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β-Glucosidases
by
Esen, Asim
, Ketudat Cairns, James R.
in
active sites
/ amino acid sequences
/ Amino acids
/ Animal metabolism
/ Animals
/ Aromatic compounds
/ beta-glucans
/ beta-glucosidase
/ Biochemistry
/ biomass
/ Biomedical and Life Sciences
/ Biomedicine
/ Carbohydrates
/ Catalytic Domain
/ Cell Biology
/ Cell walls
/ Cellular biology
/ Cellulases
/ Cellulases - chemistry
/ Cellulases - metabolism
/ chemistry
/ Enzymes
/ Glucan
/ Glycosidases
/ Glycoside hydrolase
/ Glycosides
/ Humans
/ Industrial applications
/ Life Sciences
/ lignification
/ metabolism
/ Microorganisms
/ Molecular biology
/ plant hormones
/ Proteins
/ Review
/ Saccharides
/ Substrate Specificity
2010
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β-Glucosidases
by
Esen, Asim
, Ketudat Cairns, James R.
in
active sites
/ amino acid sequences
/ Amino acids
/ Animal metabolism
/ Animals
/ Aromatic compounds
/ beta-glucans
/ beta-glucosidase
/ Biochemistry
/ biomass
/ Biomedical and Life Sciences
/ Biomedicine
/ Carbohydrates
/ Catalytic Domain
/ Cell Biology
/ Cell walls
/ Cellular biology
/ Cellulases
/ Cellulases - chemistry
/ Cellulases - metabolism
/ chemistry
/ Enzymes
/ Glucan
/ Glycosidases
/ Glycoside hydrolase
/ Glycosides
/ Humans
/ Industrial applications
/ Life Sciences
/ lignification
/ metabolism
/ Microorganisms
/ Molecular biology
/ plant hormones
/ Proteins
/ Review
/ Saccharides
/ Substrate Specificity
2010
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Do you wish to request the book?
β-Glucosidases
by
Esen, Asim
, Ketudat Cairns, James R.
in
active sites
/ amino acid sequences
/ Amino acids
/ Animal metabolism
/ Animals
/ Aromatic compounds
/ beta-glucans
/ beta-glucosidase
/ Biochemistry
/ biomass
/ Biomedical and Life Sciences
/ Biomedicine
/ Carbohydrates
/ Catalytic Domain
/ Cell Biology
/ Cell walls
/ Cellular biology
/ Cellulases
/ Cellulases - chemistry
/ Cellulases - metabolism
/ chemistry
/ Enzymes
/ Glucan
/ Glycosidases
/ Glycoside hydrolase
/ Glycosides
/ Humans
/ Industrial applications
/ Life Sciences
/ lignification
/ metabolism
/ Microorganisms
/ Molecular biology
/ plant hormones
/ Proteins
/ Review
/ Saccharides
/ Substrate Specificity
2010
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Journal Article
β-Glucosidases
2010
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Overview
β-Glucosidases (3.2.1.21) are found in all domains of living organisms, where they play essential roles in the removal of nonreducing terminal glucosyl residues from saccharides and glycosides. β-Glucosidases function in glycolipid and exogenous glycoside metabolism in animals, defense, cell wall lignification, cell wall β-glucan turnover, phytohormone activation, and release of aromatic compounds in plants, and biomass conversion in microorganisms. These functions lead to many agricultural and industrial applications. β-Glucosidases have been classified into glycoside hydrolase (GH) families GH1, GH3, GH5, GH9, and GH30, based on their amino acid sequences, while other β-glucosidases remain to be classified. The GH1, GH5, and GH30 β-glucosidases fall in GH Clan A, which consists of proteins with (β/α)
8
-barrel structures. In contrast, the active site of GH3 enzymes comprises two domains, while GH9 enzymes have (α/α)
6
barrel structures. The mechanism by which GH1 enzymes recognize and hydrolyze substrates with different specificities remains an area of intense study.
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