EC number:1.2.1.88
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.2 Acting on the aldehyde or oxo group of donors |
| 1.2.1 With NAD+ or NADP+ as acceptor |
| ID: | 1.2.1.88 | ||
|---|---|---|---|
| Description: | L-glutamate gamma-semialdehyde dehydrogenase. | ||
| Alternative Name: |
Pyrroline-5-carboxylate dehydrogenase. Delta(1)-pyrroline-5-carboxylate dehydrogenase. 1-pyrroline-5-carboxylate dehydrogenase. | ||
| Prosite: | PDOC00068; | ||
| PDB: |
|
||
| 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
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.References
External Links
| UniProtKB Enzyme Link: | UniProtKB 1.2.1.88 |
| BRENDA Enzyme Link: | BRENDA 1.2.1.88 |
| KEGG Enzyme Link: | KEGG1.2.1.88 |
| BioCyc Enzyme Link: | BioCyc 1.2.1.88 |
| ExPASy Enzyme Link: | ExPASy1.2.1.88 |
| EC2PDB Enzyme Link: | EC2PDB 1.2.1.88 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.2.1.88 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.2.1.88 |
| IntEnz Enzyme Link: | IntEnz 1.2.1.88 |
| MEDLINE Enzyme Link: | MEDLINE 1.2.1.88 |
| RHEA:16417 | (S)-1-pyrroline-5-carboxylate + 2 H2O + NAD(+) = H(+) + L-glutamate + NADH |
| RULE(radius=1) | [*:1]-[N;H0;+0:2]=[CH;+0:3]-[*:4].[*:5]-[n+;H0:6]1:[cH;+0:7]:[cH;+0:8]:[cH;+0:9]:[c;H0;+0:10](-[*:11]):[cH;+0:12]:1.[OH2;+0:13].[OH2;+0:14]>>([*:4]-[C;H0;+0:3](=[O;H0;+0:14])-[OH;+0:13].[*:1]-[NH2;+0:2]).[*:5]-[N;H0;+0:6]1-[CH;+0:7]=[CH;+0:8]-[CH2;+0:9]-[C;H0;+0:10](-[*:11])=[CH;+0:12]-1 |
| Reaction |  |
| Core-to-Core |
| RHEA:24882 | (S)-1-pyrroline-5-carboxylate + 2 H2O + NADP(+) = H(+) + L-glutamate + NADPH |
| RULE(radius=1) | [*:1]-[N;H0;+0:2]=[CH;+0:3]-[*:4].[*:5]-[n+;H0:6]1:[cH;+0:7]:[cH;+0:8]:[cH;+0:9]:[c;H0;+0:10](-[*:11]):[cH;+0:12]:1.[OH2;+0:13].[OH2;+0:14]>>([*:4]-[C;H0;+0:3](=[O;H0;+0:14])-[OH;+0:13].[*:1]-[NH2;+0:2]).[*:5]-[N;H0;+0:6]1-[CH;+0:7]=[CH;+0:8]-[CH2;+0:9]-[C;H0;+0:10](-[*:11])=[CH;+0:12]-1 |
| Reaction |  |
| Core-to-Core |
| RHEA:24886 | (R)-1-pyrroline-5-carboxylate + 2 H2O + NAD(+) = D-glutamate + H(+) + NADH |
| RULE(radius=1) | [*:1]-[N;H0;+0:2]=[CH;+0:3]-[*:4].[*:5]-[n+;H0:6]1:[cH;+0:7]:[cH;+0:8]:[cH;+0:9]:[c;H0;+0:10](-[*:11]):[cH;+0:12]:1.[OH2;+0:13].[OH2;+0:14]>>([*:4]-[C;H0;+0:3](=[O;H0;+0:14])-[OH;+0:13].[*:1]-[NH2;+0:2]).[*:5]-[N;H0;+0:6]1-[CH;+0:7]=[CH;+0:8]-[CH2;+0:9]-[C;H0;+0:10](-[*:11])=[CH;+0:12]-1 |
| Reaction |  |
| Core-to-Core |
