Molecular biology of biotin attachment to proteins

被引：95

作者：

Chapman-Smith, A

Cronan, JE

机构：

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

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

来源：

JOURNAL OF NUTRITION | 1999年 / 129卷 / 02期

关键词：

biotin; domain; acceptor; ligase; post-translational;

D O I：

10.1093/jn/129.2.477S

中图分类号：

R15 [营养卫生、食品卫生]; TS201 [基础科学];

学科分类号：

100403 ;

摘要：

Enzymatic attachment of biotin to proteins requires the interaction of a distinct domain of the acceptor protein (the "biotin domain") with the enzyme, biotin protein ligase, that catalyzes this essential and rare post-translational modification. Both biotin domains and biotin protein ligases are very strongly conserved throughout biology. This review concerns the protein structures and mechanisms involved in the covalent attachment of biotin to proteins.

引用

页码：477S / 484S

页数：8

共 58 条

[31]

MCALLISTER HC, 1966, J BIOL CHEM, V241, P2855

[32] Purification, regulation, and molecular and biochemical characterization of pyruvate carboxylase from Methanobacterium thermoautotrophicum strain ΔH [J].