Carboxylic ester hydrolases from hyperthermophiles. [PDF]
Extremophiles, 2009 Carboxylic ester hydrolyzing enzymes constitute a large group of enzymes that are able to catalyze the hydrolysis, synthesis or transesterification of an ester bond. They can be found in all three domains of life, including the group of hyperthermophilic
Levisson M, van der Oost J, Kengen SW.
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Organic-Solvent-Tolerant Carboxylic Ester Hydrolases for Organic Synthesis. [PDF]
Appl Environ Microbiol, 2020 Major challenges hampering biotechnological applications of esterases include the requirement to accept nonnatural and chemically demanding substrates and the tolerance of the enzymes toward organic solvents which are often required to solubilize such substrates.
Bollinger A +6 more
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Carboxylic ester hydrolases of rat pancreatic juice
Journal of Lipid Research, 1966 An attempt was made to establish the number and characteristics of the enzymes in pancreatic juice that hydrolyze nitrogen- and phosphorus-free esters of fatty acids.
F.H. Mattson, R.A. Volpenhein
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Carboxylic ester hydrolases: Classification and database derived from their primary, secondary, and tertiary structures. [PDF]
Protein Sci, 2016 AbstractWe classified the carboxylic ester hydrolases (CEHs) into families and clans by use of multiple sequence alignments, secondary structure analysis, and tertiary structure superpositions. Our work for the first time has fully established their systematic structural classification.
Chen Y, Black DS, Reilly PJ.
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Carboxylic Ester Hydrolases in Bacteria: Active Site, Structure, Function and Application [PDF]
Crystals, 2019 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.
Changsuk Oh +2 more
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Structure–function relationships in the carboxylic‐ester‐hydrolase superfamily [PDF]
European Journal of Biochemistry, 2000 CNBr fragments from porcine intestinal glycerol‐ester hydrolase were separated by SDS/PAGE under reducing and nonreducing conditions, and their amino‐acid sequences were analysed. Two intra‐chain disulfide bridges were identified, namely Cys70–Cys99 (loop A) and Cys256–Cys267 (loop B).
Sylvie Smialowski‐Fléter +3 more
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Identification and expression of MarCE, a marine carboxylesterase with synthetic ester‐degrading activity [PDF]
Microbial BiotechnologyCarboxylic ester hydrolases with the capacity to degrade polyesters are currently highly sought after for their potential use in the biological degradation of PET and other chemically synthesized polymers.
Clodagh M. Carr +8 more
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A study of carboxylic ester hydrolases: structural classification, properties, and database
, 2015 The carboxylic ester hydrolases (CEHs) are enzymes that hydrolyze an ester bond to form a carboxylic acid and an alcohol. They are one of the enzyme groups that are most explored industrially for their applications in the food, flavor, pharmaceutical, organic synthesis, and detergent industries.
Yingfei Chen
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Microbial carboxylic ester hydrolases (EC 3.1.1) in food biotechnology [PDF]
Letters in Applied Microbiology, 1993 Ester linkages between carboxylic acid groups and hydroxyl groups are basic to the structure of carboxyesters and lipids, and occur commonly as modifications of polysaccharide molecules. Microorganisms produce enzymes which hydrolyse the carboxylic ester linkages in substrates which are being utilized for growth.
A.M. McKay
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Carboxylic ester hydrolase in acute pancreatitis : a clinical and experimental study
, 1994 Diagnosis of acute pancreatitis (AP) is erroneous in up to one third of patients when based on clinical criteria and elevated serum amylase values. Furthermore, according to autopsy reports fatal pancreatitis remains clinically undiagnosed in 22 to 86 % of hospitalised patients.
P. Jonas Blind
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