can significantly alter body and prostate weight and plasma androgen hormone levels without affecting gonadotropin or testicular StAR levels. The findings of this study identify the biological actions of phytoestrogens on male reproductive endocrinology and provide insights into the protective effects these estrogen mimics exert in male reproductive disorders such as benign prostatic hyperplasia and prostate cancer.  (+info)

Polymorphic markers in the SRD5A2 gene and prostate cancer risk: a population-based case-control study. (7/92)

It has been suggested that the activity of the steroid 5alpha-reductase type II enzyme (encoded by the SRD5A2 gene) may be associated with prostate cancer risk and that population differences in this enzyme's activity may account for part of the substantial racial/ethnic disparity in prostate cancer risk. To provide etiological clues, we evaluated the relationships of four polymorphic markers in the SRD5A2 gene, specifically, A49T (a substitution of threonine for alanine at codon 49), V89L (a substitution of leucine for valine at codon 89), R227Q (a substitution of glutamine for arginine at codon 227), and a (TA)n dinucleotide repeat, with prostate cancer risk in a population-based case-control study in China, a population with the lowest reported prostate cancer incidence rate in the world. Genotypes of these four markers were determined from genomic DNA of 191 incident cases of prostate cancer and 304 healthy controls using PCR-based assays, and serum androgen levels were measured in relation to these genotypes. All study subjects had the wild-type AA genotype of the A49T marker, and 99% had the RR genotype of the R227Q marker. For the V89L marker, prevalences of the LL, VV, and VL genotypes among controls were 35%, 21%, and 45%, respectively. Compared with men with the VV genotype, those with the LL genotype had a statistically nonsignificant 12% reduced risk (odds ratio = 0.88, 95% confidence interval, 0.53-1.47). In addition, men with the LL genotype had significantly higher serum levels of testosterone and significantly lower serum levels of 5alpha-androstane-3alpha,17beta-diol glucuronide than men with other genotypes. Men heterozygous for the (TA)0 allele of the (TA)n marker had a modest, statistically nonsignificant risk reduction (odds ratio = 0.67; 95% confidence interval, 0.39-1.12) compared with men homozygous for the (TA)0 allele, along with significantly higher serum dihydrotestosterone levels. The observed V89L genotype prevalences and the association between V89L genotypes and serum androgen levels support the hypothesis that genotypes associated with lower levels of 5alpha-reductase activity are more common in low-risk populations. Although we found no statistically significant associations of these SRD5A2 polymorphisms with prostate cancer risk, a small effect of these markers cannot be ruled out because of the rarity of certain marker genotypes. Larger studies are needed to further clarify the role of these markers and to elucidate whether genetic diversity of the SRD5A2 gene, alone or in combination with other susceptibility genes, can help explain the large racial/ethnic differences in prostate cancer risk.  (+info)

Allelic frequencies of six polymorphic markers for risk of prostate cancer. (8/92)

The aim of the present study was to evaluate the distribution of polymorphisms for the androgen receptor (AR) (CAG, StuI, GGN), SRD5A2 (Ala49Thr, Val89Leu) and CYP17 (MspA1) genes that are considered to be relevant for risk of prostate cancer. We studied 200 individuals from two cities in the State of Sao Paulo, by PCR, PCR-RFLP and ASOH techniques. The allelic frequencies of the autosomal markers and the StuI polymorphism of the AR gene were very similar to those described in most North American and European populations. In relation to the CAG and GGN number of repeats, the study subjects had smaller repeat lengths (mean of 20.65 and 22.38, respectively) than those described in North American, European and Chinese populations. In the present study, 30.5% of the individuals had less than 22 CAG repeats and 45.5% had less than 23 GGN repeats. When both repeat lengths are considered jointly, this Brazilian population is remarkably different from the others. Further studies on prostate cancer patients need to be conducted to assess the significance of these markers in the Brazilian population.  (+info)

Cholesterol oxidase is an enzyme that catalyzes the conversion of cholesterol to cholest-4-en-3-one, while reducing molecular oxygen to hydrogen peroxide. This reaction is commonly used in clinical and research settings to measure cholesterol levels in samples of blood or other biological fluids. The enzyme is produced by various bacteria, fungi, and plants, and can be purified for use in diagnostic kits and biochemical assays. In addition to its role in cholesterol analysis, cholesterol oxidase has also been studied as a potential therapeutic agent for the treatment of bacterial infections and cancer.

5-alpha Reductase Inhibitors are a class of drugs that block the action of the enzyme 5-alpha reductase, which is responsible for converting testosterone to dihydrotestosterone (DHT). DHT is a more potent form of testosterone that plays a key role in the development and maintenance of male sexual characteristics and is involved in the pathogenesis of benign prostatic hyperplasia (BPH) and androgenetic alopecia (male pattern baldness).

By inhibiting the action of 5-alpha reductase, these drugs reduce the levels of DHT in the body, which can help to shrink the prostate gland and improve symptoms of BPH such as difficulty urinating, frequent urination, and weak urine stream. They are also used off-label to treat hair loss in men.

Examples of 5-alpha reductase inhibitors include finasteride (Proscar, Propecia) and dutasteride (Avodart). Common side effects of these drugs may include decreased libido, erectile dysfunction, and breast tenderness or enlargement.

Cholestenone 5 alpha-reductase is an enzyme that plays a role in the conversion of cholesterol and other steroid hormones in the body. Specifically, it catalyzes the reduction of 5,7-dihydroxycholest-4-en-3-one (also known as cholestenone) to 5α-androstan-3α,17β-diol, which is a precursor to the male sex hormone testosterone.

This enzyme is found in various tissues throughout the body, including the prostate gland, skin, and liver. In the prostate gland, 5 alpha-reductase helps regulate the growth and function of the gland by converting testosterone to dihydrotestosterone (DHT), a more potent form of the hormone.

Inhibitors of 5 alpha-reductase are sometimes used as medications to treat conditions such as benign prostatic hyperplasia (BPH) and male pattern baldness, as reducing DHT levels can help alleviate symptoms associated with these conditions.

I'm sorry for any confusion, but "Azasteroids" is not a medical term or concept. The term "azasteroids" is used in the field of chemistry to refer to a class of compounds that are structurally similar to steroids but have an aziridine ring (a three-membered ring containing two carbon atoms and one nitrogen atom) instead of the usual four-membered ring in the steroid structure.

These compounds may have potential applications in various fields, including medicinal chemistry, but they are not a medical concept or diagnosis. If you have any questions related to medical terminology or health concerns, I would be happy to help you with those!

Finasteride is a synthetic 4-azasteroid compound that acts as a specific inhibitor of Type II 5α-reductase, an intracellular enzyme that converts testosterone to dihydrotestosterone (DHT). DHT is a hormonal byproduct thought to be responsible for the development and worsening of benign prostatic hyperplasia (BPH) and androgenetic alopecia (AGA), also known as male pattern baldness.

Finasteride is available in two formulations: finasteride 1 mg (Proscar) and finasteride 5 mg (Propecia). Finasteride 1 mg is used to treat BPH, while finasteride 5 mg is used for the treatment of AGA in men. The drug works by reducing the production of DHT, which in turn slows down the progression of BPH and AGA.