| RHEA:24890 | 1-pyrroline-3-hydroxy-5-carboxylate + 2 H2O + NAD(+) = 4-hydroxy-L-glutamate + H(+) + NADH |
| RULE(radius=1) | [*:1]-[N;H0;+0:2]=[CH;+0:3]-[*:4].[*:5]-[n+;H0:6]1:[cH;+0:7]:[cH;+0:8]:[cH;+0:9]:[c;H0;+0:10](-[*:11]):[cH;+0:12]:1.[OH2;+0:13].[OH2;+0:14]>>([*:4]-[C;H0;+0:3](=[O;H0;+0:14])-[OH;+0:13].[*:1]-[NH2;+0:2]).[*:5]-[N;H0;+0:6]1-[CH;+0:7]=[CH;+0:8]-[CH2;+0:9]-[C;H0;+0:10](-[*:11])=[CH;+0:12]-1 |
| Reaction |  |
| Core-to-Core |
| RHEA:24939 | (R)-1-pyrroline-5-carboxylate + 2 H2O + NADP(+) = D-glutamate + H(+) + NADPH |
| RULE(radius=1) | [*:1]-[N;H0;+0:2]=[CH;+0:3]-[*:4].[*:5]-[n+;H0:6]1:[cH;+0:7]:[cH;+0:8]:[cH;+0:9]:[c;H0;+0:10](-[*:11]):[cH;+0:12]:1.[OH2;+0:13].[OH2;+0:14]>>([*:4]-[C;H0;+0:3](=[O;H0;+0:14])-[OH;+0:13].[*:1]-[NH2;+0:2]).[*:5]-[N;H0;+0:6]1-[CH;+0:7]=[CH;+0:8]-[CH2;+0:9]-[C;H0;+0:10](-[*:11])=[CH;+0:12]-1 |
| Reaction |  |
| Core-to-Core |
| RHEA:24943 | 1-pyrroline-3-hydroxy-5-carboxylate + 2 H2O + NADP(+) = 4-hydroxy-L-glutamate + H(+) + NADPH |
| RULE(radius=1) | [*:1]-[N;H0;+0:2]=[CH;+0:3]-[*:4].[*:5]-[n+;H0:6]1:[cH;+0:7]:[cH;+0:8]:[cH;+0:9]:[c;H0;+0:10](-[*:11]):[cH;+0:12]:1.[OH2;+0:13].[OH2;+0:14]>>([*:4]-[C;H0;+0:3](=[O;H0;+0:14])-[OH;+0:13].[*:1]-[NH2;+0:2]).[*:5]-[N;H0;+0:6]1-[CH;+0:7]=[CH;+0:8]-[CH2;+0:9]-[C;H0;+0:10](-[*:11])=[CH;+0:12]-1 |
| Reaction |  |
| Core-to-Core |
| RHEA:30235 | H2O + L-glutamate 5-semialdehyde + NAD(+) = 2 H(+) + L-glutamate + NADH |
| RULE(radius=1) | [*:1]-[n+;H0:2]1:[cH;+0:3]:[cH;+0:4]:[cH;+0:5]:[c;H0;+0:6](-[*:7]):[cH;+0:8]:1.[*:9]=[CH;+0:10]-[*:11].[OH2;+0:12]>>[*:1]-[N;H0;+0:2]1-[CH;+0:3]=[CH;+0:4]-[CH2;+0:5]-[C;H0;+0:6](-[*:7])=[CH;+0:8]-1.[*:9]=[C;H0;+0:10](-[*:11])-[OH;+0:12] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| New insights into the binding mode of coenzymes: structure of Thermus thermophilus Delta1-pyrroline-5-carboxylate dehydrogenase complexed with NADP+. | Inagaki E, Ohshima N, Sakamoto K, Babayeva ND, Kato H, Yokoyama S, Tahirov TH | 2007 Jun 1 | 17554163 |
| Hydroxyproline metabolism. IV. Enzymatic synthesis of gamma-hydroxyglutamate from Delta 1-pyrroline-3-hydroxy-5-carboxylate. | ADAMS E, GOLDSTONE A | 1960 Dec | 13681370 |
| [delta]1-Pyrroline-5-Carboxylate Dehydrogenase from Cultured Cells of Potato (Purification and Properties). | Forlani G, Scainelli D, Nielsen E | 1997 Apr | 12223682 |
| Redesigned purification yields a fully functional PutA protein dimer from Escherichia coli. | Brown ED, Wood JM | 1992 Jun 25 | 1618807 |