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Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
multichain type mechanism
-
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
catalytic mechanism
-
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
catalytic mechanism, reaction mechanism
-
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
mechanism
-
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
acts on starch, glycogen and related polysaccharides and oligosaccharides producing beta-maltose by an inversion, the term beta relates to the initial anomeric configuration of the free sugar group released and not to the configuration of the linkage hydrolysed
-
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
mode of action of the exo-amylase
-
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
mode of action of the exo-amylase
-
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
mode of action of the exo-amylase
-
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
mode of action of the exo-amylase
Debaryomyces sp.
-
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
mode of action of the exo-amylase
-
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
mode of action of the exo-amylase
-
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
mode of action of the exo-amylase
-
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
mode of action of the exo-amylase
-
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
mode of action of the exo-amylase
-
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
mode of action of the exo-amylase
-
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
mode of action of the exo-amylase
-
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
mode of action of the exo-amylase
-
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
mode of action of the exo-amylase
-
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
mode of action of the exo-amylase
-
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
Glu367 is important in catalysis, the plant enzyme shows a reaction mechanism different from the bacterial enzyme, overview
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
active site structure, carbohydrate binding subsites, role of a conformational change of the inner loop in the catalytic mechanism, T342 is involved, overview
-
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
catalytic mechanism
-
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
roles of Glu186 and Glu380 as general acid and general base catalyst in the catalytic reaction, substrate binding and reaction mechanism
-
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
general acid-base catalytic reaction mechanism
-
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
roles of Glu186 and Glu380 as general acid and general base catalyst in the catalytic reaction, reaction mechanism involving residue T342
-
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
mode of action of the exo-amylase
-
-
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
acts on starch, glycogen and related polysaccharides and oligosaccharides producing beta-maltose by an inversion, the term beta relates to the initial anomeric configuration of the free sugar group released and not to the configuration of the linkage hydrolysed
-
-
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
-
-
-
-
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4-nitrophenyl alpha-D-galactoside + H2O
4-nitrophenol + D-galactose
-
-
-
?
4-nitrophenyl alpha-maltopyranoside + H2O
4-nitrophenol + alpha-maltopyranose
-
-
-
?
4-nitrophenyl maltopentaose + H2O
4-nitrophenol + maltopentaose
-
-
-
?
4-nitrophenyl-maltoheptaoside + H2O
?
-
-
-
-
?
4-nitrophenyl-maltopentaoside + H2O
?
-
-
-
-
?
alpha-glucan + H2O
?
-
-
-
?
amylopectin + H2O
beta-maltose + ?
amylopectin + H2O
maltose + ?
amylose + H2O
beta-maltose
amylose + H2O
maltose
Sorghum sp.
-
from starch
-
-
?
amylose + H2O
maltose + ?
catalyzes the release of maltose residues, less good substrate than starch and amylopectin
-
-
?
glycogen + H2O
beta-maltose
glycogen + H2O
maltose + ?
maltal + H2O
2-deoxymaltose
-
-
-
?
maltodextrin + H2O
maltose
-
maltodextrins with chain length from 9 to 198 glucose residues
and very small amounts of glucose and maltotriose
?
maltoheptaose + H2O
maltose
-
the exo-type enzyme can catalyze the successive liberation of beta-maltose from the nonreducing ends of alpha-1,4-linked glucopyranosyl polymers. A phenomenon called multiple or repetitive attack is observed where the enzyme releases several maltose molecules in a single enzyme-substrate complex. The multiple attack action needs the force of enzyme sliding on the substrate. In addition, it is important for the multiple attack that the enzyme and substrate have the characteristics of a stable productive substrate-enzyme complex through a hydrogen bond between the nonreducing end of the substrate and the carboxyl residue of the enzyme
-
-
?
maltooligosaccharide + H2O
?
-
beta-amylase hydrolyzes maltooligosaccharides more readily as their degree of polymerization increases, this being strongest for maltooligosaccharides larger than 13 glucose residues and very weakly for maltotriose, exo-hydrolase that releases beta-maltose from the non-reducing end of alpha-1,4-linked poly- and oligoglucans until the first alpha-1,6-branching point along the substrate molecule is encountered
-
-
?
maltopentaose + H2O
2 maltose + D-glucose
the enzyme displays dual hydrolysis activity toward alpha-1,4- and alpha-1,6-glycosidic linkages, the catalytic efficiency of 6-O-maltosyl-beta-cyclodextrin is 16fold higher than that of maltotriose. Compared to the kcat/Km value toward maltotriose, the values for longer substrates such as maltotetraose and maltopentaose are negligible
-
-
?
maltopentaose + H2O
maltose
-
substrate/product binding structure, sugar subsite conformations, overview
-
-
?
maltose + H2O
?
the enzyme is specific for short alpha-glucans. Similar responses to maltose, glycogen, and starch but not to pullulan
-
-
?
maltotetraose + H2O
2 maltose
maltotriose + H2O
?
-
very poor substrate
-
-
?
maltotriose + H2O
maltose + D-glucose
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + glucose
-
-
-
-
?
p-nitrophenylmaltopentaoside + H2O
?
p-nitrophenylmaltopentaoside + H2O
p-nitrophenol + maltopentaose
catalyzes the release of p-nitrophenol, specific substrate
-
-
?
pullulan + H2O
?
-
-
-
-
?
soluble starch + H2O
maltose + ?
starch + H2O
beta-maltose
starch + H2O
beta-maltose + ?
-
-
-
-
?
additional information
?
-
amylopectin + H2O
?
-
88% of the activity with starch
-
-
?
amylopectin + H2O
?
