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大肠杆菌异柠檬酸裂解酶与蓖麻异柠檬酸裂解酶之间的高度序列保守性。

High sequence conservation between isocitrate lyase from Escherichia coli and Ricinus communis.

作者信息

Beeching J R

机构信息

School of Biological Sciences, University of Bath, UK.

出版信息

Protein Seq Data Anal. 1989 Dec;2(6):463-6.

PMID:2696959
Abstract

The deduced amino acid sequences of isocitrate lyase (EC 4.1.3.1) from Escherichia coli and Ricinus communis (castor bean) were compared and regions of high homology between the two enzymes were identified. The castor-bean enzyme had a 14 amino acid amino-terminal, and a 25 amino acid carboxy-terminal extension and a 102 amino acid central insertion compared to the E. coli enzyme. Enzymatic data were used to attempt to identify specific amino acids in the active site. Comparisons with putative peroxisomal/gloxysomal targeting sequences were made and a region including part of the central insertion of the castor bean enzyme was tentatively identified.

摘要

对来自大肠杆菌和蓖麻(蓖麻子)的异柠檬酸裂解酶(EC 4.1.3.1)推导的氨基酸序列进行了比较,并确定了两种酶之间的高度同源区域。与大肠杆菌的酶相比,蓖麻酶有一个14个氨基酸的氨基末端、一个25个氨基酸的羧基末端延伸以及一个102个氨基酸的中央插入序列。利用酶学数据试图确定活性位点中的特定氨基酸。与假定的过氧化物酶体/乙醛酸循环体靶向序列进行了比较,并初步确定了蓖麻酶中央插入序列一部分的区域。

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