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


Gul-Karaguler N. , SESSIONS R., CLARKE A., HOLBROOK J.

BIOTECHNOLOGY LETTERS, vol.23, no.4, pp.283-287, 2001 (Journal Indexed in SCI) identifier identifier

  • Publication Type: Article / Article
  • Volume: 23 Issue: 4
  • Publication Date: 2001
  • Doi Number: 10.1023/a:1005610414179
  • Title of Journal : BIOTECHNOLOGY LETTERS
  • Page Numbers: pp.283-287

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 oxoreductases. 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.