Abstract
In order to elucidate the enzyme-substrate-cofactor interaction in 3-isopropylmalate dehydrogenase, the coenzyme activity of NAD analogs which have a 3-substituted pyridine ring was examined. Analogs 3-5 showed diminished kcat values compared with those of NAD+, whereas thiocarboxamide 2 was almost as equally active as NAD+. This suggests that the NH2 functionality of NAD+ is more important for the catalysis of IPMDH than a carbonyl group. © 1999, Taylor & Francis Group, LLC. All rights reserved.
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Chiba, A., Eguchi, T., Oshima, T., & Kakinuma, K. (1999). Coenzyme activity of NAD analogs for 3-isopropylmalate dehydrogenase from thermus thermophilus HB8. Bioscience, Biotechnology and Biochemistry, 63(9), 1647–1649. https://doi.org/10.1271/bbb.63.1647
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