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(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
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(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
mode of action
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(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
active site structure, catalytic residue is Tyr464, catalytic domain and raw starch binding site
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
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(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
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(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
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(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
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(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
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(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
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(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
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(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
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(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
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(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
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(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
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(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
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(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
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(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
Mucor rouxians
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(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
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(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
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(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
reaction mechanism depends on the substrate, i.e. hydrolysis or transglycosylation, overview
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
residue Trp622 is important in substrate binding rather than in determination of pH optimum, and probably does not interact with the catalytic base
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(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
structure-function relationship, ligand binding
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(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
the enzyme catalyses the cleavage of alpha-1,4- and alpha-1,6-glycosidic bonds. Glucoamylases use a classical acid/base Koshland-type inverting mechanism, releasing alpha-glucose from the nonreducing end of an alpha-glucan chain
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
the enzyme catalyses the cleavage of alpha-1,4- and alpha-1,6-glycosidic bonds. Glucoamylases use a classical acid/base Koshland-type inverting mechanism, releasing alpha-glucose from the nonreducing end of an alpha-glucan chain
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
the enzyme catalyses the cleavage of alpha-1,4- and alpha-1,6-glycosidic bonds. Glucoamylases use a classical acid/base Koshland-type inverting mechanism, releasing alpha-glucose from the nonreducing end of an alpha-glucan chain
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
the enzyme from Aspergillus tritici strain WZ99 degrades alpha-1,4 glucoside linkages faster than alpha-1,6 glucoside linkages
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
the enzyme catalyses the cleavage of alpha-1,4- and alpha-1,6-glycosidic bonds. Glucoamylases use a classical acid/base Koshland-type inverting mechanism, releasing alpha-glucose from the nonreducing end of an alpha-glucan chain
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(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
the enzyme catalyses the cleavage of alpha-1,4- and alpha-1,6-glycosidic bonds. Glucoamylases use a classical acid/base Koshland-type inverting mechanism, releasing alpha-glucose from the nonreducing end of an alpha-glucan chain
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(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
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(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
the enzyme from Aspergillus tritici strain WZ99 degrades alpha-1,4 glucoside linkages faster than alpha-1,6 glucoside linkages
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(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
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(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
active site structure, catalytic residue is Tyr464, catalytic domain and raw starch binding site
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(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
mode of action
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(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
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(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
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(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
residue Trp622 is important in substrate binding rather than in determination of pH optimum, and probably does not interact with the catalytic base
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(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
the enzyme from Aspergillus tritici strain WZ99 degrades alpha-1,4 glucoside linkages faster than alpha-1,6 glucoside linkages
-
-
(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
active site structure, catalytic residue is Tyr464, catalytic domain and raw starch binding site
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(alpha-D-glucopyranosyl-(1-4))n-alpha-D-glucopyranose + H2O = (alpha-D-glucopyranosyl-(1-4))n-1-alpha-D-glucopyranose + beta-D-glucopyranose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
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