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Carboxylic Ester Hydrolases in Bacteria: Active Site, Structure, Function and Applicationopen access

Authors
Oh, ChangsukKim, T. DoohunKim, Kyeong Kyu
Issue Date
Nov-2019
Publisher
MDPI
Keywords
carboxylic ester hydrolase (CEH); carboxylic ester; Protein Data Bank (PDB); crystal structure; active site
Citation
CRYSTALS, v.9, no.11
Journal Title
CRYSTALS
Volume
9
Number
11
URI
https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/2754
DOI
10.3390/cryst9110597
ISSN
2073-4352
Abstract
Carboxylic ester hydrolases (CEHs), which catalyze the hydrolysis of carboxylic esters to produce alcohol and acid, are identified in three domains of life. In the Protein Data Bank (PDB), 136 crystal structures of bacterial CEHs (424 PDB codes) from 52 genera and metagenome have been reported. In this review, we categorize these structures based on catalytic machinery, structure and substrate specificity to provide a comprehensive understanding of the bacterial CEHs. CEHs use Ser, Asp or water as a nucleophile to drive diverse catalytic machinery. The alpha/beta/alpha sandwich architecture is most frequently found in CEHs, but 3-solenoid, beta-barrel, up-down bundle, alpha/beta/beta/alpha 4-layer sandwich, 6 or 7 propeller and alpha/beta barrel architectures are also found in these CEHs. Most are substrate-specific to various esters with types of head group and lengths of the acyl chain, but some CEHs exhibit peptidase or lactamase activities. CEHs are widely used in industrial applications, and are the objects of research in structure- or mutation-based protein engineering. Structural studies of CEHs are still necessary for understanding their biological roles, identifying their structure-based functions and structure-based engineering and their potential industrial applications.
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