The phosphopantetheinyl transferases: catalysis of a post-translational modification crucial for life

被引:255
作者
Beld, Joris [1 ]
Sonnenschein, Eva C. [1 ]
Vickery, Christopher R. [1 ,2 ]
Noel, Joseph P. [2 ]
Burkart, Michael D. [1 ]
机构
[1] Univ Calif San Diego, Dept Chem & Biochem, La Jolla, CA 92093 USA
[2] Jack H Skirball Ctr Chem Biol & Prote, Salk Inst Biol Studies, Howard Hughes Med Inst, La Jolla, CA 92037 USA
基金
美国国家科学基金会;
关键词
ACYL-CARRIER-PROTEIN; NONRIBOSOMAL PEPTIDE SYNTHETASE; BIOSYNTHETIC GENE-CLUSTER; FATTY-ACID SYNTHASE; ALPHA-AMINOADIPATE REDUCTASE; PUTATIVE 4'-PHOSPHOPANTETHEINYL TRANSFERASE; PRODRUG ACTIVATION MECHANISM; DIRECTED MUTATIONAL ANALYSIS; COMPLETE GENOME SEQUENCE; ESCHERICHIA-COLI K-12;
D O I
10.1039/c3np70054b
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
Although holo-acyl carrier protein synthase, AcpS, a phosphopantetheinyl transferase (PPTase), was characterized in the 1960s, it was not until the publication of the landmark paper by Lambalot et at. in 1996 that PPTases garnered wide-spread attention being classified as a distinct enzyme superfamily. In the past two decades an increasing number of papers have been published on PPTases ranging from identification, characterization, structure determination, mutagenesis, inhibition, and engineering in synthetic biology. In this review, we comprehensively discuss all current knowledge on this class of enzymes that post-translationally install a 4'-phosphopantetheine arm on various carrier proteins.
引用
收藏
页码:61 / 108
页数:48
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