Catalytic-rate improvement of a thermostable malate dehydrogenase by a subtle alteration in cofactor binding.

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 i...

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Bibliografiske detaljer
Main Authors: Alldread, R M, Halsall, D M, Clarke, A R, Sundaram, T K, Atkinson, T, Scawen, M D, Nicholls, D J
Format: Artigo
Sprog:Inglês
Udgivet: 1995
Fag:
Research Article
Online adgang:https://ncbi.nlm.nih.gov/pmc/articles/PMC1136396/
https://ncbi.nlm.nih.gov/pubmed/7832772
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