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

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-dependen...

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Bibliographic Details
Published in:Biotechnology letters 2001-02, Vol.23 (4), p.283-287
Main Authors: GUL-KARAGULER, Nevin, SESSIONS, Richard B, CLARKE, Anthony R, HOLBROOK, J. John
Format: Article
Language:English
Subjects:
Biological and medical sciences
Biotechnology
Candida methylica
cmFDH gene
Dehydrogenase
Enzymes
Fundamental and applied biological sciences. Psychology
Methods. Procedures. Technologies
Mutation
Protein engineering
Pseudomonas
psFDH gene
Yeast
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Summary: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.[PUBLICATION ABSTRACT]
ISSN:0141-5492
1573-6776
DOI:10.1023/A:1005610414179