It's important to note that finasteride is not approved for use in women or children, and it should be used with caution in men due to potential side effects such as decreased sexual desire, difficulty in achieving an erection, and a decrease in the amount of semen produced.

3-Oxo-5-alpha-steroid 4-dehydrogenase is an enzyme that plays a role in steroid metabolism. It is involved in the conversion of certain steroids into others by removing hydrogen atoms and adding oxygen to create double bonds in the steroid molecule. Specifically, this enzyme catalyzes the dehydrogenation of 3-oxo-5-alpha-steroids at the 4th position, which results in the formation of a 4,5-double bond.

The enzyme is found in various tissues throughout the body and is involved in the metabolism of several important steroid hormones, including cortisol, aldosterone, and androgens. It helps to regulate the levels of these hormones in the body by converting them into their active or inactive forms as needed.

Deficiencies or mutations in the 3-oxo-5-alpha-steroid 4-dehydrogenase enzyme can lead to various medical conditions, such as congenital adrenal hyperplasia, which is characterized by abnormal hormone levels and development of sexual characteristics.

Urinary retention is a medical condition in which the bladder cannot empty completely or at all, resulting in the accumulation of urine in the bladder. This can lead to discomfort, pain, and difficulty in passing urine. Urinary retention can be acute (sudden onset) or chronic (long-term). Acute urinary retention is a medical emergency that requires immediate attention, while chronic urinary retention may be managed with medications or surgery. The causes of urinary retention include nerve damage, bladder muscle weakness, prostate gland enlargement, and side effects of certain medications.

Oxidoreductases acting on CH-CH group donors are a class of enzymes within the larger group of oxidoreductases, which are responsible for catalyzing oxidation-reduction reactions. Specifically, this subclass of enzymes acts upon donors containing a carbon-carbon (CH-CH) bond, where one atom or group of atoms is oxidized and another is reduced during the reaction process. These enzymes play crucial roles in various metabolic pathways, including the breakdown and synthesis of carbohydrates, lipids, and amino acids.

The reactions catalyzed by these enzymes involve the transfer of electrons and hydrogen atoms between the donor and an acceptor molecule. This process often results in the formation or cleavage of carbon-carbon bonds, making them essential for numerous biological processes. The systematic name for this class of enzymes is typically structured as "donor:acceptor oxidoreductase," where donor and acceptor represent the molecules involved in the electron transfer process.

Examples of enzymes that fall under this category include:

1. Aldehyde dehydrogenases (EC 1.2.1.3): These enzymes catalyze the oxidation of aldehydes to carboxylic acids, using NAD+ as an electron acceptor.
2. Dihydrodiol dehydrogenase (EC 1.3.1.14): This enzyme is responsible for the oxidation of dihydrodiols to catechols in the biodegradation of aromatic compounds.
3. Succinate dehydrogenase (EC 1.3.5.1): A key enzyme in the citric acid cycle, succinate dehydrogenase catalyzes the oxidation of succinate to fumarate and reduces FAD to FADH2.
4. Xylose reductase (EC 1.1.1.307): This enzyme is involved in the metabolism of pentoses, where it reduces xylose to xylitol using NADPH as a cofactor.

Prostatic hyperplasia, also known as benign prostatic hyperplasia (BPH), is a noncancerous enlargement of the prostate gland. The prostate gland surrounds the urethra, the tube that carries urine and semen out of the body. When the prostate gland enlarges, it can squeeze or partially block the urethra, causing problems with urination, such as a weak stream, difficulty starting or stopping the flow, and more frequent urination, especially at night. Prostatic hyperplasia is a common condition as men age and does not necessarily lead to cancer. However, it can cause significant discomfort and decreased quality of life if left untreated. Treatment options include medications, minimally invasive procedures, and surgery.

Nitrate reductases are a group of enzymes that catalyze the reduction of nitrate (NO3-) to nitrite (NO2-). This process is an essential part of the nitrogen cycle, where nitrate serves as a terminal electron acceptor in anaerobic respiration for many bacteria and archaea. In plants, this enzyme plays a crucial role in nitrogen assimilation by reducing nitrate to ammonium (NH4+), which can then be incorporated into organic compounds. Nitrate reductases require various cofactors, such as molybdenum, heme, and/or FAD, for their activity. There are three main types of nitrate reductases: membrane-bound (which use menaquinol as an electron donor), cytoplasmic (which use NADH or NADPH as an electron donor), and assimilatory (which also use NADH or NADPH as an electron donor).

Hydroxymethylglutaryl CoA (HMG-CoA) reductase is an enzyme that plays a crucial role in the synthesis of cholesterol in the body. It is found in the endoplasmic reticulum of cells and catalyzes the conversion of HMG-CoA to mevalonic acid, which is a key rate-limiting step in the cholesterol biosynthetic pathway.

The reaction catalyzed by HMG-CoA reductase is as follows:

HMG-CoA + 2 NADPH + 2 H+ → mevalonic acid + CoA + 2 NADP+

This enzyme is the target of statin drugs, which are commonly prescribed to lower cholesterol levels in the treatment of cardiovascular diseases. Statins work by inhibiting HMG-CoA reductase, thereby reducing the production of cholesterol in the body.

Ribonucleotide Reductases (RNRs) are enzymes that play a crucial role in DNA synthesis and repair. They catalyze the conversion of ribonucleotides to deoxyribonucleotides, which are the building blocks of DNA. This process involves the reduction of the 2'-hydroxyl group of the ribose sugar to a hydrogen, resulting in the formation of deoxyribose.

RNRs are highly regulated and exist in various forms across different species. They are divided into three classes (I, II, and III) based on their structure, mechanism, and cofactor requirements. Class I RNRs are further divided into two subclasses (Ia and Ib), which differ in their active site architecture and regulation.

Class Ia RNRs, found in eukaryotes and some bacteria, contain a stable tyrosyl radical that acts as the catalytic center for hydrogen abstraction. Class Ib RNRs, found in many bacteria, use a pair of iron centers to perform the same function. Class II RNRs are present in some bacteria and archaea and utilize adenosine triphosphate (ATP) as a cofactor for reduction. Class III RNRs, found in anaerobic bacteria and archaea, use a unique mechanism involving a radical S-adenosylmethionine (SAM) cofactor to facilitate the reduction reaction.

RNRs are essential for DNA replication and repair, and their dysregulation has been linked to various diseases, including cancer and neurodegenerative disorders. Therefore, understanding the structure, function, and regulation of RNRs is of great interest in biochemistry, molecular biology, and medicine.

Nitrite reductases are a group of enzymes that catalyze the reduction of nitrite (NO2-) to nitric oxide (NO). This reaction is an important part of the nitrogen cycle, particularly in denitrification and dissimilatory nitrate reduction to ammonium (DNRA) processes. Nitrite reductases can be classified into two main types based on their metal co-factors: copper-containing nitrite reductases (CuNiRs) and cytochrome cd1 nitrite reductases. CuNiRs are typically found in bacteria and fungi, while cytochrome cd1 nitrite reductases are primarily found in bacteria. These enzymes play a crucial role in the global nitrogen cycle and have potential implications for environmental and medical research.

