Catalytic activity in crystals of mitochondrial aspartate aminotransferase as detected by microspectrophotometry. - Suppr | 超能文献

Catalytic activity in crystals of mitochondrial aspartate aminotransferase as detected by microspectrophotometry.

作者信息

Eichele G, Karabelnik D, Halonbrenner R, Jansonius J N, Christen P

出版信息

J Biol Chem. 1978 Aug 10;253(15):5239-42.

Abstract

摘要

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Catalytic activity in crystals of mitochondrial aspartate aminotransferase as detected by microspectrophotometry.

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Chemical modification of a functional arginyl residue (Arg 292) of mitochondrial aspartate aminotransferase. Identification as the binding site for the distal carboxylate group of the substrate.

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[Catalytic properties of aspartate aminotransferase].[天冬氨酸氨基转移酶的催化特性]

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From protein structure to function via single crystal optical spectroscopy.从蛋白质结构到功能的单晶体光学光谱学研究。

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Three-dimensional structure of a pyridoxal-phosphate-dependent enzyme, mitochondrial aspartate aminotransferase.一种磷酸吡哆醛依赖性酶——线粒体天冬氨酸氨基转移酶的三维结构

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Catalytic activity of non-cross-linked microcrystals of aspartate aminotransferase in poly(ethylene glycol).天冬氨酸转氨酶非交联微晶在聚乙二醇中的催化活性。

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Crystalline aspartate aminotransferase: lattice-induced functional asymmetry of the two subunits.结晶天冬氨酸转氨酶：晶格诱导的两个亚基的功能不对称性。

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