Diversity in enoyl-acyl carrier protein reductases

被引:157
作者
Massengo-Tiasse, R. P. [1 ]
Cronan, J. E. [1 ,2 ]
机构
[1] Univ Illinois, Dept Microbiol, Chem & Life Sci Lab, Urbana, IL 61801 USA
[2] Univ Illinois, Dept Biochem, Urbana, IL 61801 USA
关键词
Enoyl-acyl carrier protein reductase; fatty acid biosynthesis; Fatty acid synthesis II; triclosan; short-chain dehydrogenase reductase; medium-chain dehydrogenase reductase; FATTY-ACID SYNTHASE; SHORT-CHAIN DEHYDROGENASES/REDUCTASES; 2-ENOYL THIOESTER REDUCTASE; ESCHERICHIA-COLI; ACP REDUCTASE; MYCOBACTERIUM-TUBERCULOSIS; STREPTOCOCCUS-PNEUMONIAE; LIPOIC ACID; CRYSTAL-STRUCTURE; PHENYLIMIDAZOLE DERIVATIVES;
D O I
10.1007/s00018-009-8704-7
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 enoyl-acyl carrier protein reductase (ENR) is the last enzyme in the fatty acid elongation cycle. Unlike most enzymes in this essential pathway, ENR displays an unusual diversity among organisms. The growing interest in ENRs is mainly due to the fact that a variety of both synthetic and natural antibacterial compounds are shown to specifically target their activity. The primary anti-tuberculosis drug, isoniazid, and the broadly used antibacterial compound, triclosan, both target this enzyme. In this review, we discuss the diversity of ENRs, and their inhibitors in the light of current research progress.
引用
收藏
页码:1507 / 1517
页数:11
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