Glutathione reductase (GR) is an enzyme that plays a crucial role in maintaining the cellular redox state. The primary function of GR is to reduce oxidized glutathione (GSSG) to its reduced form (GSH), which is an essential intracellular antioxidant. This enzyme utilizes nicotinamide adenine dinucleotide phosphate (NADPH) as a reducing agent in the reaction, converting it to NADP+. The medical definition of Glutathione Reductase is:

Glutathione reductase (GSR; EC 1.8.1.7) is a homodimeric flavoprotein that catalyzes the reduction of oxidized glutathione (GSSG) to reduced glutathione (GSH) in the presence of NADPH as a cofactor. This enzyme is essential for maintaining the cellular redox balance and protecting cells from oxidative stress by regenerating the active form of glutathione, a vital antioxidant and detoxifying agent.

Flavin Mononucleotide (FMN) Reductase is an enzyme that catalyzes the reduction of FMN to FMNH2 using NADH or NADPH as an electron donor. This enzyme plays a crucial role in the electron transport chain and is involved in various redox reactions within the cell. It is found in many organisms, including bacteria, fungi, plants, and animals. In humans, FMN Reductase is encoded by the RIBFLR gene and is primarily located in the mitochondria. Defects in this enzyme can lead to various metabolic disorders.

Thioredoxin-disulfide reductase (Txnrd, TrxR) is an enzyme that belongs to the pyridine nucleotide-disulfide oxidoreductase family. It plays a crucial role in maintaining the intracellular redox balance by reducing disulfide bonds in proteins and keeping them in their reduced state. This enzyme utilizes NADPH as an electron donor to reduce thioredoxin (Trx), which then transfers its electrons to various target proteins, thereby regulating their activity, protein folding, and antioxidant defense mechanisms.

Txnrd is essential for several cellular processes, including DNA synthesis, gene expression, signal transduction, and protection against oxidative stress. Dysregulation of Txnrd has been implicated in various pathological conditions, such as cancer, neurodegenerative diseases, and inflammatory disorders. Therefore, understanding the function and regulation of this enzyme is of great interest for developing novel therapeutic strategies.

NADPH-ferrihemoprotein reductase, also known as diaphorase or NO synthase reductase, is an enzyme that catalyzes the reduction of ferrihemoproteins using NADPH as a reducing cofactor. This reaction plays a crucial role in various biological processes such as the detoxification of certain compounds and the regulation of cellular signaling pathways.

The systematic name for this enzyme is NADPH:ferrihemoprotein oxidoreductase, and it belongs to the family of oxidoreductases that use NADH or NADPH as electron donors. The reaction catalyzed by this enzyme can be represented as follows:

NADPH + H+ + ferrihemoprotein ↔ NADP+ + ferrohemoprotein

In this reaction, the ferric (FeIII) form of hemoproteins is reduced to its ferrous (FeII) form by accepting electrons from NADPH. This enzyme is widely distributed in various tissues and organisms, including bacteria, fungi, plants, and animals. It has been identified as a component of several multi-enzyme complexes involved in different metabolic pathways, such as nitric oxide synthase (NOS) and cytochrome P450 reductase.

In summary, NADPH-ferrihemoprotein reductase is an essential enzyme that catalyzes the reduction of ferrihemoproteins using NADPH as a reducing agent, playing a critical role in various biological processes and metabolic pathways.

Ferredoxin-NADP Reductase (FDNR) is an enzyme that catalyzes the electron transfer from ferredoxin to NADP+, reducing it to NADPH. This reaction plays a crucial role in several metabolic pathways, including photosynthesis and nitrogen fixation.

In photosynthesis, FDNR is located in the stroma of chloroplasts and receives electrons from ferredoxin, which is reduced by photosystem I. The enzyme then transfers these electrons to NADP+, generating NADPH, which is used in the Calvin cycle for carbon fixation.

In nitrogen fixation, FDNR is found in the nitrogen-fixing bacteria and receives electrons from ferredoxin, which is reduced by nitrogenase. The enzyme then transfers these electrons to NADP+, generating NADPH, which is used in the reduction of nitrogen gas (N2) to ammonia (NH3).

FDNR is a flavoprotein that contains a FAD cofactor and an iron-sulfur cluster. The enzyme catalyzes the electron transfer through a series of conformational changes that bring ferredoxin and NADP+ in close proximity, allowing for efficient electron transfer.

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.

Cytochrome reductases are a group of enzymes that play a crucial role in the electron transport chain, a process that occurs in the mitochondria of cells and is responsible for generating energy in the form of ATP (adenosine triphosphate). Specifically, cytochrome reductases are responsible for transferring electrons from one component of the electron transport chain to another, specifically to cytochromes.

There are several types of cytochrome reductases, including NADH dehydrogenase (also known as Complex I), succinate dehydrogenase (also known as Complex II), and ubiquinone-cytochrome c reductase (also known as Complex III). These enzymes help to facilitate the flow of electrons through the electron transport chain, which is essential for the production of ATP and the maintenance of cellular homeostasis.

Defects in cytochrome reductases can lead to a variety of mitochondrial diseases, which can affect multiple organ systems and may be associated with symptoms such as muscle weakness, developmental delays, and cardiac dysfunction.

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

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

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

Tetrahydrofolate dehydrogenase (EC 1.5.1.20) is an enzyme involved in folate metabolism. The enzyme catalyzes the oxidation of tetrahydrofolate (THF) to dihydrofolate (DHF), while simultaneously reducing NADP+ to NADPH.

The reaction can be summarized as follows:

THF + NADP+ -> DHF + NADPH + H+

This enzyme plays a crucial role in the synthesis of purines and thymidylate, which are essential components of DNA and RNA. Therefore, any defects or deficiencies in tetrahydrofolate dehydrogenase can lead to various medical conditions, including megaloblastic anemia and neural tube defects during fetal development.

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.

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.

Methionine sulfoxide reductases (MSRs) are a group of enzymes that catalyze the reduction of methionine sulfoxides back to methionine in proteins. Methionine residues in proteins can be oxidized by reactive oxygen species (ROS) or other oxidizing agents, leading to the formation of methionine sulfoxide. This modification can affect protein function and stability. MSRs play a crucial role in protecting proteins from oxidative damage and maintaining their proper function.

There are two types of MSRs, designated as MSRA and MSRB. MSRA reduces methionine-S-sulfoxides, while MSRB reduces methionine-R-sulfoxides. Both enzymes require the cofactor thioredoxin to reduce the methionine sulfoxide back to methionine. The activity of MSRs is important in various biological processes, including protein folding, stress response, and aging. Defects in MSRs have been implicated in several diseases, such as Alzheimer's disease, Parkinson's disease, and cancer.

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

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

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

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

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.

Ribonucleoside Diphosphate Reductase (RNR) is an enzyme that plays a crucial role in the regulation of DNA synthesis and repair. It catalyzes the conversion of ribonucleoside diphosphates (NDPs) to deoxyribonucleoside diphosphates (dNDPs), which are the building blocks of DNA. This reaction is essential for the synthesis of new DNA strands during replication and repair processes. The enzyme's activity is tightly regulated, as it must be carefully controlled to prevent errors in DNA synthesis that could lead to mutations and genomic instability. RNR is a target for chemotherapeutic agents due to its essential role in DNA synthesis.

