Structure, function, and regulation of thioesterases

被引:21
|
作者
Swarbrick, Crystall M. D. [1 ]
Nanson, Jeffrey D. [2 ]
Patterson, Edward I. [3 ]
Forwood, Jade K. [4 ]
机构
[1] Griffith Univ, Inst Glyc, Southport, Qld 4222, Australia
[2] Univ Queensland, Australian Infect Dis Res Ctr, Inst Mol Biosci, Sch Chem & Mol Biosci, Brisbane, Qld 4072, Australia
[3] Univ Liverpool Liverpool Sch Trop Med, Dept Vector Biol & Trop Dis Biol, Ctr Neglected Trop Dis, Pembroke Pl, Liverpool L3 5QA, Merseyside, England
[4] Charles Sturt Univ, Sch Biomed Sci, Boorooma St, Wagga Wagga, NSW, Australia
关键词
Thioesterase; Hydrolase; Coenzyme A; Fatty acyl-CoA; Hotdog domain; Regulation; ACYL-COA THIOESTERASE; FATTY-ACID SYNTHASE; S-FORMYLGLUTATHIONE HYDROLASE; HOTDOG-FOLD THIOESTERASE; ENCODING PROTEASE-I; CRYSTAL-STRUCTURE; ESCHERICHIA-COLI; SUBSTRATE-SPECIFICITY; POLYKETIDE SYNTHASE; MOLECULAR-CLONING;
D O I
10.1016/j.plipres.2020.101036
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
Thioesterases are present in all living cells and perform a wide range of important biological functions by catalysing the cleavage of thioester bonds present in a diverse array of cellular substrates. Thioesterases are organised into 25 families based on their sequence conservation, tertiary and quaternary structure, active site configuration, and substrate specificity. Recent structural and functional characterisation of thioesterases has led to significant changes in our understanding of the regulatory mechanisms that govern enzyme activity and their respective cellular roles. The resulting dogma changes in thioesterase regulation include mechanistic insights into ATP and GDP-mediated regulation by oligomerisation, the role of new key regulatory regions, and new insights into a conserved quaternary structure within TE4 family members. Here we provide a current and comparative snapshot of our understanding of thioesterase structure, function, and regulation across the different thioesterase families.
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页数:31
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