EC number:1.4.1.18
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.4 Acting on the CH-NH2 group of donors |
| 1.4.1 With NAD+ or NADP+ as acceptor |
| ID: | 1.4.1.18 | ||
|---|---|---|---|
| Description: | Lysine 6-dehydrogenase. | ||
| Alternative Name: |
LysDH. L-lysine epsilon-dehydrogenase. L-lysine 6-dehydrogenase. | ||
| Prosite: | PDOC00068; | ||
| PDB: |
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3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.4.1.18 |
| BRENDA Enzyme Link: | BRENDA 1.4.1.18 |
| KEGG Enzyme Link: | KEGG1.4.1.18 |
| BioCyc Enzyme Link: | BioCyc 1.4.1.18 |
| ExPASy Enzyme Link: | ExPASy1.4.1.18 |
| EC2PDB Enzyme Link: | EC2PDB 1.4.1.18 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.4.1.18 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.4.1.18 |
| IntEnz Enzyme Link: | IntEnz 1.4.1.18 |
| MEDLINE Enzyme Link: | MEDLINE 1.4.1.18 |
| RHEA:12408 | L-lysine + NAD(+) = 2 H(+) + L-1-piperideine-6-carboxylate + NADH + NH4(+) |
| RULE(radius=1) | ([*:1]-[CH2;+0:2]-[NH2;+0:3].[*:4]-[NH2;+0:5]).[*:6]-[n+;H0:7]1:[cH;+0:8]:[cH;+0:9]:[cH;+0:10]:[c;H0;+0:11](-[*:12]):[cH;+0:13]:1>>[*:6]-[N;H0;+0:7]1-[CH;+0:8]=[CH;+0:9]-[CH2;+0:10]-[C;H0;+0:11](-[*:12])=[CH;+0:13]-1.[*:4]-[N;H0;+0:5]=[CH;+0:2]-[*:1].[NH3;+0:3] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Occurrence of L-lysine epsilon-dehydrogenase in Agrobacterium tumefaciens. | Misono H, Nagasaki S | 1982 Apr | 6801024 |
| Properties of L-lysine epsilon-dehydrogenase from Agrobacterium tumefaciens. | Misono H, Hashimoto H, Uehigashi H, Nagata S, Nagasaki S | 1989 Jun | 2768207 |
| First crystal structure of L-lysine 6-dehydrogenase as an NAD-dependent amine dehydrogenase. | Yoneda K, Fukuda J, Sakuraba H, Ohshima T | 2010 Mar 12 | 20056607 |
| Highly stable L-lysine 6-dehydrogenase from the thermophile Geobacillus stearothermophilus isolated from a Japanese hot spring: characterization, gene cloning and sequencing, and expression. | Heydari M, Ohshima T, Nunoura-Kominato N, Sakuraba H | 2004 Feb | 14766574 |