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来自天蓝色链霉菌A3(2)的磷酸甘油酸变位酶:酶的纯化与特性鉴定以及基因的克隆与序列分析

Phosphoglycerate mutase from Streptomyces coelicolor A3(2): purification and characterization of the enzyme and cloning and sequence analysis of the gene.

作者信息

White P J, Nairn J, Price N C, Nimmo H G, Coggins J R, Hunter I S

机构信息

Department of Biochemistry, University of Glasgow, United Kingdom.

出版信息

J Bacteriol. 1992 Jan;174(2):434-40. doi: 10.1128/jb.174.2.434-440.1992.

Abstract

The enzyme 3-phosphoglycerate mutase was purified 192-fold from Streptomyces coelicolor, and its N-terminal sequence was determined. The enzyme is tetrameric with a subunit Mr of 29,000. It is 2,3-bisphosphoglycerate dependent and inhibited by vanadate. The gene encoding the enzyme was cloned by using a synthetic oligonucleotide probe designed from the N-terminal peptide sequence, and the complete coding sequence was determined. The deduced amino acid sequence is 64% identical to that of the phosphoglycerate mutase of Saccharomyces cerevisiae and has substantial identity to those of other phosphoglycerate mutases.

摘要

从天蓝色链霉菌中纯化出3-磷酸甘油酸变位酶,纯化倍数为192倍,并测定了其N端序列。该酶为四聚体,亚基分子量为29,000。它依赖2,3-二磷酸甘油酸,并受钒酸盐抑制。利用根据N端肽序列设计的合成寡核苷酸探针克隆了编码该酶的基因,并测定了完整的编码序列。推导的氨基酸序列与酿酒酵母的磷酸甘油酸变位酶的氨基酸序列有64%的同一性,与其他磷酸甘油酸变位酶的氨基酸序列也有显著的同一性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f572/205734/868e06a49227/jbacter00068-0103-a.jpg

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