Protein biotinylation in higher plants: Characterization of biotin holocarboxylase synthetase activity from pea (Pisum sativum) leaves

被引：23

作者：

Tissot, G ^{[1
]}

Job, D ^{[1
]}

Douce, R ^{[1
]}

Alban, C ^{[1
]}

机构：

[1] RHONE POULENC AGROCHIM,CNRS,UMR 41,F-69263 LYON 9,FRANCE

来源：

BIOCHEMICAL JOURNAL | 1996年 / 314卷

关键词：

D O I：

10.1042/bj3140391

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 holocarboxylase synthetase was partially purified from pea leaves by a sequence of ammonium sulphate fractionation and DEAE 52-cellulose chromatography. Enzyme activity was assayed using apo-(biotin carboxyl carrier protein) from an Escherichia coli bir A mutant affected in biotin holocarboxylase synthetase activity. Conditions for optimal catalytic activity and biochemical parameters of the plant enzyme were determined. This is the first direct evidence of the existence of biotin holocarboxylase synthetase activity in plants.

引用

页码：391 / 395

页数：5

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