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.
glucoamylase is an exoglycosidase responsible for hydrolyzing the terminal alpha-1,4 glucosidic bonds of dextrins and related oligo- and polysaccharides, the reaction involves a proton transfer by acid catalysis, followed by formation of a transition state analogous to an oxocarbonium ion, and finally, a base-catalyzed nucleophilic attack of water, glutamic acid present in different regions of the enzyme-active site acts as the acid and base catalysts required for the reaction
glucoamylase is an exoglycosidase responsible for hydrolyzing the terminal alpha-1,4 glucosidic bonds of dextrins and related oligo- and polysaccharides, the reaction involves a proton transfer by acid catalysis, followed by formation of a transition state analogous to an oxocarbonium ion, and finally, a base-catalyzed nucleophilic attack of water, glutamic acid present in different regions of the enzyme-active site acts as the acid and base catalysts required for the reaction
the replacement of native beta-glucosidase Bgl1 signal peptide by that of Sta1, SPS-Bgl1, increases the production of the enzyme by about threefold without affecting the ratio between the values of activity associated to cells and free in the medium
glucoamylase is a two-domain protein composed by a N-terminal serinethreonine-rich domain and a C-terminal domain with the typical structure of the catalytic domain of fungal glucoamylases
construction of a series of hybrid enzymes by interchanging domains of glucoamylase Sta1 from Saccharomyces cerevisiae and beta-glucosidase Bgl1 from Saccharomycopsis fibuligera strain ATCC 9947 based on the homology-based structural models of the two proteins. The replacement of native Bgl1 signal peptide by that of Sta1, SPS-Bgl1, increases the production of the enzyme by about threefold without affecting the ratio between the values of activity associated to cells and free in the medium
glucoamylases have been used with alpha-amylases for the industrial conversion of starch into glucose, intact cells of thermotolerant yeasts can be used as colloidal biocatalysts in starch degradation processes
Marin-Navarro, J.; Gurgu, L.; Alamar, S.; Polaina, J.
Structural and functional analysis of hybrid enzymes generated by domain shuffling between Saccharomyces cerevisiae (var. diastaticus) Sta1 glucoamylase and Saccharomycopsis fibuligera Bgl1 beta-glucosidase