Enzymes
| UniProtKB help_outline | 4 proteins |
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- Name help_outline (17R,20S)-17,20-dihydroxypregn-4-en-3-one Identifier CHEBI:16418 (Beilstein: 6223300,3214896; CAS: 652-69-7) help_outline Charge 0 Formula C21H32O3 InChIKeyhelp_outline MASCESDECGBIBB-HNXXTFFGSA-N SMILEShelp_outline [H][C@@]12CCC3=CC(=O)CC[C@]3(C)[C@@]1([H])CC[C@@]1(C)[C@@]2([H])CC[C@]1(O)[C@H](C)O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline NADP+ Identifier CHEBI:58349 Charge -3 Formula C21H25N7O17P3 InChIKeyhelp_outline XJLXINKUBYWONI-NNYOXOHSSA-K SMILEShelp_outline NC(=O)c1ccc[n+](c1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](OP([O-])([O-])=O)[C@@H]2O)n2cnc3c(N)ncnc23)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,253 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 17α-hydroxyprogesterone Identifier CHEBI:17252 (Beilstein: 2062088; CAS: 68-96-2) help_outline Charge 0 Formula C21H30O3 InChIKeyhelp_outline DBPWSSGDRRHUNT-CEGNMAFCSA-N SMILEShelp_outline [H][C@@]12CC[C@](O)(C(C)=O)[C@@]1(C)CC[C@@]1([H])[C@@]2([H])CCC2=CC(=O)CC[C@]12C 2D coordinates Mol file for the small molecule Search links Involved in 7 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,176 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline NADPH Identifier CHEBI:57783 (Beilstein: 10411862) help_outline Charge -4 Formula C21H26N7O17P3 InChIKeyhelp_outline ACFIXJIJDZMPPO-NNYOXOHSSA-J SMILEShelp_outline NC(=O)C1=CN(C=CC1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](OP([O-])([O-])=O)[C@@H]2O)n2cnc3c(N)ncnc23)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,247 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:15857 | RHEA:15858 | RHEA:15859 | RHEA:15860 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Related reactions help_outline
More general form(s) of this reaction
Publications
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Relationship of human liver dihydrodiol dehydrogenases to hepatic bile-acid-binding protein and an oxidoreductase of human colon cells.
Hara A., Matsuura K., Tamada Y., Sato K., Miyabe Y., Deyashiki Y., Ishida N.
We previously isolated three monomeric dihydrodiol dehydrogenases, DD1, DD2 and DD4, from human liver, and cloned a cDNA (C9) thought to encode DD2, which is identical with those for human bile-acid-binding protein and an oxidoreductase of human colon carcinoma HT29 cells. In the present study we ... >> More
We previously isolated three monomeric dihydrodiol dehydrogenases, DD1, DD2 and DD4, from human liver, and cloned a cDNA (C9) thought to encode DD2, which is identical with those for human bile-acid-binding protein and an oxidoreductase of human colon carcinoma HT29 cells. In the present study we have provided evidence that the C9 cDNA clone encodes DD1, not DD2. A recombinant enzyme expressed from the cDNA in a bacterial system was purified, and its catalytic properties, bile-acid-binding ability and primary sequence were compared with those of the hepatic dihydrodiol dehydrogenases. The results show that DD1 encoded by C9 possesses prostaglandin F synthase activity but low affinity for lithocholic acid, whereas DD2, showing differences of six amino acid residues from the DD1 sequence, exhibited high-affinity binding for the bile acid. Refined relationship between dihydrodiol dehydrogenases and their related proteins of human tissues is proposed. << Less
Biochem. J. 313:373-376(1996) [PubMed] [EuropePMC]
This publication is cited by 4 other entries.
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Human placental 17 beta-estradiol dehydrogenase and 20 alpha-hydroxysteroid dehydrogenase. Two activities at a single enzyme active site.
Strickler R.C., Tobias B., Covey D.F.
