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Dual Role of the Active Site Residues of Thermus thermophilus 3-Isopropylmalate Dehydrogenase: Chemical Catalysis and Domain Closure.

Biochemistry - 26 Jan 2016

Gráczer Éva, Szimler Tamás, Garamszegi Anita, Konarev Petr V, Lábas Anikó, Oláh Julianna, Palló Anna, Svergun Dmitri I, Merli Angelo, Závodszky Péter, Weiss Manfred S, Vas Mária

Abstract excerpt

The key active site residues K185, Y139, D217, D241, D245, and N102 of Thermus thermophilus 3-isopropylmalate dehydrogenase (Tt-IPMDH) have been replaced, one by one, with Ala. A drastic decrease in the kcat value (0.06% compared to that of the wild-type enzyme) has been observed for the K185A and D241A mutants. Similarly, the catalytic interactions (Km values) of these two mutants with the substrate IPM are...

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PMID: 26731489
DOI: 10.1021/acs.biochem.5b00839

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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