A single mutation in the NAD-specific formate dehydrogenase from Candida methylica allows the enzyme to use NADP

Nevin Gul-Karaguler, Richard B. Sessions*, Anthony R. Clarke, J. John Holbrook

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

50 Citations (Scopus)

Abstract

An homology model of Candida methylica formate dehydrogenase (cmFDH) was constructed based on the Pseudomonas sp. 101 formate dehydrogenase (psFDH) structure. An aspartic acid residue in the model was predicted to interact with the adenine ribose of the NAD cofactor, in common with many NAD-dependent ox-oreductases. Replacement of this aspartic acid residue by serine in cmFDH removed the absolute requirement for NAD over NADP shown by the wild type enzyme. Taken with similar results shown by D- and L-lactate dehydrogenases, this suggests that an aspartic acid in this position is a major determinant of coenzyme specificity in NAD/NADP-dependent dehydrogenases.

Original languageEnglish
Pages (from-to)283-287
Number of pages5
JournalBiotechnology Letters
Volume23
Issue number4
DOIs
Publication statusPublished - 2001

Keywords

  • Coenzyme specificity
  • Dehydrogenase
  • Formate
  • Kinetics
  • Modelling

Fingerprint

Dive into the research topics of 'A single mutation in the NAD-specific formate dehydrogenase from Candida methylica allows the enzyme to use NADP'. Together they form a unique fingerprint.

Cite this