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2
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Tyr-139 in Thermus thermophilus 3-isopropylmalate dehydrogenase is involved in catalytic function.嗜热栖热菌3-异丙基苹果酸脱氢酶中的酪氨酸-139参与催化功能。
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Kinetic analysis on the substrate specificity of 3-isopropylmalate dehydrogenase.3-异丙基苹果酸脱氢酶底物特异性的动力学分析
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Structure of isocitrate dehydrogenase with isocitrate, nicotinamide adenine dinucleotide phosphate, and calcium at 2.5-A resolution: a pseudo-Michaelis ternary complex.异柠檬酸脱氢酶与异柠檬酸、烟酰胺腺嘌呤二核苷酸磷酸及钙的2.5埃分辨率结构：一种拟米氏三元复合物
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Crystallographic investigations of nicotinamide adenine dinucleotide binding to horse liver alcohol dehydrogenase.烟酰胺腺嘌呤二核苷酸与马肝醇脱氢酶结合的晶体学研究。
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A general method applicable to the search for similarities in the amino acid sequence of two proteins.一种适用于寻找两种蛋白质氨基酸序列相似性的通用方法。
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Use of intermediate partitioning to calculate intrinsic isotope effects for the reaction catalyzed by malic enzyme.使用中间分配法计算苹果酸酶催化反应的本征同位素效应。
Biochemistry. 1985 Feb 12;24(4):944-8. doi: 10.1021/bi00325a020.
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Automated docking of substrates to proteins by simulated annealing.通过模拟退火实现底物与蛋白质的自动对接。
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Electrostatic and steric contributions to regulation at the active site of isocitrate dehydrogenase.静电和空间因素对异柠檬酸脱氢酶活性位点调控的贡献。
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Catalytic mechanism of NADP(+)-dependent isocitrate dehydrogenase: implications from the structures of magnesium-isocitrate and NADP+ complexes.NADP(+)-依赖型异柠檬酸脱氢酶的催化机制：来自镁-异柠檬酸和NADP+复合物结构的启示
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嗜热栖热菌异丙基苹果酸脱氢酶中底物结合的建模

Modeling substrate binding in Thermus thermophilus isopropylmalate dehydrogenase.

作者信息

Zhang T, Koshland D E

机构信息

Department of Molecular and Cell Biology, University of California, Berkeley 94720, USA.

出版信息

Protein Sci. 1995 Jan;4(1):84-92. doi: 10.1002/pro.5560040111.

DOI:10.1002/pro.5560040111
PMID:7773180
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2142962/
Abstract

The Thermus thermophilus 3-isopropylmalate dehydrogenase (IPMDH) and Escherichia coli isocitrate dehydrogenase (ICDH) are two functionally and evolutionarily related enzymes with distinct substrate specificities. To understand the determinants of substrate specificities of the two proteins, the substrate and coenzyme in IPMDH were docked into their respective binding sites based on the published structure for apo IPMDH and its sequence and structural homology to ICDH. This modeling study suggests that (1) the substrate and coenzyme (NAD) binding modes of IPMDH are significantly different from those of ICDH, (2) the interactions between the substrates and coenzymes help explain the differences in substrate specificities of IPMDH and ICDH, and (3) binding of the substrate and coenzyme should induce a conformational change in the structure of IPMDH.

摘要

嗜热栖热菌3-异丙基苹果酸脱氢酶（IPMDH）和大肠杆菌异柠檬酸脱氢酶（ICDH）是两种在功能和进化上相关但具有不同底物特异性的酶。为了理解这两种蛋白质底物特异性的决定因素，基于已发表的脱辅基IPMDH结构及其与ICDH的序列和结构同源性，将IPMDH中的底物和辅酶对接至它们各自的结合位点。该建模研究表明：（1）IPMDH的底物和辅酶（NAD）结合模式与ICDH的显著不同；（2）底物与辅酶之间的相互作用有助于解释IPMDH和ICDH底物特异性的差异；（3）底物和辅酶的结合应诱导IPMDH结构发生构象变化。