Results 211 to 220 of about 511,400 (248)
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Identification of catalytically important amino acid residues of Streptomyces lividans acetylxylan esterase A from carbohydrate esterase family 4

Biochimica Et Biophysica Acta - Proteins and Proteomics, 2006
Multiple sequence alignment of Streptomyces lividans acetylxylan esterase A and other carbohydrate esterase family 4 enzymes revealed the following conserved amino acid residues: Asp-12, Asp-13, His-62, His-66, Asp-130, and His-155. These amino acids were mutated in order to investigate a functional role of these residues in catalysis.
Vladimír Puchart
exaly   +4 more sources

Monosaccharide inhibitors targeting carbohydrate esterase family 4 de-N-acetylases.

Bioorganic & Medicinal Chemistry, 2018
The Carbohydrate Esterase family 4 contains virulence factors which modify peptidoglycan and biofilm-related exopolysaccharides. Despite the importance of this family of enzymes, a potent mechanism-based inhibition strategy has yet to emerge.
B. Difrancesco   +2 more
semanticscholar   +3 more sources

Identification of a novel carbohydrate esterase fromBjerkandera adusta: Structural and function predictions through bioinformatics analysis and molecular modeling

Proteins: Structure, Function and Bioinformatics, 2015
Gilberto Valdes-Garcia   +2 more
exaly   +2 more sources

Microbial xylanolytic carbohydrate esterases

Essays in Biochemistry, 2023
AbstractThis article reviews microbial esterases participating in the degradation of the major plant hemicellulose, xylan. The main chain of this polysaccharide built of β-1,4-glycosidically linked xylopyranosyl residues is substituted by other sugars and also partially acetylated.
Vladimír Puchart, Peter Biely
openaire   +2 more sources

A thermotolerant and pH stable rhamnogalacturonan acetylesterase (CtPae12B), a family 12 carbohydrate esterase from Clostridium thermocellum with broad substrate specificity.

International Journal of Biological Macromolecules, 2022
The gene encoding rhamnogalacturonan acetylesterase, CtPae12B from Clostridium thermocellum was cloned, expressed, purified and biochemically characterized. Purified CtPae12B was soluble and exhibited homogenous single band.
Jebin Ahmed, Krishan Kumar, A. Goyal
semanticscholar   +1 more source

Computational and SAXS-based structure insights of pectin acetyl esterase (CtPae12B) of family 12 carbohydrate esterase from Clostridium thermocellum ATCC 27405

Journal of Biomolecular Structure and Dynamics, 2021
Pectin is a complex form of polysaccharide and is composed of several structural components that require the concerted action of several pectinases for its complete degradation. In this study, in silico and solution structure of a pectin acetyl esterase (
Jebin Ahmed   +4 more
semanticscholar   +1 more source

Distinct roles of carbohydrate esterase family CE16 acetyl esterases and polymer-acting acetyl xylan esterases in xylan deacetylation.

Journal of Biotechnology, 2013
Mass spectrometric analysis was used to compare the roles of two acetyl esterases (AE, carbohydrate esterase family CE16) and three acetyl xylan esterases (AXE, families CE1 and CE5) in deacetylation of natural substrates, neutral (linear) and 4-O-methyl glucuronic acid (MeGlcA) substituted xylooligosaccharides (XOS).
S. Koutaniemi   +6 more
semanticscholar   +3 more sources

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