The enzymatic biotinylation of proteins: a post-translational modification of exceptional specificity

被引：189

作者：

Chapman-Smith, A ^{[1
]}

Cronan, JE

机构：

[1] Univ Adelaide, Dept Biochem, Adelaide, SA, Australia

[2] Univ Illinois, Dept Microbiol, Urbana, IL 61801 USA

[3] Univ Illinois, Dept Biochem, Urbana, IL 61801 USA

来源：

TRENDS IN BIOCHEMICAL SCIENCES | 1999年 / 24卷 / 09期

关键词：

D O I：

10.1016/S0968-0004(99)01438-3

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Biotin is a coenzyme essential to all life forms. The vitamin has biological activity only when covalently attached to certain key metabolic enzymes. Most organisms have only one enzyme for attachment of biotin to other proteins and the sequences of these proteins and their substrate proteins are strongly conserved throughout nature. Structures of both the biotin ligase and the biotin carrier protein domain from Escherichia coli have been determined. These, together with mutational analyses of biotinylated proteins, are beginning to elucidate the exceptional specificity of this protein modification.

引用

页码：359 / 363

页数：5

共 30 条

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