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人肝脏醛脱氢酶的活性位点。

Active site of human liver aldehyde dehydrogenase.

作者信息

Abriola D P, Fields R, Stein S, MacKerell A D, Pietruszko R

机构信息

Center of Alcohol Studies, Busch Campus, Rutgers University, Piscataway, New Jersey 08854.

出版信息

Biochemistry. 1987 Sep 8;26(18):5679-84. doi: 10.1021/bi00392a015.

Abstract

Bromoacetophenone (2-bromo-1-phenylethanone) functions as an affinity reagent for human aldehyde dehydrogenase (EC 1.2.1.3) and has been found specifically to label a unique tryptic peptide in the enzyme. Amino-terminal sequence analysis of the labeled peptide after purification by two different procedures revealed the following sequence: Val-Thr-Leu-Glu-Leu-Gly-Gly-Lys. Radioactivity was found to be associated with the glutamate residue, which was identified as Glu-268 by reference to the known amino acid sequence. This paper constitutes the first identification of an active site of aldehyde dehydrogenase.

摘要

溴苯乙酮(2-溴-1-苯基乙酮)作为人醛脱氢酶(EC 1.2.1.3)的亲和试剂,已被发现能特异性标记该酶中一个独特的胰蛋白酶肽段。通过两种不同方法纯化后,对标记肽段进行氨基末端序列分析,结果显示以下序列:缬氨酸-苏氨酸-亮氨酸-谷氨酸-亮氨酸-甘氨酸-甘氨酸-赖氨酸。发现放射性与谷氨酸残基相关,通过参考已知氨基酸序列确定其为Glu-268。本文首次鉴定了醛脱氢酶的一个活性位点。

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