EC number:1.5.1.49
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.5 Acting on the CH-NH group of donors |
| 1.5.1 With NAD+ or NADP+ as acceptor |
| ID: | 1.5.1.49 |
|---|---|
| Description: | 1-pyrroline-2-carboxylate reductase (NAD(P)H). |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.5.1.49 |
| BRENDA Enzyme Link: | BRENDA 1.5.1.49 |
| KEGG Enzyme Link: | KEGG1.5.1.49 |
| BioCyc Enzyme Link: | BioCyc 1.5.1.49 |
| ExPASy Enzyme Link: | ExPASy1.5.1.49 |
| EC2PDB Enzyme Link: | EC2PDB 1.5.1.49 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.5.1.49 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.5.1.49 |
| IntEnz Enzyme Link: | IntEnz 1.5.1.49 |
| MEDLINE Enzyme Link: | MEDLINE 1.5.1.49 |
| RHEA:20321 | L-proline + NAD(+) = 1-pyrroline-2-carboxylate + H(+) + NADH |
| RULE(radius=1) | [*:1]-[CH;+0:2](-[*:3])-[NH;+0:4]-[*:5].[*:6]-[n+;H0:7]1:[cH;+0:8]:[cH;+0:9]:[cH;+0:10]:[c;H0;+0:11](-[*:12]):[cH;+0:13]:1>>[*:1]-[C;H0;+0:2](-[*:3])=[N;H0;+0:4]-[*:5].[*:6]-[N;H0;+0:7]1-[CH;+0:8]=[CH;+0:9]-[CH2;+0:10]-[C;H0;+0:11](-[*:12])=[CH;+0:13]-1 |
| Reaction |  |
| Core-to-Core | |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| A unique cis-3-hydroxy-l-proline dehydratase in the enolase superfamily. | Zhang X, Kumar R, Vetting MW, Zhao S, Jacobson MP, Almo SC, Gerlt JA | 2015 Feb 4 | 25608448 |
| Prediction and characterization of enzymatic activities guided by sequence similarity and genome neighborhood networks. | Zhao S, Sakai A, Zhang X, Vetting MW, Kumar R, Hillerich B, San Francisco B, Solbiati J, Steves A, Brown S, Akiva E, Barber A, Seidel RD, Babbitt PC, Almo SC, Gerlt JA, Jacobson MP | 2014 Jun 30 | 24980702 |
| Identification and characterization of trans-3-hydroxy-l-proline dehydratase and Δ(1)-pyrroline-2-carboxylate reductase involved in trans-3-hydroxy-l-proline metabolism of bacteria. | Watanabe S, Tanimoto Y, Yamauchi S, Tozawa Y, Sawayama S, Watanabe Y | 2014 | 24649405 |
| RHEA:20317 | L-proline + NADP(+) = 1-pyrroline-2-carboxylate + H(+) + NADPH |
| RULE(radius=1) | [*:1]-[CH;+0:2](-[*:3])-[NH;+0:4]-[*:5].[*:6]-[n+;H0:7]1:[cH;+0:8]:[cH;+0:9]:[cH;+0:10]:[c;H0;+0:11](-[*:12]):[cH;+0:13]:1>>[*:1]-[C;H0;+0:2](-[*:3])=[N;H0;+0:4]-[*:5].[*:6]-[N;H0;+0:7]1-[CH;+0:8]=[CH;+0:9]-[CH2;+0:10]-[C;H0;+0:11](-[*:12])=[CH;+0:13]-1 |
| Reaction |  |
| Core-to-Core | |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| delta1-piperideine-2-carboxylate reductase of Pseudomonas putida. | Payton CW, Chang YF | 1982 Mar | 6801013 |
| A unique cis-3-hydroxy-l-proline dehydratase in the enolase superfamily. | Zhang X, Kumar R, Vetting MW, Zhao S, Jacobson MP, Almo SC, Gerlt JA | 2015 Feb 4 | 25608448 |
| Prediction and characterization of enzymatic activities guided by sequence similarity and genome neighborhood networks. | Zhao S, Sakai A, Zhang X, Vetting MW, Kumar R, Hillerich B, San Francisco B, Solbiati J, Steves A, Brown S, Akiva E, Barber A, Seidel RD, Babbitt PC, Almo SC, Gerlt JA, Jacobson MP | 2014 Jun 30 | 24980702 |
| Identification and characterization of trans-3-hydroxy-l-proline dehydratase and Δ(1)-pyrroline-2-carboxylate reductase involved in trans-3-hydroxy-l-proline metabolism of bacteria. | Watanabe S, Tanimoto Y, Yamauchi S, Tozawa Y, Sawayama S, Watanabe Y | 2014 | 24649405 |
| Crystal structures of Delta1-piperideine-2-carboxylate/Delta1-pyrroline-2-carboxylate reductase belonging to a new family of NAD(P)H-dependent oxidoreductases: conformational change, substrate recognition, and stereochemistry of the reaction. | Goto M, Muramatsu H, Mihara H, Kurihara T, Esaki N, Omi R, Miyahara I, Hirotsu K | 2005 Dec 9 | 16192274 |
| The putative malate/lactate dehydrogenase from Pseudomonas putida is an NADPH-dependent delta1-piperideine-2-carboxylate/delta1-pyrroline-2-carboxylate reductase involved in the catabolism of D-lysine and D-proline. | Muramatsu H, Mihara H, Kakutani R, Yasuda M, Ueda M, Kurihara T, Esaki N | 2005 Feb 18 | 15561717 |