Hydroxymethylglutaryl-CoA (HMG-CoA) reductase inhibitors, also known as statins, are a class of cholesterol-lowering medications. They work by inhibiting the enzyme HMG-CoA reductase, which plays a central role in the production of cholesterol in the liver. By blocking this enzyme, the liver is stimulated to take up more low-density lipoprotein (LDL) cholesterol from the bloodstream, leading to a decrease in LDL cholesterol levels and a reduced risk of cardiovascular disease.

Examples of HMG-CoA reductase inhibitors include atorvastatin, simvastatin, pravastatin, rosuvastatin, and fluvastatin. These medications are commonly prescribed to individuals with high cholesterol levels, particularly those who are at risk for or have established cardiovascular disease.

It's important to note that while HMG-CoA reductase inhibitors can be effective in reducing LDL cholesterol levels and the risk of cardiovascular events, they should be used as part of a comprehensive approach to managing high cholesterol, which may also include lifestyle modifications such as dietary changes, exercise, and weight management.

Quinone reductases are a group of enzymes that catalyze the reduction of quinones to hydroquinones, using NADH or NADPH as an electron donor. This reaction is important in the detoxification of quinones, which are potentially toxic compounds produced during the metabolism of certain drugs, chemicals, and endogenous substances.

There are two main types of quinone reductases: NQO1 (NAD(P)H:quinone oxidoreductase 1) and NQO2 (NAD(P)H:quinone oxidoreductase 2). NQO1 is a cytosolic enzyme that can reduce a wide range of quinones, while NQO2 is a mitochondrial enzyme with a narrower substrate specificity.

Quinone reductases have been studied for their potential role in cancer prevention and treatment, as they may help to protect cells from oxidative stress and DNA damage caused by quinones and other toxic compounds. Additionally, some quinone reductase inhibitors have been developed as chemotherapeutic agents, as they can enhance the cytotoxicity of certain drugs that require quinone reduction for activation.

Hypoxia-Inducible Factor 1 (HIF-1) is a transcription factor that plays a crucial role in the body's response to low oxygen levels, also known as hypoxia. HIF-1 is a heterodimeric protein composed of two subunits: an alpha subunit (HIF-1α) and a beta subunit (HIF-1β).

The alpha subunit, HIF-1α, is the regulatory subunit that is subject to oxygen-dependent degradation. Under normal oxygen conditions (normoxia), HIF-1α is constantly produced in the cell but is rapidly degraded by proteasomes due to hydroxylation of specific proline residues by prolyl hydroxylase domain-containing proteins (PHDs). This hydroxylation reaction requires oxygen as a substrate, and under hypoxic conditions, the activity of PHDs is inhibited, leading to the stabilization and accumulation of HIF-1α.

Once stabilized, HIF-1α translocates to the nucleus, where it heterodimerizes with HIF-1β and binds to hypoxia-responsive elements (HREs) in the promoter regions of target genes. This binding results in the activation of gene transcription programs that promote cellular adaptation to low oxygen levels. These adaptive responses include increased erythropoiesis, angiogenesis, glucose metabolism, and pH regulation, among others.

Therefore, HIF-1α is a critical regulator of the body's response to hypoxia, and its dysregulation has been implicated in various pathological conditions, including cancer, cardiovascular disease, and neurodegenerative disorders.

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.

NADH, NADPH oxidoreductases are a class of enzymes that catalyze the redox reaction between NADH or NADPH and various electron acceptors. These enzymes play a crucial role in cellular metabolism by transferring electrons from NADH or NADPH to other molecules, which is essential for many biochemical reactions.

NADH (nicotinamide adenine dinucleotide hydrogen) and NADPH (nicotinamide adenine dinucleotide phosphate hydrogen) are coenzymes that act as electron carriers in redox reactions. They consist of a nicotinamide ring, which undergoes reduction or oxidation by accepting or donating electrons and a proton (H+).

NADH, NADPH oxidoreductases are classified based on their structure and mechanism of action. Some examples include:

1. Dehydrogenases: These enzymes catalyze the oxidation of NADH or NADPH to NAD+ or NADP+ while reducing an organic substrate. Examples include lactate dehydrogenase, alcohol dehydrogenase, and malate dehydrogenase.
2. Oxidases: These enzymes catalyze the oxidation of NADH or NADPH to NAD+ or NADP+ while reducing molecular oxygen (O2) to water (H2O). Examples include NADH oxidase and NADPH oxidase.
3. Reductases: These enzymes catalyze the reduction of various electron acceptors using NADH or NADPH as a source of electrons. Examples include glutathione reductase, thioredoxin reductase, and nitrate reductase.

Overall, NADH, NADPH oxidoreductases are essential for maintaining the redox balance in cells and play a critical role in various metabolic pathways, including energy production, detoxification, and biosynthesis.

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.

Dihydropteridine reductase is an enzyme that plays a crucial role in the metabolism of certain amino acids, specifically phenylalanine and tyrosine. This enzyme is responsible for reducing dihydropteridines to tetrahydropteridines, which is a necessary step in the regeneration of tetrahydrobiopterin (BH4), an essential cofactor for the enzymes phenylalanine hydroxylase and tyrosine hydroxylase.

Phenylalanine hydroxylase and tyrosine hydroxylase are involved in the conversion of the amino acids phenylalanine and tyrosine to tyrosine and dopa, respectively. Without sufficient BH4, these enzymes cannot function properly, leading to an accumulation of phenylalanine and a decrease in the levels of important neurotransmitters such as dopamine, norepinephrine, and serotonin.

Deficiency in dihydropteridine reductase can lead to a rare genetic disorder known as dihydropteridine reductase deficiency (DPRD), which is characterized by elevated levels of phenylalanine and neurotransmitter imbalances, resulting in neurological symptoms such as developmental delay, seizures, and hypotonia. Treatment typically involves a low-phenylalanine diet and supplementation with BH4.

Oxidation-Reduction (redox) reactions are a type of chemical reaction involving a transfer of electrons between two species. The substance that loses electrons in the reaction is oxidized, and the substance that gains electrons is reduced. Oxidation and reduction always occur together in a redox reaction, hence the term "oxidation-reduction."

In biological systems, redox reactions play a crucial role in many cellular processes, including energy production, metabolism, and signaling. The transfer of electrons in these reactions is often facilitated by specialized molecules called electron carriers, such as nicotinamide adenine dinucleotide (NAD+/NADH) and flavin adenine dinucleotide (FAD/FADH2).

The oxidation state of an element in a compound is a measure of the number of electrons that have been gained or lost relative to its neutral state. In redox reactions, the oxidation state of one or more elements changes as they gain or lose electrons. The substance that is oxidized has a higher oxidation state, while the substance that is reduced has a lower oxidation state.

Overall, oxidation-reduction reactions are fundamental to the functioning of living organisms and are involved in many important biological processes.

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.

Thioredoxin Reductase 1 (TXNRD1) is an enzyme that belongs to the thioredoxin reductase family. It is a homodimeric flavoprotein that contains a selenocysteine residue at its active site, which is essential for its catalytic activity.

