Results 201 to 210 of about 11,083 (244)
Beyond defense: microbial modifications of plant specialized metabolites alter and expand their ecological functions. [PDF]
New PhytolUnger K, Agler MT.
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Substrate Specificity of GH29 α-L-Glucosidases from Cecembia lonarensis. [PDF]
J Appl Glycosci (1999)Kang HJ, Tagami T, Okuyama M.
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Bio-inspired designer cellulosomes show strongest synergy on industrial substrates under natural-like conditions. [PDF]
J Ind Microbiol BiotechnolLamote B +5 more
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Cellular and Molecular Life Sciences, 2010
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
James R, Ketudat Cairns, Asim, Esen
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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
James R, Ketudat Cairns, Asim, Esen
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1994
Abstract Initial studies on partially purified a-glucosidase I from rat liver1·2 and oviduct microsomes3 .4 demonstrated that this enzyme removes a single glucose residue from Glc3Man9GlcNAc2. a-Glucosidase I was subsequently purified from calf5 and porcine6 liver, lactating bovine mammary tissue7, mung bean seedlings8, and 5 ...
R Trimble, K Moremcn,, A Herscovics
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Abstract Initial studies on partially purified a-glucosidase I from rat liver1·2 and oviduct microsomes3 .4 demonstrated that this enzyme removes a single glucose residue from Glc3Man9GlcNAc2. a-Glucosidase I was subsequently purified from calf5 and porcine6 liver, lactating bovine mammary tissue7, mung bean seedlings8, and 5 ...
R Trimble, K Moremcn,, A Herscovics
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Endocrinology and Metabolism Clinics of North America, 1997
Alpha-glucosidase inhibitors are antihyperglycemic agents that lower blood glucose by delaying the digestion and absorption of complex carbohydrates. They are competitive inhibitors of the enzymes in the brush border of enterocytes that cleave eligosaccharides to monosaccharides.
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Alpha-glucosidase inhibitors are antihyperglycemic agents that lower blood glucose by delaying the digestion and absorption of complex carbohydrates. They are competitive inhibitors of the enzymes in the brush border of enterocytes that cleave eligosaccharides to monosaccharides.
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Glucosidases and exo-glucanases
Canadian Journal of Biochemistry, 1968A comparison was made of exo-α-glucanases with α-glucosidases, and of exo-β1 → 3-glucanases with β-glucosidases to establish criteria for their characterization. Dimers, trimers, and tetramers of glucose are substrates for both exo-glucanases and glucosidases. Exo-glucanases act more rapidly on the longer oligomers, glucosidases on the shorter.
E T, Reese, A H, Maguire, F W, Parrish
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Immobilization of ?-D-Glucosidase and ?-D-Glucosidase-polyphenolic complexes
Biotechnology Letters, 1983β-D-Glucosidase, alone and after copolymerizing with a resorcinol polymer, was immobilized on a PM 10 ultrafiltration membrane, κ-carrageenan and DEAE (DE52) cellulose. The best support for both enzyme preparations, in terms of high Vmax values, was the ultrafiltration membrane.
Sarkar, J M, Burns, Richard G
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Biochemistry. Biokhimiia, 2001
This review highlights the main properties of mammalian, plant, and microbial alpha-glucosidases. Special attention is given to the classification of these enzymes, possible catalytic mechanisms, their tertiary structure, and the structure of major inhibitors.
V V, Krasikov, D V, Karelov, L M, Firsov
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This review highlights the main properties of mammalian, plant, and microbial alpha-glucosidases. Special attention is given to the classification of these enzymes, possible catalytic mechanisms, their tertiary structure, and the structure of major inhibitors.
V V, Krasikov, D V, Karelov, L M, Firsov
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