Crystal structures of two bacterial 3-hydroxy-3-methylglutaryl-CoA lyases suggest a common catalytic mechanism among a family of TIM barrel metalloenzymes cleaving carbon-carbon bonds.
第一作者:
Farhad,Forouhar
第一单位:
Department of Biological Sciences and Northeast Structural Genomics Consortium, Columbia University, New York, NY 10027, USA.
作者:
主题词
2-异丙基苹果酸合酶(2-Isopropylmalate Synthase);氨基酸序列(Amino Acid Sequence);天冬氨酸(Aspartic Acid);枯草芽孢杆菌(Bacillus subtilis);结合部位(Binding Sites);马尔他布鲁杆菌(Brucella melitensis);碳(Carbon);催化作用(Catalysis);催化域(Catalytic Domain);阳离子(Cations);色谱法, 凝胶(Chromatography, Gel);结晶学, X线(Crystallography, X-Ray);人类(Humans);动力学(Kinetics);光(Light);赖氨酸(Lysine);模型, 化学(Models, Chemical);模型, 分子(Models, Molecular);分子序列数据(Molecular Sequence Data);氧化性应激(Oxidative Stress);氧-酸裂合酶类(Oxo-Acid-Lyases);点突变(Point Mutation);蛋白质结合(Protein Binding);蛋白质构象(Protein Conformation);蛋白质折叠(Protein Folding);蛋白质结构, 二级(Protein Structure, Secondary);蛋白质结构, 三级(Protein Structure, Tertiary);散射, 辐射(Scattering, Radiation);序列同源性, 氨基酸(Sequence Homology, Amino Acid);立体异构现象(Stereoisomerism)
DOI
10.1074/jbc.M507996200
PMID
16330546
发布时间
2021-02-09
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