The primary function of TXNRD1 is to reduce and regenerate the oxidized form of thioredoxin (TXN) by using NADPH as an electron donor. Thioredoxin is a small protein that plays a crucial role in maintaining the redox balance within the cell by regulating various cellular processes, such as DNA synthesis, gene expression, and apoptosis.

TXNRD1 is widely expressed in various tissues and is localized in the cytosol of the cell. It has been implicated in several physiological and pathological processes, including inflammation, oxidative stress, cancer, and neurodegenerative diseases. Inhibition of TXNRD1 has been shown to have potential therapeutic benefits in various disease models, making it an attractive target for drug development.

In enzymology, a cholestenone 5alpha-reductase (EC 1.3.1.22) is an enzyme that catalyzes the chemical reaction 5alpha-cholestan ... Other names in common use include testosterone Delta4-5alpha-reductase, steroid 5alpha-reductase, 3-oxosteroid Delta4- ... 4-ene-5alpha-reductase, Delta4-3-ketosteroid 5alpha-oxidoreductase, cholest-4-en-3-one 5alpha-reductase, and testosterone ... 3-oxosteroid 5alpha-reductase, testosterone Delta4-hydrogenase, 4-ene-3-oxosteroid 5alpha-reductase, reduced nicotinamide ...
... alpha -substrate}+NADP+}}} 5α-DHP is a major hormone in circulation of normal cycling and pregnant women. 5α-Reductase is most ... Cholestenone5α-Cholestanone Progesterone → 5α-Dihydroprogesterone 3α-Dihydroprogesterone → Allopregnanolone 3β- ... Killian J, Pratis K, Clifton RJ, Stanton PG, Robertson DM, O'Donnell L (May 2003). "5alpha-reductase isoenzymes 1 and 2 in the ... Thiele S, Hoppe U, Holterhus PM, Hiort O (June 2005). "Isoenzyme type 1 of 5alpha-reductase is abundantly transcribed in normal ...
... cholestenone 5β-reductase, cortisone 5β-reductase, cortisone Δ4-5β-reductase, steroid 5β-reductase, testosterone 5β-reductase, ... Delta4-3-oxosteroid+5beta-reductase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology ( ... Charbonneau A, The VL (January 2001). "Genomic organization of a human 5beta-reductase and its pseudogene and substrate ... 5β-Reductase, or Δ4-3-oxosteroid 5β-reductase (EC 1.3.1.3, 3-oxo-Δ4-steroid 5β-reductase, androstenedione 5β-reductase, ...
... cholestenone 5alpha-reductase MeSH D08.811.682.660.250 - coproporphyrinogen oxidase MeSH D08.811.682.660.275 - ... gtp-binding protein alpha subunits MeSH D08.811.277.040.330.300.200.100.100 - gtp-binding protein alpha subunits, g12-g13 MeSH ... gmp reductase MeSH D08.811.682.655.500 - nitrate reductases MeSH D08.811.682.655.500.124 - nitrate reductase MeSH D08.811. ... nitrite reductases MeSH D08.811.682.655.750.249 - ferredoxin-nitrite reductase MeSH D08.811.682.655.750.500 - nitrite reductase ...
"Cholestenone 5 alpha-Reductase" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH ( ... This graph shows the total number of publications written about "Cholestenone 5 alpha-Reductase" by people in this website by ... Below are the most recent publications written about "Cholestenone 5 alpha-Reductase" by people in Profiles. ... Below are MeSH descriptors whose meaning is more general than "Cholestenone 5 alpha-Reductase". ...
In enzymology, a cholestenone 5alpha-reductase (EC 1.3.1.22) is an enzyme that catalyzes the chemical reaction 5alpha-cholestan ... Other names in common use include testosterone Delta4-5alpha-reductase, steroid 5alpha-reductase, 3-oxosteroid Delta4- ... 4-ene-5alpha-reductase, Delta4-3-ketosteroid 5alpha-oxidoreductase, cholest-4-en-3-one 5alpha-reductase, and testosterone ... 3-oxosteroid 5alpha-reductase, testosterone Delta4-hydrogenase, 4-ene-3-oxosteroid 5alpha-reductase, reduced nicotinamide ...
... coactivates the cardiac-enriched nuclear receptors estrogen-related receptor-alpha and -gamma. Identification of novel leucine- ... Enoyl-(Acyl-Carrier Protein) Reductase (NADPH, B-Specific). *Enoyl-(Acyl-Carrier-Protein) Reductase (NADH) ... Cholestenone 5 alpha-Reductase. *Coproporphyrinogen Oxidase. *Dihydrodipicolinate Reductase. *Dihydroorotate Oxidase. * ...
Cholestenone 5 alpha-Reductase. *Coproporphyrinogen Oxidase. *Dihydrodipicolinate Reductase. *Dihydroorotate Oxidase. * ... Enoyl-(Acyl-Carrier Protein) Reductase (NADPH, B-Specific)*Enoyl-(Acyl-Carrier Protein) Reductase (NADPH, B-Specific) ... Below are the most recent publications written about "Enoyl-(Acyl-Carrier Protein) Reductase (NADPH, B-Specific)" by people in ... This graph shows the total number of publications written about "Enoyl-(Acyl-Carrier Protein) Reductase (NADPH, B-Specific)" by ...
Enoyl-(Acyl-Carrier Protein) Reductase (NADPH, B-Specific) [D08.811.682.660.390] Enoyl-(Acyl-Carrier Protein) Reductase (NADPH ... Cholestenone 5 alpha-Reductase [D08.811.682.660.200] Cholestenone 5 alpha-Reductase * Coproporphyrinogen Oxidase [D08.811. ...
Cholestenone 5 alpha-Reductase/pharmacology , Chromatography, High Pressure Liquid , Lignans/pharmacology , Magnetic Resonance ... 5. Phytochemistry and biological properties of Drimys winteri JR et G. Forster var chilensis (DC) A / Fitoquímica y propiedades ... The inhibitory activities on 5α-reductase were evaluated in vitro. As a result, ten secolignans,(2R,4S)-2,4-bis(3-methoxyl-4- ... Compound 7 was potent in inhibiting 5α-reductase.. Subject(s). 5-alpha Reductase Inhibitors , ...
Enoyl-(Acyl-Carrier Protein) Reductase (NADPH, B-Specific). *Enoyl-(Acyl-Carrier-Protein) Reductase (NADH) ... Cholestenone 5 alpha-Reductase. *Coproporphyrinogen Oxidase. *Dihydrodipicolinate Reductase. *Dihydroorotate Oxidase. * ...
