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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

A specific, highly active malate dehydrogenase by redesign of a lactate dehydrogenase framework.

Three variations to the structure of the nicotinamide adenine dinucleotide (NAD)-dependent L-lactate dehydrogenase from Bacillus stearothermophilus were made to try to change the substrate specificity from lactate to malate: Asp197----Asn, Thr246----Gly, and Gln102----Arg). Each modification shifts the specificity from lactate to malate, although only the last (Gln102----Arg) provides an effective and highly specific catalyst for the new substrate. This synthetic enzyme has a ratio of catalytic rate (kcat) to Michaelis constant (Km) for oxaloacetate of 4.2 x 10(6)M-1 s-1, equal to that of native lactate dehydrogenase for its natural substrate, pyruvate, and a maximum velocity (250 s-1), which is double that reported for a natural malate dehydrogenase from B. stearothermophilus.[1]

References

  1. A specific, highly active malate dehydrogenase by redesign of a lactate dehydrogenase framework. Wilks, H.M., Hart, K.W., Feeney, R., Dunn, C.R., Muirhead, H., Chia, W.N., Barstow, D.A., Atkinson, T., Clarke, A.R., Holbrook, J.J. Science (1988) [Pubmed]
 
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