首页> 外文会议>12th Symposium on Bioluminescence and Chemiluminescence, Apr 5-9, 2002, Robinson College, University of Cambridge, UK >CATALYTIC PROPERTIES AND BIOLUMINESCENCE SPECTRA OF RECOMBINANT FIREFLY LUCIFERASE LUCIOLA MINGRELICA WITH POINT MUTATIONS OUT OF THE ENZYME ACTIVE SITE
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CATALYTIC PROPERTIES AND BIOLUMINESCENCE SPECTRA OF RECOMBINANT FIREFLY LUCIFERASE LUCIOLA MINGRELICA WITH POINT MUTATIONS OUT OF THE ENZYME ACTIVE SITE

机译:酶活性部位外点突变的重组萤光酶LUCIOLA MINGRELICA的催化性能和生物发光光谱

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摘要

The His433Tyr mutation in Luciola cruciata and Hotaria parvula firefly luciferases resulted in bioluminescence color changes from 570 to 610 nm. It means that the highly conservative His433 residue located out of the luciferase active site plays a very important role in enzyme function. The goal of this work was to construct mutants His433Asn and His433Ser for Luciola mingrelica firefly luciferase, which has high homology with luciferases indicated above. We studied catalytic properties of the enzyme mutant forms and their bioluminescence spectra. Analysis of the data obtained permitted us to elucidate the mechanism of the influence of the His433 residue on the luciferase active site.
机译:Luciola cruciata和Hotaria parvula萤火虫荧光素酶中的His433Tyr突变导致生物发光颜色从570 nm变为610 nm。这意味着位于荧光素酶活性位点之外的高度保守的His433残基在酶功能中起着非常重要的作用。这项工作的目的是构建与上述萤光素酶具有高度同源性的Luciola mingrelica萤火虫萤光素酶的突变体His433Asn和His433Ser。我们研究了酶突变体形式的催化特性及其生物发光光谱。对获得的数据的分析使我们能够阐明His433残基对荧光素酶活性位点的影响机理。

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