Identification of the catalytic residue of human short/branched chain acyl-CoA dehydrogenase by in vitro mutagenesis

Barbara Binzak; Jan Willard; Jerry Vockley

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Identification of the catalytic residue of human short/branched chain acyl-CoA dehydrogenase by in vitro mutagenesis

机译：通过体外诱变鉴定人短/支链酰基辅酶A脱氢酶的催化残基

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The acyl-CoA dehydrogenases (ACDs) are a family of related enzymes which catalyze the α,β-dehydrogenation of acyl-CoA esters, transferring electrons to electron transferring flavoprotein. We have recently cloned and characterized the cDNA for human short/branched chain acyl-CoA dehydrogenase (SBCAD). Based on homology with the other ACDs we hypothesized that E381 is the catalytic residue for this enzyme. Alteration of this amino acid to glutamine, glycine or arginine resulted in an inactive enzyme. Substitution of aspartate at this position led to an enzyme with reduced activity compared to the wild type. An E381G/G260E double mutation (which places a glutamate in a position homologous to the catalytic residue identified in other members of this gene family) restored enzyme activity. These data confirm the crucial nature of E381 to the activity of this enzyme and strongly support its role as the α-proton abstracting base.

机译：酰基辅酶A脱氢酶（ACD）是一族相关的酶，它们催化酰基辅酶A酯的α，β脱氢，将电子转移至电子转移黄素蛋白。我们最近克隆并鉴定了人类短/支链酰基辅酶A脱氢酶（SBCAD）的cDNA。基于与其他ACD的同源性，我们假设E381是该酶的催化残基。将该氨基酸改变为谷氨酰胺，甘氨酸或精氨酸会导致酶失活。与野生型相比，在该位置处的天冬氨酸取代导致酶活性降低。 E381G / G260E双重突变（将谷氨酸置于与该基因家族其他成员中鉴定出的催化残基同源的位置）恢复了酶活性。这些数据证实了E381对该酶活性的关键性质，并强烈支持其作为α-质子提取碱基的作用。

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《Biochimica et Biophysica Acta. Protein Structure and Molecular Enzymology》 |1998年第0期|共6页
作者
Barbara Binzak; Jan Willard; Jerry Vockley;
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正文语种 eng
中图分类生物化学;分子生物学;
关键词
acyl-CoA dehydrogenase; active site; catalysis; short/branched chain acyl-CoA dehydrogenase; in vitro mutagenesis;

机译：酰基辅酶A脱氢酶活性位点催化短/支链酰基辅酶A脱氢酶体外诱变;

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1. Identification of the catalytic residue of human short/branched chain acyl-CoA dehydrogenase by in vitro mutagenesis. [J] . Binzak B, Willard J, Vockley J Biochimica et biophysica acta: international journal of biochemistry and biophysics . 1998,第1期

机译：通过体外诱变鉴定人短/支链酰基辅酶A脱氢酶的催化残基。
2. Identification of the Catalytic Residue of Rat Acyl-CoA Dehydrogenase 9 by Site-Directed Mutagenesis [J] . Zeng Jia, Deng Senwen, Wang Yiping Applied biochemistry and biotechnology, Part A. enzyme engineering and biotechnology . 2017,第3期

机译：鉴定大鼠酰基 - 辅助脱氢酶9的催化残基通过定位诱变诱变
3. Role of isovaleryl-CoA dehydrogenase and short branched-chain acyl-CoA dehydrogenase in the metabolism of valproic acid: implications for the branched-chain amino acid oxidation pathway. [J] . Luis PB, Ruiter JP, Ijlst L, Drug Metabolism and Disposition: The Biological Fate of Chemicals . 2011,第7期

机译：异戊酰-CoA脱氢酶和短支链酰基-CoA脱氢酶在丙戊酸代谢中的作用：对支链氨基酸氧化途径的影响。
4. Probing the structure of human tissue factor by site-directed mutagenesis of tryptophan residues and in vim incorporation of tryptophan analogs [C] . C. A. Hasselbacher, Elena Rusinova, Evan Waxman, Fluorescence Science and Technology . 2000

机译：试抗鱼类残留物和vim掺入对色氨酸残基的人体组织因子结构的探讨
5. Thermodynamic investigation of substrate activation and regulation in human short-chain acyl-CoA dehydrogenases. [D] . Saenger, Amy Kay. 2004

机译：人类短链酰基辅酶A脱氢酶中底物激活和调控的热力学研究。
6. Isolated 2-Methylbutyrylglycinuria Caused by Short/Branched-Chain Acyl-CoA Dehydrogenase Deficiency: Identification of a New Enzyme Defect Resolution of Its Molecular Basis and Evidence for Distinct Acyl-CoA Dehydrogenases in Isoleucine And Valine Metabolism [O] . Brage Storstein Andresen, Ernst Christensen, Thomas J. Corydon, 2000

机译：短/支链酰基辅酶A脱氢酶缺乏症引起的孤立的2-甲基丁酰甘氨酸尿症：一种新的酶缺陷的鉴定其分子基础的解析以及异亮氨酸和缬氨酸代谢中不同的酰基辅酶A脱氢酶的证据
7. Isolated 2-Methylbutyrylglycinuria Caused by Short/Branched-Chain Acyl-CoA Dehydrogenase Deficiency: Identification of a New Enzyme Defect, Resolution of Its Molecular Basis, and Evidence for Distinct Acyl-CoA Dehydrogenases in Isoleucine And Valine Metabolism [O] . Andresen, Brage Storstein, Christensen, Ernst, Corydon, Thomas J., 2000

机译：短/支链酰基辅酶A脱氢酶缺乏症引起的孤立的2-甲基丁酰甘氨酸尿症：一种新酶缺陷的鉴定，其分子基础的解析以及异亮氨酸和缬氨酸代谢中不同的酰基辅酶A脱氢酶的证据

Identification of the catalytic residue of human short/branched chain acyl-CoA dehydrogenase by in vitro mutagenesis

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