BMB Reports
- Volume 32 Issue 1
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- Pages.39-44
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- 1999
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- 1976-670X(eISSN)
Effect of Mutagenesis of V111 and L112 on the Substrate Specificity of Zymomonas mobilis Pyruvate Decarboxylase
- Huang, Chang-Yi (Centre for Protein Structure, Function and Engineering, Department of Biochemistry, University of Queensland) ;
- Nixon, Peter F. (Centre for Protein Structure, Function and Engineering, Department of Biochemistry, University of Queensland) ;
- Duggleby, Ronald G. (Centre for Protein Structure, Function and Engineering, Department of Biochemistry, University of Queensland)
- Published : 1999.01.31
Abstract
Pyruvate decarboxylase (PDC) catalyzes the conversion of pyruvate to acetaldehyde as the penultimate step in alcohol fermentation. The enzyme requires two cofactors, thiamin diphosphate (ThDP) and
Keywords
- Pyruvate decarboxylase;
- Site-directed mutagenesis;
- Substrate specificity;
- Thiamin diphosphate;
- Zymomonas mobilis