The Enzyme Database

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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, 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]
[EC 1.2.1.20 created 1965, modified 2021]
 
 


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