Carboxylic Ester Hydrolases in Bacteria: Active Site, Structure, Function and Application
1
Department of Molecular Cell Biology, Sungkyunkwan University School of Medicine, Suwon 16419, Korea
2
Department of Chemistry, College of Natural Science, Sookmyung Women’s University, Seoul 04310, Korea
*
Authors to whom correspondence should be addressed.
Crystals 2019, 9(11), 597; https://doi.org/10.3390/cryst9110597
Received: 4 October 2019 / Revised: 30 October 2019 / Accepted: 7 November 2019 / Published: 14 November 2019
(This article belongs to the Special Issue Crystallographic Studies of Enzymes)
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 α/β/α sandwich architecture is most frequently found in CEHs, but 3-solenoid, β-barrel, up-down bundle, α/β/β/α 4-layer sandwich, 6 or 7 propeller and α/β 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.
View Full-Text
Keywords:
carboxylic ester hydrolase (CEH); carboxylic ester; Protein Data Bank (PDB); crystal structure; active site
▼
Show Figures
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited
MDPI and ACS Style
Oh, C.; Kim, T.D.; Kim, K.K. Carboxylic Ester Hydrolases in Bacteria: Active Site, Structure, Function and Application. Crystals 2019, 9, 597. https://doi.org/10.3390/cryst9110597
AMA Style
Oh C, Kim TD, Kim KK. Carboxylic Ester Hydrolases in Bacteria: Active Site, Structure, Function and Application. Crystals. 2019; 9(11):597. https://doi.org/10.3390/cryst9110597
Chicago/Turabian StyleOh, Changsuk; Kim, T. D.; Kim, Kyeong K. 2019. "Carboxylic Ester Hydrolases in Bacteria: Active Site, Structure, Function and Application" Crystals 9, no. 11: 597. https://doi.org/10.3390/cryst9110597
Find Other Styles
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.
Search more from Scilit