Two soluble enzyme activities, 17 beta-estradiol dehydrogenase and 20 alpha-hydroxysteroid dehydrogenase, present in the cytosol fraction of term human placenta, were co-purified with a constant ratio of specific activities, approximating 100:1, respectively. The "pure enzyme" is a single band on ... >> More
Two soluble enzyme activities, 17 beta-estradiol dehydrogenase and 20 alpha-hydroxysteroid dehydrogenase, present in the cytosol fraction of term human placenta, were co-purified with a constant ratio of specific activities, approximating 100:1, respectively. The "pure enzyme" is a single band on sodium dodecyl sulfate disc gel electrophoresis. To evaluate whether catalysis of the estrogen and progestin substrates occurs at a single active site, alkylation studies using 16 alpha-bromoacetoxyprogesterone were designed. This affinity alkylating steroid binds at the enzyme-active site (km 256 microM; Vmax = 0.012 mumol/min/mg), inactivates the enzyme in an irreversible and time-dependent manner which follows pseudo-first order kinetics, and causes coincident loss of both the 17 beta- and 20 alpha-activities. Affinity radioalkylation studies using 16 alpha-[2'-3H]bromoacetoxyprogesterone indicate that 2 mol of steroid bind per mol of inactivated enzyme dimer (Mr = 68,000). Amino acid analyses of the acid hydrolysate of radioalkylated enzyme show that 16 alpha-bromoacetoxyprogesterone dicarboxymethylates a histidyl residue in the active site. These results are identical with those reported for 16 alpha-[2'-3H]bromoacetoxyestradiol 3-methyl ether inactivation and radioalkylation of identically purified "17 beta-estradiol dehydrogenase." Computer graphics were used to construct a model in which: 1) binding of estrogen and progestin substrates at one active site permits stereospecific catalysis; 2) the estrogen and progestin analogs' alkylating side arms have access to a common histidine residue. These observations clearly demonstrate that the catalysis of estrogen and progestin substrates can occur at a single active site of one enzyme. << Less
J Biol Chem 256:316-321(1981) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Characterization of a human 20alpha-hydroxysteroid dehydrogenase.
Zhang Y., Dufort I., Rheault P., Luu-The V.
It has been suggested that 20alpha-hydroxysteroid dehydrogenase (20alpha-HSD) is a T-cell differentiation marker in mice. In the human, this enzyme has generally been associated with types 1 and 2 17beta-HSDs, which belong to the short-chain alcohol dehydrogenase family, whereas the rat, rabbit, p ... >> More
It has been suggested that 20alpha-hydroxysteroid dehydrogenase (20alpha-HSD) is a T-cell differentiation marker in mice. In the human, this enzyme has generally been associated with types 1 and 2 17beta-HSDs, which belong to the short-chain alcohol dehydrogenase family, whereas the rat, rabbit, pig and bovine 20alpha-HSDs are members of the aldoketo reductase superfamily, which also includes the 3alpha-HSD family. In this study, we report the cloning, from a human skin cDNA library, of a cDNA that shows, after transfection into human embryonic kidney (HEK-293) cells, high 20alpha-HSD activity but negligible 3alpha- and 17beta-hydroxysteroid dehydrogenase activities. A comparison of the amino acid sequence of the human 20alpha-HSD with those of other related 20alpha- and 3alpha-HSDs indicates that the human 20alpha-HSD shares 79.9, 68.7 and 52.3% identity with rabbit, rat and bovine 20alpha-HSDs, whereas it shows 97, 84 and 65% identity with human type 3, type 1 and rat 3alpha-HSDs. In contrast, the enzyme shares only 15.2 and 15.0% identity with type 1 and type 2 human 17beta-HSDs. DNA analysis predicts a protein of 323 amino acids, with a calculated molecular weight of 36 767 Da. In intact transfected cells, the human 20alpha-HSD preferentially catalyzes the reduction of progesterone to 20alpha-hydroxyprogesterone with a K(m) value of 0.6 microM, the reverse reaction (oxidation) being negligible. In a cell cytosolic preparation, the enzyme could use both NADPH and NADH as cofactors, but NADPH, which gave 4-fold lower K(m) values, was preferred. We detected the expression of 20alpha-HSD mRNA in liver, prostate, testis, adrenal, brain, uterus and mammary-gland tissues and in human keratinocyte (HaCaT) cells. The present study clearly indicates that the genuine human 20alpha-HSD belongs to the aldoketo reductase family, like the 20alpha-HSDs from other species. << Less
J. Mol. Endocrinol. 25:221-228(2000) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Further studies on 20-alpha-hydroxysteroid dehydrogenase of rat testes.
Shikita M., Inano H., Tamaoki B.
Biochemistry 6:1760-1764(1967) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.