Subunit structure, function and organisation of pyruvate decarboxylases from various organisms

被引:49
作者
König, S [1 ]
机构
[1] Univ Halle Wittenberg, Fachbereich Biochem Biotechnol, Inst Biochem, D-06099 Halle, Germany
来源
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 1998年 / 1385卷 / 02期
关键词
crystal structure model; small-angle X-ray scattering; low resolution model; mutant; substrate activation; thiol group;
D O I
10.1016/S0167-4838(98)00074-0
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The nature of the environment of macromolecules influences and determines the state of their overall structure and the extent of binding of specific (cofactors, substrates) or unspecific ligands. How these interactions between enzyme molecules and ligands influence their quaternary structures and, in this way, the realisation of high catalytic activity will be discussed here for the enzyme pyruvate decarboxylase from various organisms: brewer's yeast, brewer's yeast strain, recombinant wild type and site-specific mutants of Saccharomyces cerevisiae, the recombinant wild type of the bacterium Zymomonas mobilis and germinating seeds of the plant Pisum sativum from a structural point of view including both high resolution models from crystal structure analysis and low resolution models from small angle X-ray solution scattering with synchrotron radiation. (C) 1998 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:271 / 286
页数:16
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