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CATH domain | Related DB codes (homologues) |
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3.40.50.720 : Rossmann fold | S00543,S00551,S00552,S00553,S00602,S00604,S00605,S00608,S00610,S00625,S00319,S00328,S00329,S00330,S00331,S00332,D00456,D00457,D00458,S00324,S00320,S00326,S00327,D00459,S00335,S00336,S00334,T00219,S00339,D00513,D00001,D00002,D00003,D00005,D00007,D00008,D00010,D00012,D00017,D00018,D00023,D00027,D00028,D00031,D00032,D00033,D00034,D00035,D00037,D00048,D00071,D00476,D00481,D00482,D00490,D00492,D00494,D00545,D00601,D00603,D00604,D00605,D00615,D00845,D00857,D00858,M00161,M00171,M00210,T00002,T00010,T00011,T00015,T00227,T00247,T00408,T00414,D00827,D00262,D00274,D00275,M00035,T00109 |
Enzyme Name | UniProtKB | KEGG |
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| P80702 |
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Protein name | 3-alpha-hydroxysteroid dehydrogenase | 3alpha-hydroxysteroid dehydrogenase (B-specific) (EC 1.1.1.50)hydroxyprostaglandin dehydrogenase (EC 1.1.1.50)3alpha-hydroxysteroid oxidoreductase (EC 1.1.1.50)sterognost 3alpha (EC 1.1.1.50)carbonyl reductase (NADPH) (EC 1.1.1.184)aldehyde reductase 1 (EC 1.1.1.184)prostaglandin 9-ketoreductase (EC 1.1.1.184)xenobiotic ketone reductase (EC 1.1.1.184)NADPH-dependent carbonyl reductase (EC 1.1.1.184)ALR3 (EC 1.1.1.184)carbonyl reductase (EC 1.1.1.184)nonspecific NADPH-dependent carbonyl reductase (EC 1.1.1.184)aldehyde reductase 1 (EC 1.1.1.184)carbonyl reductase (NADPH) (EC 1.1.1.184) |
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Synonyms | 3-alpha-HSDEC 1.1.1.50Hydroxyprostaglandin dehydrogenaseHSD28 |
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UniProtKB:Accession Number | P80702 |
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Entry name | DIDH_COMTE |
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Activity | Androsterone + NAD(P)(+) = 5-alpha-androstane-3,17-dione + NAD(P)H. |
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Subunit | Homodimer. |
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Subcellular location | Cytoplasm. |
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Cofactor |
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Compound table: links to PDB-related databases & PoSSuM |
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| Substrates | Products |
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KEGG-id | C00523 | C00003 | C01612 | C00674 | C01450 | C00004 | C00080 |
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E.C. | 1.1.1.50 | 1.1.1.50,1.1.1.184 | 1.1.1.184 | 1.1.1.50 | 1.1.1.184 | 1.1.1.50,1.1.1.184 | 1.1.1.50,1.1.1.184 |
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Compound | Androsterone | NAD+ | R-CHOH-R' | 5alpha-Androstane-3,17-dione | R-CO-R' | NADH | H+ |
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Type | carbohydrate,steroid | amide group,amine group,nucleotide | carbohydrate | carbohydrate,steroid | carbohydrate | amide group,amine group,nucleotide | others |
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ChEBI | 16032
| 15846
|
| 15994
|
| 16908
| 15378
|
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PubChem | 5879
| 5893
|
| 439289 222865
|
| 439153
| 1038
|
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| | | | | | | | | | | | | | |
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1fjhA |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
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1fjhB |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
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1fk8A |  |  |  |  |  |  |  | Unbound | Bound:NAD | Bound:NAD | Unbound | Unbound | Unbound | |
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1fk8B |  |  |  |  |  |  |  | Unbound | Bound:NAD | Bound:NAD | Unbound | Unbound | Unbound | |
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References for Catalytic Mechanism | References | Sections | No. of steps in catalysis |
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[3] | p.41336-41337 |
| [4] | p.714-715 |
| [6] | Fig.5A |
|
references | [1] |
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PubMed ID | 9812981 |
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Journal | J Biol Chem |
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Year | 1998 |
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Volume | 273 |
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Pages | 30888-96 |
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Authors | Mobus E, Maser E |
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Title | Molecular cloning, overexpression, and characterization of steroid-inducible 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni. A novel member of the short-chain dehydrogenase/reductase superfamily. |
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[2] |
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PubMed ID | 10833462 |
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Journal | Biochem Biophys Res Commun |
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Year | 2000 |
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Volume | 272 |
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Pages | 622-8 |
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Authors | Maser E, Mobus E, Xiong G |
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Title | Functional expression, purification, and characterization of 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni. |
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[3] |
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Comments | X-ray crystallography |
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PubMed ID | 11007791 |
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Journal | J Biol Chem |
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Year | 2000 |
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Volume | 275 |
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Pages | 41333-9 |
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Authors | Grimm C, Maser E, Mobus E, Klebe G, Reuter K, Ficner R |
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Title | The crystal structure of 3alpha -hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni shows a novel oligomerization pattern within the short chain dehydrogenase/reductase family. |
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Related PDB | 1fjh,1fk8 |
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[4] |
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PubMed ID | 11306088 |
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Journal | Chem Biol Interact |
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Year | 2001 |
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Volume | 130-132 |
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Pages | 707-22 |
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Authors | Maser E, Xiong G, Grimm C, Ficner R, Reuter K |
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Title | 3alpha-Hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni: biological significance, three-dimensional structure and gene regulation. |
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[5] |
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PubMed ID | 11306089 |
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Journal | Chem Biol Interact |
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Year | 2001 |
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Volume | 130-132 |
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Pages | 723-36 |
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Authors | Xiong G, Martin H, Blum A, Schafers C, Maser E |
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Title | A model on the regulation of 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase expression in Comamonas testosteroni. |
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[6] |
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PubMed ID | 15572373 |
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Journal | J Biol Chem |
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Year | 2004 |
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Volume | 280 |
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Pages | 3522-8 |
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Authors | Hwang CC, Chang YH, Hsu CN, Hsu HH, Li CW, Pon HI |
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Title | Mechanistic roles of Ser114, Tyr155 and Lys159 in 3alpha -hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni. |
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comments | According to the Swiss-prot data (Q9ZFY9), "Acyl-[acyl-carrier protein]" and "trans-2,3-dehydroacyl-[acyl-carrier protein]" are substrate and product, respectively, suggesting that its E.C. number should be 1.3.1.9, instead of 1.1.1.50. However, according to the literature [4] & [6], this enzyme catalyzes dehydrogenation of 3alpha-OH of androsterone. This enzyme belongs to the short-chain dehydrogenase/reductase (SDR) superfamily, along with Drosophia alcohol dehydrogenase (S00319 in EzCatDB). This enzyme has got a catalytic triad composed of conserved residues, Ser, Tyr, and Lys. The conformation of these residues, compared to that of the NAD molecule, seems to be similar to that of the homologous enzymes. Thus, its catalytic mechanism must be similar to those of the homologous enzymes.
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created | updated |
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2004-05-13 | 2012-06-26 |
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