Cholestenone 5 alpha-Reductase. Colestenona 5 alfa-Reductasa. Complexo Citocromos b6f. Cytochrome b6f Complex. Complejo de ... GTP-Binding Protein alpha Subunits, G12-G13. Subunidades alfa de la Proteína de Enlace a GTP G12-G13. ... Methylenetetrahydrofolate Reductase (NADPH2). Metilenotetrahidrofolato Reductasa (NADPH2). Metilmalonil-CoA Descarboxilase. ... GTP-Binding Protein alpha Subunits, Gq-G11. Subunidades alfa de Proteína de Enlace a GTP Gq-G11. ...
Cholestenone 5 alpha-Reductase. Colestenona 5 alfa-Redutase. Complejo I de Transporte de Electrón. Electron Transport Complex I ... GTP-Binding Protein alpha Subunits, Gq-G11. Subunidades alfa Gq-G11 de Proteína de Ligação a GTP. ... Methylenetetrahydrofolate Reductase (NADPH2). Metilenotetraidrofolato Redutase (NADPH2). Metilmalonil-CoA Descarboxilasa. ... GTP-Binding Protein alpha Subunits, G12-G13. Subunidades alfa G12-G13 de Proteína de Ligação a GTP. ...
Cholestenone 5 alpha-Reductase. Colestenona 5 alfa-Redutase. Complejo I de Transporte de Electrón. Electron Transport Complex I ... GTP-Binding Protein alpha Subunits, Gq-G11. Subunidades alfa Gq-G11 de Proteína de Ligação a GTP. ... Methylenetetrahydrofolate Reductase (NADPH2). Metilenotetraidrofolato Redutase (NADPH2). Metilmalonil-CoA Descarboxilasa. ... GTP-Binding Protein alpha Subunits, G12-G13. Subunidades alfa G12-G13 de Proteína de Ligação a GTP. ...
Cholestenone 5 alpha-Reductase. Colestenona 5 alfa-Redutase. Complejo I de Transporte de Electrón. Electron Transport Complex I ... GTP-Binding Protein alpha Subunits, Gq-G11. Subunidades alfa Gq-G11 de Proteína de Ligação a GTP. ... Methylenetetrahydrofolate Reductase (NADPH2). Metilenotetraidrofolato Redutase (NADPH2). Metilmalonil-CoA Descarboxilasa. ... GTP-Binding Protein alpha Subunits, G12-G13. Subunidades alfa G12-G13 de Proteína de Ligação a GTP. ...
GTP-Binding Protein alpha Subunits. Subunidades alfa de Proteína de Ligação a GTP. Subunidades alfa de la Proteína de Enlace a ... Cholestenone 5 alpha-Reductase. Colestenona 5 alfa-Redutase. Colestenona 5 alfa-Reductasa. ... Methylenetetrahydrofolate Reductase (NADPH2). Metilenotetraidrofolato Redutase (NADPH2). Metilenotetrahidrofolato Reductasa ( ... GTP-Binding Protein alpha Subunits, G12-G13. Subunidades alfa G12-G13 de Proteína de Ligação a GTP. Subunidades alfa de la ...
Cholestenone 5 alpha-Reductase. Colestenona 5 alfa-Reductasa. Complexo Citocromos b6f. Cytochrome b6f Complex. Complejo de ... GTP-Binding Protein alpha Subunits, G12-G13. Subunidades alfa de la Proteína de Enlace a GTP G12-G13. ... Methylenetetrahydrofolate Reductase (NADPH2). Metilenotetrahidrofolato Reductasa (NADPH2). Metilmalonil-CoA Descarboxilase. ... GTP-Binding Protein alpha Subunits, Gq-G11. Subunidades alfa de Proteína de Enlace a GTP Gq-G11. ...
Cholestenone 5 alpha-Reductase. Colestenona 5 alfa-Reductasa. Complexo Citocromos b6f. Cytochrome b6f Complex. Complejo de ... GTP-Binding Protein alpha Subunits, G12-G13. Subunidades alfa de la Proteína de Enlace a GTP G12-G13. ... Methylenetetrahydrofolate Reductase (NADPH2). Metilenotetrahidrofolato Reductasa (NADPH2). Metilmalonil-CoA Descarboxilase. ... GTP-Binding Protein alpha Subunits, Gq-G11. Subunidades alfa de Proteína de Enlace a GTP Gq-G11. ...
GTP-Binding Protein alpha Subunits. Subunidades alfa de Proteína de Ligação a GTP. Subunidades alfa de la Proteína de Enlace a ... Cholestenone 5 alpha-Reductase. Colestenona 5 alfa-Redutase. Colestenona 5 alfa-Reductasa. ... Methylenetetrahydrofolate Reductase (NADPH2). Metilenotetraidrofolato Redutase (NADPH2). Metilenotetrahidrofolato Reductasa ( ... GTP-Binding Protein alpha Subunits, G12-G13. Subunidades alfa G12-G13 de Proteína de Ligação a GTP. Subunidades alfa de la ...
Cholestenone 5 alpha-Reductase. Colestenona 5 alfa-Redutase. Complejo I de Transporte de Electrón. Electron Transport Complex I ... GTP-Binding Protein alpha Subunits, Gq-G11. Subunidades alfa Gq-G11 de Proteína de Ligação a GTP. ... Methylenetetrahydrofolate Reductase (NADPH2). Metilenotetraidrofolato Redutase (NADPH2). Metilmalonil-CoA Descarboxilasa. ... GTP-Binding Protein alpha Subunits, G12-G13. Subunidades alfa G12-G13 de Proteína de Ligação a GTP. ...
GTP-Binding Protein alpha Subunits. Subunidades alfa de Proteína de Ligação a GTP. Subunidades alfa de la Proteína de Enlace a ... Cholestenone 5 alpha-Reductase. Colestenona 5 alfa-Redutase. Colestenona 5 alfa-Reductasa. ... Methylenetetrahydrofolate Reductase (NADPH2). Metilenotetraidrofolato Redutase (NADPH2). Metilenotetrahidrofolato Reductasa ( ... GTP-Binding Protein alpha Subunits, G12-G13. Subunidades alfa G12-G13 de Proteína de Ligação a GTP. Subunidades alfa de la ...
Cholestenone 5 alpha-Reductase. Colestenona 5 alfa-Redutase. Complejo I de Transporte de Electrón. Electron Transport Complex I ... GTP-Binding Protein alpha Subunits, Gq-G11. Subunidades alfa Gq-G11 de Proteína de Ligação a GTP. ... Methylenetetrahydrofolate Reductase (NADPH2). Metilenotetraidrofolato Redutase (NADPH2). Metilmalonil-CoA Descarboxilasa. ... GTP-Binding Protein alpha Subunits, G12-G13. Subunidades alfa G12-G13 de Proteína de Ligação a GTP. ...
GTP-Binding Protein alpha Subunits. Subunidades alfa de Proteína de Ligação a GTP. Subunidades alfa de la Proteína de Enlace a ... Cholestenone 5 alpha-Reductase. Colestenona 5 alfa-Redutase. Colestenona 5 alfa-Reductasa. ... Methylenetetrahydrofolate Reductase (NADPH2). Metilenotetraidrofolato Redutase (NADPH2). Metilenotetrahidrofolato Reductasa ( ... GTP-Binding Protein alpha Subunits, G12-G13. Subunidades alfa G12-G13 de Proteína de Ligação a GTP. Subunidades alfa de la ...
Cholestenone 5 alpha-Reductase/analogs & derivatives. 5-alpha Reductase Inhibitors. Lacrimal Duct Obstruction/surgery. ... 5. Tularemia. *Removing redundant information found elsewhere in the MeSH Browser record. For example, this 2015 annotation has ...
