Most forms of the enzyme can rapidly hydrolyse 1,6-alpha-D-glucosidic bonds when the next bond in the sequence is 1,4, and some preparations of this enzyme hydrolyse 1,6- and 1,3-alpha-D-glucosidic bonds in other polysaccharides. This entry covers all such enzymes acting on polysaccharides more rapidly than on oligosaccharides. EC 3.2.1.20 alpha-glucosidase, from mammalian intestine, can catalyse similar reactions.
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SYSTEMATIC NAME
IUBMB Comments
4-alpha-D-glucan glucohydrolase
Most forms of the enzyme can rapidly hydrolyse 1,6-alpha-D-glucosidic bonds when the next bond in the sequence is 1,4, and some preparations of this enzyme hydrolyse 1,6- and 1,3-alpha-D-glucosidic bonds in other polysaccharides. This entry covers all such enzymes acting on polysaccharides more rapidly than on oligosaccharides. EC 3.2.1.20 alpha-glucosidase, from mammalian intestine, can catalyse similar reactions.
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus, the enzyme contains 7 subsites for substrate binding
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus, the enzyme contains 7 subsites for substrate binding
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus, the enzyme contains 7 subsites for substrate binding
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus, the enzyme contains 7 subsites for substrate binding
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus, the enzyme contains 7 subsites for substrate binding
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus, the enzyme contains 7 subsites for substrate binding
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant nonglycosylated enzyme, 10 mg/ml protein in 50 mM acetate, pH 5.4, with 15% PEG 8000, X-ray diffraction structure determination and analysis at 1.1-1.6 A resolution, modelling
purified recombinant nonglycosylated enzyme, 10 mg/ml protein in 50 mM acetate, pH 5.4, with 15% PEG 8000, X-ray diffraction structure determination and analysis at 1.1-1.6 A resolution, modelling
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant enzymes from Saccharomyces cerevisiae strain AH22 medium by gel filtration and ion exchange chromatography to homogeneity
recombinant wild-type and mutant enzymes from Saccharomyces cerevisiae strain AH22 medium by gel filtration and ion exchange chromatography to homogeneity