EC number:1.21.4.1
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.21 Catalysing the reaction X-H + Y-H = X-Y |
| 1.21.4 With a disulfide as acceptor |
| ID: | 1.21.4.1 |
|---|---|
| Description: | D-proline reductase. |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.21.4.1 |
| BRENDA Enzyme Link: | BRENDA 1.21.4.1 |
| KEGG Enzyme Link: | KEGG1.21.4.1 |
| BioCyc Enzyme Link: | BioCyc 1.21.4.1 |
| ExPASy Enzyme Link: | ExPASy1.21.4.1 |
| EC2PDB Enzyme Link: | EC2PDB 1.21.4.1 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.21.4.1 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.21.4.1 |
| IntEnz Enzyme Link: | IntEnz 1.21.4.1 |
| MEDLINE Enzyme Link: | MEDLINE 1.21.4.1 |
| RHEA:12737 | (R)-lipoate + 5-aminopentanoate = (R)-dihydrolipoate + D-proline |
| RULE(radius=1) | ([*:1]-[CH2;+0:2]-[*:3].[*:4]-[NH2;+0:5]).[*:6]-[S;H0;+0:7]-[S;H0;+0:8]-[*:9]>>[*:1]-[CH;+0:2](-[*:3])-[NH;+0:5]-[*:4].([*:6]-[SH;+0:7].[*:9]-[SH;+0:8]) |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Studies of the mechanism of action of D-proline reductase: the presence on covalently bound pyruvate and its role in the catalytic process. | Hodgins DS, Abeles RH | 1969 Mar | 5778643 |
| Identification of D-proline reductase from Clostridium sticklandii as a selenoenzyme and indications for a catalytically active pyruvoyl group derived from a cysteine residue by cleavage of a proprotein. | Kabisch UC, Gräntzdörffer A, Schierhorn A, Rücknagel KP, Andreesen JR, Pich A | 1999 Mar 26 | 10085076 |
| Clostridium sticklandii, a specialist in amino acid degradation:revisiting its metabolism through its genome sequence. | Fonknechten N, Chaussonnerie S, Tricot S, Lajus A, Andreesen JR, Perchat N, Pelletier E, Gouyvenoux M, Barbe V, Salanoubat M, Le Paslier D, Weissenbach J, Cohen GN, Kreimeyer A | 2010 Oct 11 | 20937090 |
| Studies on the enzymic reduction of amino acids. II. Purification and properties of D-proline reductase and a proline racemase from Clostridium sticklandii. | STADTMAN TC, ELLIOTT P | 1957 Oct | 13475375 |
| In vitro processing of the proproteins GrdE of protein B of glycine reductase and PrdA of D-proline reductase from Clostridium sticklandii: formation of a pyruvoyl group from a cysteine residue. | Bednarski B, Andreesen JR, Pich A | 2001 Jun | 11422384 |