Journal Article

Substrate Recognition of Isocitrate Dehydrogenase and 3-Isopropylmalate Dehydrogenase from <i>Thermus thermophilus</i> HB8

Takuro Yaoi, Kentaro Miyazaki and Tairo Oshima

in The Journal of Biochemistry

Published on behalf of The Japanese Biochemical Society

Volume 121, issue 1, pages 77-81
Published in print January 1997 | ISSN: 0021-924X
Published online January 1997 | e-ISSN: 1756-2651 | DOI: http://dx.doi.org/10.1093/oxfordjournals.jbchem.a021573
Substrate Recognition of Isocitrate Dehydrogenase and 3-Isopropylmalate Dehydrogenase from Thermus thermophilus HB8

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The substrate-binding sites of NADP-dependent isocitrate dehydrogenase and NAD-dependent 3-isopropylmalate dehydrogenase from Thermus thermophilus were analyzed by site-directed mutagenesis. Ser97 and Asn99 of isocitrate dehydrogenase were identified to be involved in the isocitrate recognition. In 3-isopropylmalate dehydrogenase, the corresponding residues, Leu90 and Leu91, appear to recognize the substrate by forming a hydrophobic pocket. Double mutation of Asp78 and Glu87 revealed that negative charge of these residues plays a crucial role in discriminating isopropylmalate from isocitrate.

Keywords: active site; site-directed mutagenesis; substrate specificity; thermophilic enzymes

Journal Article.  0 words. 

Subjects: Biochemistry

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