EC number:1.5.5.2
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.5 Acting on the CH-NH group of donors |
| 1.5.5 With a quinone or similar compound as acceptor |
| ID: | 1.5.5.2 | ||
|---|---|---|---|
| Description: | Proline dehydrogenase. | ||
| Prosite: | PDOC00068; | ||
| PDB: |
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| Cath: | 1.10.1220.10; 1.10.287.2770; 1.20.5.1420; 3.20.20.220; 3.20.20.530; 3.30.60.70; 3.30.70.20; 3.30.70.2010; 3.40.605.10; 2.160.10.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.5.5.2 |
| BRENDA Enzyme Link: | BRENDA 1.5.5.2 |
| KEGG Enzyme Link: | KEGG1.5.5.2 |
| BioCyc Enzyme Link: | BioCyc 1.5.5.2 |
| ExPASy Enzyme Link: | ExPASy1.5.5.2 |
| EC2PDB Enzyme Link: | EC2PDB 1.5.5.2 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.5.5.2 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.5.5.2 |
| IntEnz Enzyme Link: | IntEnz 1.5.5.2 |
| MEDLINE Enzyme Link: | MEDLINE 1.5.5.2 |
| RHEA:42416 | a ubiquinone + L-proline = (S)-1-pyrroline-5-carboxylate + a ubiquinol + H(+) |
| RULE(radius=1) | [*:1]-[C;H0;+0:2]1=[C;H0;+0:3](-[*:4])-[C;H0;+0:5](=[O;H0;+0:6])-[C;H0;+0:7](-[*:8])=[C;H0;+0:9](-[*:10])-[C;H0;+0:11]-1=[O;H0;+0:12].[*:13]-[NH;+0:14]-[CH2;+0:15]-[*:16]>>[*:13]-[N;H0;+0:14]=[CH;+0:15]-[*:16].[*:1]-[c;H0;+0:2]1:[c;H0;+0:3](-[*:4]):[c;H0;+0:5](-[OH;+0:6]):[c;H0;+0:7](-[*:8]):[c;H0;+0:9](-[*:10]):[c;H0;+0:11]:1-[OH;+0:12] |
| Reaction |  |
| Core-to-Core | |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Steady-state kinetic mechanism of the proline:ubiquinone oxidoreductase activity of proline utilization A (PutA) from Escherichia coli. | Moxley MA, Tanner JJ, Becker DF | 2011 Dec 15 | 22040654 |
| RHEA:23784 | a quinone + L-proline = (S)-1-pyrroline-5-carboxylate + a quinol + H(+) |
| RULE(radius=1) | [*:1]-[NH;+0:2]-[CH2;+0:3]-[*:4].[O;H0;+0:5]=[C;H0;+0:6]1-[CH;+0:7]=[CH;+0:8]-[C;H0;+0:9](=[O;H0;+0:10])-[CH;+0:11]=[CH;+0:12]-1>>[*:1]-[N;H0;+0:2]=[CH;+0:3]-[*:4].[OH;+0:5]-[c;H0;+0:6]1:[cH;+0:7]:[cH;+0:8]:[c;H0;+0:9](-[OH;+0:10]):[cH;+0:11]:[cH;+0:12]:1 |
| Reaction |  |
| Core-to-Core | |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Membrane-bound proline dehydrogenase from Escherichia coli. Solubilization, purification, and characterization. | Scarpulla RC, Soffer RL | 1978 Sep 10 | 355248 |
| Steady-state kinetic mechanism of the proline:ubiquinone oxidoreductase activity of proline utilization A (PutA) from Escherichia coli. | Moxley MA, Tanner JJ, Becker DF | 2011 Dec 15 | 22040654 |
| Delta1-pyrroline-5-carboxylic acid formed by proline dehydrogenase from the Bacillus subtilis ssp. natto expressed in Escherichia coli as a precursor for 2-acetyl-1-pyrroline. | Huang TC, Huang YW, Hung HJ, Ho CT, Wu ML | 2007 Jun 27 | 17536821 |
| Redesigned purification yields a fully functional PutA protein dimer from Escherichia coli. | Brown ED, Wood JM | 1992 Jun 25 | 1618807 |
| Functional consequences of PRODH missense mutations. | Bender HU, Almashanu S, Steel G, Hu CA, Lin WW, Willis A, Pulver A, Valle D | 2005 Mar | 15662599 |