Polymorphisms within the 5alpha-reductase gene are interesting biomarkers for the development of benign prostatic hyperplasia ... Cholestenone 5 alpha-Reductase Actions. * Search in PubMed * Search in MeSH * Add to Search ... The 5alpha-reductase type II A49T and V89L high-activity allelic variants are more common in men with prostate cancer compared ... In parallel, polymorphisms within the 5alpha-reductase gene (SRD5A2 V89L and A49T), the androgen receptor gene (AR; number of ...
Cholestenone 5 alpha-Reductase / antagonists & inhibitors* Actions. * Search in PubMed * Search in MeSH ... A review of the clinical efficacy and safety of 5alpha-reductase inhibitors for the enlarged prostate. Naslund MJ, Miner M. ... The REDUCE trial: chemoprevention in prostate cancer using a dual 5alpha-reductase inhibitor, dutasteride. Musquera M, Fleshner ... 5-alpha-reductase and the development of the human prostate. Radmayr C, Lunacek A, Schwentner C, Oswald J, Klocker H, Bartsch G ...
alpha-Reductase, Cholestenone 5. Tree number(s):. D08.811.682.660.200. RDF Unique Identifier:. https://id.nlm.nih.gov/mesh/ ... Enoyl-(Acyl-Carrier Protein) Reductase (NADPH, B-Specific) [D08.811.682.660.390] Enoyl-(Acyl-Carrier Protein) Reductase (NADPH ... Cholestenone 5 alpha-Reductase - Preferred Concept UI. M0072874. Scope note. An oxidoreductase that catalyzes the conversion of ... Cholestenone 5 alpha-Reductase Entry term(s). 4 Ene Steroid 5 alpha Reductase 4-Ene Steroid 5 alpha-Reductase 5 alpha Reductase ...
Enoyl-(Acyl-Carrier-Protein) Reductase (NADH) [D08.811.682.660.387] * Enoyl-(Acyl-Carrier Protein) Reductase (NADPH, B-Specific ... Cholestenone 5 alpha-Reductase Preferred Concept UI. M0072874. Registry Number. EC 1.3.1.22. Related Numbers. 37255-34-8. EC ... Cholestenone 5 alpha-Reductase Preferred Term Term UI T102877. LexicalTag NON. ThesaurusID NLM (2004). ... 2004; use CHOLESTENONE 5 ALPHA-REDUCTASE (NM) 1980-2003. Entry Combination. analogs & derivatives:5-alpha Reductase Inhibitors ...
Enoyl-(Acyl-Carrier-Protein) Reductase (NADH) [D08.811.682.660.387] * Enoyl-(Acyl-Carrier Protein) Reductase (NADPH, B-Specific ... Cholestenone 5 alpha-Reductase Preferred Concept UI. M0072874. Registry Number. EC 1.3.1.22. Related Numbers. 37255-34-8. EC ... Cholestenone 5 alpha-Reductase Preferred Term Term UI T102877. LexicalTag NON. ThesaurusID NLM (2004). ... 2004; use CHOLESTENONE 5 ALPHA-REDUCTASE (NM) 1980-2003. Entry Combination. analogs & derivatives:5-alpha Reductase Inhibitors ...
13-dienoic Acid N0000167928 15-Oxoprostaglandin 13-Reductase N0000171021 16,16-Dimethylprostaglandin E2 N0000179012 17-alpha- ... N0000167934 Cholestenone 5 alpha-Reductase N0000167434 Cholestenones N0000007064 Cholesterol N0000170032 Cholesterol 7-alpha- ... alpha 1-Antitrypsin N0000169495 alpha Catenin N0000169678 alpha Karyopherins N0000170004 alpha-2-Antiplasmin N0000183458 alpha- ... alpha-Galactosidase N0000178561 alpha-Globins N0000007645 Alpha-Globulins N0000167711 alpha-Glucosidases N0000167712 alpha-L- ...
AN - /DEFIC: consider also ALPHA-MANNOSIDOSIS HN - 2004; use ALPHA-MANNOSIDASE (NM) 1980-2003 BX - Lysosomal alpha-Mannosidase ... HN - 2004; use METHYLENETETRAHYDROFOLATE REDUCTASE (NADPH2) (NM) 1986-2003 BX - Methylene-THF Reductase (NADPH) MH - ... HN - 2004; use CHOLESTENONE 5 ALPHA-REDUCTASE (NM) 1980-2003 MH - Chondrus UI - D044723 MN - B2.100.150 MS - A genus of RED ... G alpha q Protein BX - G-Protein, Gq BX - G-Protein, Gq alpha Family BX - G-Protein, Gq-G11 alpha Family MH - GTP-Binding ...
Cholestenone 5alpha-reductase Current Synonym true false 2647400010 3-Oxo-5alpha-steroid delta^4^-dehydrogenase Current Synonym ... Testosterone 5-alpha-reductase Current Synonym true false 144134010 ... Cholestenone 5alpha-reductase (substance). Code System Preferred Concept Name. Cholestenone 5alpha-reductase (substance). ...
5alpha-Reductase 1 is expressed in all portions of the hair follicle, whereas 5alpha-Reductase 2 is expressed only in ... alpha polypeptide 1 (3-oxo-5 alpha-steroid delta 4-dehydrogenase alpha 1) ... cholestenone 5-alpha-reductase activity NADPH binding ... In addition, 5alpha-Reductase 1 is mainly expressed in human ... Steroid 5alpha-Reductase is an important enzyme in androgen physiology because it catalyzes the conversion of testosterone into ...
Enoyl-(Acyl-Carrier-Protein) Reductase (NADH) [D08.811.682.660.387] * Enoyl-(Acyl-Carrier Protein) Reductase (NADPH, B-Specific ... Cholestenone 5 alpha-Reductase [D08.811.682.660.200] * Coproporphyrinogen Oxidase [D08.811.682.660.250] ... It catalyzes the catabolism of THYMINE; URACIL and the chemotherapeutic drug, 5-FLUOROURACIL.. Terms. Dihydrouracil ... It catalyzes the catabolism of THYMINE; URACIL and the chemotherapeutic drug, 5-FLUOROURACIL.. Entry Term(s). Dihydropyrimidine ...
Cholestenone 5 alpha-Reductase. Colestenona 5 alfa-Reductasa. Complexo Citocromos b6f. Cytochrome b6f Complex. Complejo de ... GTP-Binding Protein alpha Subunits, G12-G13. Subunidades alfa de la Proteína de Enlace a GTP G12-G13. ... Methylenetetrahydrofolate Reductase (NADPH2). Metilenotetrahidrofolato Reductasa (NADPH2). Metilmalonil-CoA Descarboxilase. ... GTP-Binding Protein alpha Subunits, Gq-G11. Subunidades alfa de Proteína de Enlace a GTP Gq-G11. ...
Cholestenone 5 alpha-Reductase. Colestenona 5 alfa-Reductasa. Complexo Citocromos b6f. Cytochrome b6f Complex. Complejo de ... GTP-Binding Protein alpha Subunits, G12-G13. Subunidades alfa de la Proteína de Enlace a GTP G12-G13. ... Methylenetetrahydrofolate Reductase (NADPH2). Metilenotetrahidrofolato Reductasa (NADPH2). Metilmalonil-CoA Descarboxilase. ... GTP-Binding Protein alpha Subunits, Gq-G11. Subunidades alfa de Proteína de Enlace a GTP Gq-G11. ...
