Post-translational modification of polyketide and nonribosomal peptide synthases

被引：208

作者：

Walsh, CT ^{[1
]}

Gehring, AM ^{[1
]}

Weinreb, PH ^{[1
]}

Quadri, LEN ^{[1
]}

Flugel, RS ^{[1
]}

机构：

[1] Harvard Univ, Sch Med, Dept Biol Chem & Mol Pharmacol, Boston, MA 02115 USA

来源：

CURRENT OPINION IN CHEMICAL BIOLOGY | 1997年 / 1卷 / 03期

关键词：

D O I：

10.1016/S1367-5931(97)80067-1

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：

The past year has witnessed a major advance in the study of polyketide and nonribosomal peptide biosynthesis with the identification of the phosphopantetheinyl transferase enzyme family, enzymes required to produce active, post-translationally modified polyketide and peptide synthases. Phosphopantetheinyl transferases required for fatty acid, peptide and siderophore biosynthesis have been characterized and a consensus sequence noted in order to facilitate future identification of additional proteins catalyzing phosphopantetheinyl transfer.

引用

页码：309 / 315

页数：7

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