期刊论文详细信息
FEBS Letters
Escherichia coli inorganic pyrophosphatase : site‐directed mutagenesis of the metal binding sites
Rodina, Elena2  Harutyunyan, Emil1  Oganessyan, Vaheh1  Nazarova, Tatjana2  Kurilova, Svetlana2  Avaeva, Svetlana2  Vorobyeva, Natalja3  Ignatov, Pavel3 
[1] Institute of Crystallography, Russian Academy of Science, Moscow, Russian Federation;A.N Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119899, Russian Federation;Department of Chemistry, Moscow State University, Moscow, Russian Federation
关键词: Inorganic pyrophosphatase;    Aspartic acid;    Site-directed mutagenesis;    Kinetics;    Differential spectrophotometry;   
DOI  :  10.1016/S0014-5793(96)01296-3
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
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【 摘 要 】

Aspartic acids 65, 67, 70, 97 and 102 in the inorganic pyrophosphatase of Escherichia coli, identified as evolutionarily conserved residues of the active site, have been replaced by asparagine. Each mutation was found to decrease the κ app value by approx. 2–3 orders of magnitude. At the same time, the K m values changed only slightly. Only minor changes take place in the pK values of the residues essential for both substrate binding and catalysis. All mutant variants have practically the same affinity to Mg2+ as the wild-type pyrophosphatase.

【 授权许可】

Unknown   

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