Serine substitution for cysteine residues in levansucrase selectively abolishes levan forming activity

被引:0
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作者
Velusamy Senthilkumar
Stephen J.W. Busby
Paramasamy Gunasekaran
机构
[1] Madurai Kamaraj University,Department of Microbial Technology, Centre for Excellence in Genomic Sciences, School of Biological Sciences
[2] The University of Birmingham,School of Biosciences
来源
Biotechnology Letters | 2003年 / 25卷
关键词
levansucrase; protein conformation; site directed mutagenesis;
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摘要
Levansucrase is responsible for levan formation during sucrose fermentation of Zymomonas mobilis, and this decreases the efficiency of ethanol production. As thiol modifying agents decrease levan formation, a role for cysteine residues in levansucrase activity has been examined using derivatives of Z. mobilis levansucrase that carry serine substitutions of cysteine at positions 121, 151 or 244. These substitutions abolished the levan forming activity of levansucrase whilst only halving its activity in sucrose hydrolysis. Thus, polymerase and hydrolase activities of Z. mobilis levansucrase are separate and have different requirements for the enzyme's cysteine residues.
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页码:1653 / 1656
页数:3
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