| Literature DB >> 8405446 |
Abstract
The role of Tyr-139, which is thought to be located at the active site of Thermus thermophilus HB8 3-isopropylmalate dehydrogenase, has been investigated by site-specific replacement with phenylalanine. The replacement scarcely affected the Michaelis constant (Km) for 3-isopropylmalate, but caused a 13-fold decrease of that for NAD. The catalytic constant (kcat) showed a 14-fold decrease. Accordingly, the catalytic efficiency (kcat/Km) decreased for 3-isopropylmalate but not for NAD. The results suggest that Tyr-139 is involved in the catalytic function through interaction with 3-isopropylmalate.Entities:
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Year: 1993 PMID: 8405446 DOI: 10.1016/0014-5793(93)80478-d
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124