EC number:1.8.1.4
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.8 Acting on a sulfur group of donors |
| 1.8.1 With NAD+ or NADP+ as acceptor |
| ID: | 1.8.1.4 | ||
|---|---|---|---|
| Description: | Dihydrolipoyl dehydrogenase. | ||
| Alternative Name: |
Lipoyl dehydrogenase. Lipoic acid dehydrogenase. Lipoate dehydrogenase. Lipoamide reductase (NADH). Lipoamide reductase. Lipoamide oxidoreductase (NADH). Lipoamide dehydrogenase (NADH). LDP-Val. LDP-Glc. L-protein. Glycine-cleavage system L-protein. E3 component of alpha-ketoacid dehydrogenase complexes. Dihydrothioctic dehydrogenase. Dihydrolipoic dehydrogenase. Dihydrolipoamide dehydrogenase. Diaphorase. Dehydrolipoate dehydrogenase. | ||
| Prosite: | PDOC00073; | ||
| PDB: |
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| Cath: | 1.10.10.10; 1.10.287.1150; 1.20.120.530; 3.30.1360.120; 3.30.390.30; 3.30.559.10; 3.30.70.140; 3.30.70.1400; 4.10.320.10; 4.10.820.20; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.8.1.4 |
| BRENDA Enzyme Link: | BRENDA 1.8.1.4 |
| KEGG Enzyme Link: | KEGG1.8.1.4 |
| BioCyc Enzyme Link: | BioCyc 1.8.1.4 |
| ExPASy Enzyme Link: | ExPASy1.8.1.4 |
| EC2PDB Enzyme Link: | EC2PDB 1.8.1.4 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.8.1.4 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.8.1.4 |
| IntEnz Enzyme Link: | IntEnz 1.8.1.4 |
| MEDLINE Enzyme Link: | MEDLINE 1.8.1.4 |
| RHEA:33059 | (R)-dihydrolipoamide + NAD(+) = (R)-lipoamide + H(+) + NADH |
| RULE(radius=1) | ([*:1]-[SH;+0:2].[*:3]-[SH;+0:4]).[*:5]-[n+;H0:6]1:[cH;+0:7]:[cH;+0:8]:[cH;+0:9]:[c;H0;+0:10](-[*:11]):[cH;+0:12]:1>>[*:5]-[N;H0;+0:6]1-[CH;+0:7]=[CH;+0:8]-[CH2;+0:9]-[C;H0;+0:10](-[*:11])=[CH;+0:12]-1.[*:1]-[S;H0;+0:2]-[S;H0;+0:4]-[*:3] |
| Reaction |  |
| Core-to-Core |
| RHEA:15045 | (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-lipoyl-L-lysyl-[protein] + H(+) + NADH |
| RULE(radius=1) | ([*:1]-[SH;+0:2].[*:3]-[SH;+0:4]).[*:5]-[n+;H0:6]1:[cH;+0:7]:[cH;+0:8]:[cH;+0:9]:[c;H0;+0:10](-[*:11]):[cH;+0:12]:1>>[*:5]-[N;H0;+0:6]1-[CH;+0:7]=[CH;+0:8]-[CH2;+0:9]-[C;H0;+0:10](-[*:11])=[CH;+0:12]-1.[*:1]-[S;H0;+0:2]-[S;H0;+0:4]-[*:3] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Expression, purification, and physical characterization of Escherichia coli lipoyl(octanoyl)transferase. | Nesbitt NM, Baleanu-Gogonea C, Cicchillo RM, Goodson K, Iwig DF, Broadwater JA, Haas JA, Fox BG, Booker SJ | 2005 Feb | 15642479 |
| Intermediates in the catalytic action of lipoyl dehydrogenase (diaphorase). | MASSEY V, GIBSON QH, VEEGER C | 1960 Nov | 13767908 |
| Preparation and properties of highly purified diaphorase. | SAVAGE N | 1957 Sep | 13471525 |