Cholestenone 5 alpha-Reductase. Colestenona 5 alfa-Reductasa. Complexo Citocromos b6f. Cytochrome b6f Complex. Complejo de ... GTP-Binding Protein alpha Subunits, G12-G13. Subunidades alfa de la Proteína de Enlace a GTP G12-G13. ... Methylenetetrahydrofolate Reductase (NADPH2). Metilenotetrahidrofolato Reductasa (NADPH2). Metilmalonil-CoA Descarboxilase. ... GTP-Binding Protein alpha Subunits, Gq-G11. Subunidades alfa de Proteína de Enlace a GTP Gq-G11. ...
GTP-Binding Protein alpha Subunits. Subunidades alfa de Proteína de Ligação a GTP. Subunidades alfa de la Proteína de Enlace a ... Cholestenone 5 alpha-Reductase. Colestenona 5 alfa-Redutase. Colestenona 5 alfa-Reductasa. ... Methylenetetrahydrofolate Reductase (NADPH2). Metilenotetraidrofolato Redutase (NADPH2). Metilenotetrahidrofolato Reductasa ( ... GTP-Binding Protein alpha Subunits, G12-G13. Subunidades alfa G12-G13 de Proteína de Ligação a GTP. Subunidades alfa de la ...
GTP-Binding Protein alpha Subunits. Subunidades alfa de Proteína de Ligação a GTP. Subunidades alfa de la Proteína de Enlace a ... Cholestenone 5 alpha-Reductase. Colestenona 5 alfa-Redutase. Colestenona 5 alfa-Reductasa. ... Methylenetetrahydrofolate Reductase (NADPH2). Metilenotetraidrofolato Redutase (NADPH2). Metilenotetrahidrofolato Reductasa ( ... GTP-Binding Protein alpha Subunits, G12-G13. Subunidades alfa G12-G13 de Proteína de Ligação a GTP. Subunidades alfa de la ...
Cholestenone 5 alpha-Reductase. Colestenona 5 alfa-Reductasa. Complexo Citocromos b6f. Cytochrome b6f Complex. Complejo de ... GTP-Binding Protein alpha Subunits, G12-G13. Subunidades alfa de la Proteína de Enlace a GTP G12-G13. ... Methylenetetrahydrofolate Reductase (NADPH2). Metilenotetrahidrofolato Reductasa (NADPH2). Metilmalonil-CoA Descarboxilase. ... GTP-Binding Protein alpha Subunits, Gq-G11. Subunidades alfa de Proteína de Enlace a GTP Gq-G11. ...
Cholestenone 5 alpha-Reductase. Colestenona 5 alfa-Reductasa. Complexo Citocromos b6f. Cytochrome b6f Complex. Complejo de ... GTP-Binding Protein alpha Subunits, G12-G13. Subunidades alfa de la Proteína de Enlace a GTP G12-G13. ... Methylenetetrahydrofolate Reductase (NADPH2). Metilenotetrahidrofolato Reductasa (NADPH2). Metilmalonil-CoA Descarboxilase. ... GTP-Binding Protein alpha Subunits, Gq-G11. Subunidades alfa de Proteína de Enlace a GTP Gq-G11. ...
Cholestenone 5 alpha-Reductase. Colestenona 5 alfa-Reductasa. Complexo Citocromos b6f. Cytochrome b6f Complex. Complejo de ... GTP-Binding Protein alpha Subunits, G12-G13. Subunidades alfa de la Proteína de Enlace a GTP G12-G13. ... Methylenetetrahydrofolate Reductase (NADPH2). Metilenotetrahidrofolato Reductasa (NADPH2). Metilmalonil-CoA Descarboxilase. ... GTP-Binding Protein alpha Subunits, Gq-G11. Subunidades alfa de Proteína de Enlace a GTP Gq-G11. ...
Cholestenone 5 alpha-Reductase. Colestenona 5 alfa-Reductasa. Complexo Citocromos b6f. Cytochrome b6f Complex. Complejo de ... GTP-Binding Protein alpha Subunits, G12-G13. Subunidades alfa de la Proteína de Enlace a GTP G12-G13. ... Methylenetetrahydrofolate Reductase (NADPH2). Metilenotetrahidrofolato Reductasa (NADPH2). Metilmalonil-CoA Descarboxilase. ... GTP-Binding Protein alpha Subunits, Gq-G11. Subunidades alfa de Proteína de Enlace a GTP Gq-G11. ...
Cholestenone 5 alpha-Reductase. Colestenona 5 alfa-Reductasa. Complexo Citocromos b6f. Cytochrome b6f Complex. Complejo de ... GTP-Binding Protein alpha Subunits, G12-G13. Subunidades alfa de la Proteína de Enlace a GTP G12-G13. ... Methylenetetrahydrofolate Reductase (NADPH2). Metilenotetrahidrofolato Reductasa (NADPH2). Metilmalonil-CoA Descarboxilase. ... GTP-Binding Protein alpha Subunits, Gq-G11. Subunidades alfa de Proteína de Enlace a GTP Gq-G11. ...
  • This graph shows the total number of publications written about "Cholestenone 5 alpha-Reductase" by people in this website by year, and whether "Cholestenone 5 alpha-Reductase" was a major or minor topic of these publications. (jefferson.edu)
  • In enzymology, a cholestenone 5alpha-reductase (EC 1.3.1.22) is an enzyme that catalyzes the chemical reaction 5alpha-cholestan-3-one + NADP+ ⇌ {\displaystyle \rightleftharpoons } cholest-4-en-3-one + NADPH + H+ Thus, the two substrates of this enzyme are 5alpha-cholestan-3-one and NADP+, whereas its 3 products are cholest-4-en-3-one, NADPH, and H+. (wikipedia.org)
  • Polymorphisms within the 5alpha-reductase gene are interesting biomarkers for the development of benign prostatic hyperplasia and benign prostatic enlargement. (nih.gov)
  • Steroid 5alpha-Reductase is an important enzyme in androgen physiology because it catalyzes the conversion of testosterone into the more potent 5alpha-dihydro-testosterone, which mediates androgen effects on target tissues. (thermofisher.com)
  • In cultured human skin cells, 5alpha-Reductase 1 shows heterogeneity of protein, and has different levels of transcriptional and translational expression. (thermofisher.com)
  • 5alpha-Reductase 1 is expressed in all portions of the hair follicle, whereas 5alpha-Reductase 2 is expressed only in mesenchymal portions. (thermofisher.com)
  • In addition, 5alpha-Reductase 1 is mainly expressed in human breast carcinoma and may play a role in the in situ production and actions of the potent androgen 5alpha-dihydrotestosterone, including inhibition of cancer cell proliferation in hormone-dependent human breast carcinoma. (thermofisher.com)
  • The 5alpha-Reductase-3alpha-hydroxysteroid dehydrogenase complex is present in the human brain, suggesting that the complex may be involved in the synthesis of neuroactive steroids or the catabolism of neurotoxic steroids. (thermofisher.com)
  • URACIL and the chemotherapeutic drug, 5-FLUOROURACIL . (nih.gov)