Article
Catalytic-rate improvement of a thermostable malate dehydrogenase by a subtle alteration in cofactor binding.
The Biochemical journal - 15 Jan 1995
Alldread R M, Halsall D M, Clarke A R, Sundaram T K, Atkinson T, Scawen M D, Nicholls D J
Abstract excerpt
The nucleotide-binding fold of many NAD(+)-dependent dehydrogenases contains a conserved acidic amino acid residue which hydrogen-bonds with the 2'- and 3'-hydroxy groups of the adenine-ribose of the cofactor. This residue is highly conserved as aspartate in malate dehydrogenases, except in the thermophilic enzyme from Thermus aquaticus B (TaqMDH), which has glutamic acid-41 in the equivalent position. The...
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