Abstract
In the oxidation of methylglyoxal by 2-oxoaldehyde dehydrogenase, the apparent Km value for NADP+ was about 2.5 times lower than the corresponding Km for NAD+; the apparent Km values for methylglyoxal and for the amine activator L-2-aminopropan-1-ol, with NADP+ as cofactor, were also different from those obtained with NAD+. In the presence of NADP+, the enzyme was not activated by P1, in contrast with the activation of the enzyme when NAD+ was used. The significance of the results is discussed.
Full text
PDF
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Dunkerton J., James S. P. Purification of 2-oxoaldehyde dehydrogenase and its dependence on unusual amines. Biochem J. 1975 Sep;149(3):609–617. doi: 10.1042/bj1490609. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Monder C. Alpha-keto aldehyde dehydrogenase, an enzyme that catalyzes the enzymic oxidation of methylglyoxal to pyruvate. J Biol Chem. 1967 Oct 25;242(20):4603–4609. [PubMed] [Google Scholar]
- Vince R., Daluge S. Glyoxalase inhibitors. A possible approach to anticancer agents. J Med Chem. 1971 Jan;14(1):35–37. doi: 10.1021/jm00283a009. [DOI] [PubMed] [Google Scholar]
- Vince R., Daluge S., Wadd W. B. Studies on the inhibition of glyoxalase I by S-substituted glutathiones. J Med Chem. 1971 May;14(5):402–404. doi: 10.1021/jm00287a006. [DOI] [PubMed] [Google Scholar]