| Literature DB >> 12144528 |
Alexander E Serov1, Anna S Popova, Vladimir V Fedorchuk, Vladimir I Tishkov.
Abstract
A eukaryotic formate dehydrogenase (EC 1.2.1.2, FDH) with its substrate specificity changed from NAD(+) to NADP(+) has been constructed by introducing two single-point mutations, Asp(196)-->Ala (D196A) and Tyr(197)-->Arg (Y197R). The mutagenesis was based on the results of homology modelling of a NAD(+)-specific FDH from Saccharomyces cerevisiae (SceFDH) using the Pseudomonas sp.101 FDH (PseFDH) crystal structure as a template. The resulting model structure suggested that Asp(196) and Tyr(197) mediate the absolute coenzyme specificity of SceFDH for NAD(+).Entities:
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Year: 2002 PMID: 12144528 PMCID: PMC1222933 DOI: 10.1042/BJ20020379
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857