| EC |
1.2.1.20 |
| Accepted name: |
glutarate-semialdehyde dehydrogenase |
| Reaction: |
5-oxopentanoate + NADP+ + H2O = glutarate + NADPH + H+ |
| Glossary: |
5-oxopentanoate = glutarate semialdehyde |
| Other name(s): |
glutarate semialdehyde dehydrogenase; davD (gene name) |
| Systematic name: |
glutarate-semialdehyde:NADP+ oxidoreductase |
| Comments: |
The enzyme, characterized from multiple Pseudomonas strains, participates in L-lysine degradation. Unlike earlier claims, it prefers NADP+ to NAD+. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, CAS registry number: 9028-99-3 |
| References: |
| 1. |
Ichihara, A. and Ichihara, E.A. Metabolism of L-lysine by bacterial enzymes. V. Glutaric semialdehyde dehydrogenase. J. Biochem. (Tokyo) 49 (1961) 154–157. [PMID: 13717359] |
| 2. |
Chang, Y. F. and Adams, E. Glutaric semialdehyde dehydrogenase (Pseudomonas putida). Methods Enzymol. 17B (1971) 166–171. [DOI] |
| 3. |
Fothergill, J.C. and Guest, J.R. Catabolism of L-lysine by Pseudomonas aeruginosa. J. Gen. Microbiol. 99 (1977) 139–155. [DOI] [PMID: 405455] |
| 4. |
Chang, Y.F. and Adams, E. Glutarate semialdehyde dehydrogenase of Pseudomonas. Purification, properties, and relation to L-lysine catabolism. J. Biol. Chem. 252 (1977) 7979–7986. [PMID: 914857] |
| 5. |
Yamanishi, Y., Mihara, H., Osaki, M., Muramatsu, H., Esaki, N., Sato, T., Hizukuri, Y., Goto, S. and Kanehisa, M. Prediction of missing enzyme genes in a bacterial metabolic network. Reconstruction of the lysine-degradation pathway of Pseudomonas aeruginosa. FEBS J. 274 (2007) 2262–2273. [DOI] [PMID: 17388807] |
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| [EC 1.2.1.20 created 1965, modified 2021] |
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