Structure and mechanism of enzymes involved in biosynthesis and breakdown of the phosphonates fosfomycin, dehydrophos, and phosphinothricin

被引：19

作者：

Nair, Satish K. ^{[1
,3
]}

van der Donk, Wilfred A. ^{[1
,2
,3
,4
]}

机构：

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

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

[3] Univ Illinois, Inst Genom Biol, Urbana, IL 61801 USA

[4] Univ Illinois, Howard Hughes Med Inst, Urbana, IL 61801 USA

来源：

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS | 2011年 / 505卷 / 01期

基金：

美国国家卫生研究院;

关键词：

Antibiotics; Phosphonates; X-ray crystallography; Methyl transferase; Dioxygenase; Epoxidase; Resistance; CARBON-PHOSPHORUS LYASE; (S)-2-HYDROXYPROPYLPHOSPHONIC ACID EPOXIDASE; RESISTANCE PROTEIN FOSA; ESCHERICHIA-COLI; GENE-CLUSTER; STREPTOMYCES-WEDMORENSIS; CRYSTAL-STRUCTURE; NATURAL-PRODUCTS; HETEROLOGOUS EXPRESSION; ANTIBIOTIC FOSFOMYCIN;

D O I：

10.1016/j.abb.2010.09.012

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：

Recent years have seen a rapid increase in the mechanistic and structural information on enzymes that are involved in the biosynthesis and breakdown of naturally occurring phosphonates. This review focuses on these recent developments with an emphasis on those enzymes that have been characterized crystal-lographically in the past five years, including proteins involved in the biosynthesis of phosphinothricin, fosfomycin, and dehydrophos and proteins involved in resistance mechanisms. (C) 2010 Elsevier Inc. All rights reserved.

引用

页码：13 / 21

页数：9

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