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Article

A single amino acid mutation enhances the thermal stability of Escherichia coli malate dehydrogenase.

European journal of biochemistry - 15 Aug 1994

Goward C R, Miller J, Nicholls D J, Irons L I, Scawen M D, O'Brien R, Chowdhry B Z

Abstract excerpt

The stability of wild-type Escherichia coli malate dehydrogenase was compared with a mutant form of the enzyme with the amino acid residue at position 102 changed from arginine to glutamine. The mutation occurs on the underside of a mobile loop which closes over the active-site cleft on formation of the enzyme/cofactor/substrate ternary complex. The mutant enzyme is kinetically compromised while the wild-type...

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Identifiers

PMID: 8076646
DOI: 10.1111/j.1432-1033.1994.tb20018.x

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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