-
88% of the activity with starch
-
-
?
amylopectin + H2O
?
from potato, active site structure, Glu-186 and Glu-380 play important roles as general acid and base catalyst
-
-
?
amylopectin + H2O
?
-
114.6% of the activity with amylose, soluble starch, amylose and amylopectin are the most suitable substrates, exo-hydrolase that releases beta-maltose from the non-reducing end of alpha-1,4-linked poly- and oligoglucans until the first alpha-1,6-branching point along the substrate molecule is encountered
-
-
?
amylopectin + H2O
beta-maltose + ?
-
-
-
-
?
amylopectin + H2O
beta-maltose + ?
-
-
-
?
amylopectin + H2O
beta-maltose + ?
-
-
-
-
?
amylopectin + H2O
beta-maltose + ?
-
-
and limit dextrin
?
amylopectin + H2O
beta-maltose + ?
-
-
-
-
?
amylopectin + H2O
beta-maltose + ?
-
-
-
-
?
amylopectin + H2O
beta-maltose + ?
-
-
-
-
?
amylopectin + H2O
beta-maltose + ?
-
-
-
-
?
amylopectin + H2O
beta-maltose + ?
-
-
-
?
amylopectin + H2O
beta-maltose + ?
-
-
-
-
?
amylopectin + H2O
beta-maltose + ?
Paenibacillus polymyxa No. 26-1
-
-
-
-
?
amylopectin + H2O
beta-maltose + ?
-
-
-
-
?
amylopectin + H2O
beta-maltose + ?
-
-
-
-
?
amylopectin + H2O
beta-maltose + ?
-
-
-
-
?
amylopectin + H2O
beta-maltose + ?
-
-
-
-
?
amylopectin + H2O
maltose + ?
-
-
-
?
amylopectin + H2O
maltose + ?
from potato
-
-
?
amylopectin + H2O
maltose + ?
catalyzes the release of maltose residues, amylopectin and starch are better substrates than amylose
-
-
?
amylopectin + H2O
maltose + ?
-
-
-
-
?
amylopectin + H2O
maltose + ?
-
from potato
-
-
?
amylopectin + H2O
maltose + ?
Sorghum sp.
-
from starch, preferred substrate
-
-
?
amylopectin + H2O
maltose + ?
the enzyme only releases maltose from polymers such as soluble starch, amylopectin, and glycogen, while maltose is rarely detected from reaction with amylose and pullulan
-
-
?
amylopectin + H2O
maltose + ?
the enzyme only releases maltose from polymers such as soluble starch, amylopectin, and glycogen, while maltose is rarely detected from reaction with amylose and pullulan
-
-
?
amylose + H2O
?
-
DPn is 16
-
-
?
amylose + H2O
?
-
79% of the activity with starch
-
-
?
amylose + H2O
?
-
79% of the activity with starch
-
-
?
amylose + H2O
?
-
EX-I, soluble starch, amylose and amylopectin are the most suitable substrates, exo-hydrolase that releases beta-maltose from the non-reducing end of alpha-1,4-linked poly- and oligoglucans until the first alpha-1,6-branching point along the substrate molecule is encountered
-
-
?
amylose + H2O
beta-maltose
-
-
-
?
amylose + H2O
beta-maltose
-
-
-
-
?
amylose + H2O
beta-maltose
-
-
-
?
amylose + H2O
beta-maltose
-
-
-
-
?
amylose + H2O
beta-maltose
-
DP = 17
-
-
?
amylose + H2O
beta-maltose
-
-
-
-
?
amylose + H2O
beta-maltose
-
-
-
-
?
amylose + H2O
beta-maltose
-
partly oxidized amylose
-
-
?
amylose + H2O
beta-maltose
Paenibacillus polymyxa No. 26-1
-
-
-
-
?
amylose + H2O
beta-maltose
-
-
-
-
?
amylose + H2O
beta-maltose
-
-
-
?
amylose + H2O
beta-maltose
-
-
-
-
?
amylose + H2O
beta-maltose
-
-
-
-
?
amylose + H2O
beta-maltose
-
-
-
-
?
amylose + H2O
beta-maltose
-
-
-
-
?
dextrin + H2O
?
-
13% of the activity with starch
-
-
?
dextrin + H2O
?
-
13% of the activity with starch
-
-
?
dextrin + H2O
?
-
-
-
-
?
glycogen + H2O
?
-
49.4% of the activity with amylose
-
-
?
glycogen + H2O
?
the enzyme is specific for short alpha-glucans. Similar responses to maltose, glycogen, and starch but not to pullulan
-
-
?
glycogen + H2O
beta-maltose
-
-
-
?
glycogen + H2O
beta-maltose
-
-
-
-
?
glycogen + H2O
beta-maltose
-
-
and limit dextrin
?
glycogen + H2O
beta-maltose
-
from oyster
-
-
?
glycogen + H2O
beta-maltose
-
-
-
-
?
glycogen + H2O
beta-maltose
-
type III and type VIII
-
-
?
glycogen + H2O
beta-maltose
-
-
-
-
?
glycogen + H2O
maltose + ?
the enzyme only releases maltose from polymers such as soluble starch, amylopectin, and glycogen, while maltose is rarely detected from reaction with amylose and pullulan
-
-
?
glycogen + H2O
maltose + ?
the enzyme only releases maltose from polymers such as soluble starch, amylopectin, and glycogen, while maltose is rarely detected from reaction with amylose and pullulan
-
-
?
maltoheptaose + H2O
?
-
-
-
-
?
maltoheptaose + H2O
?
-
-
-
-
?
maltoheptaose + H2O
?
-
34.6% of the activity with amylose
-
-
?
maltoheptaose + H2O
?
-
-
-
-
?
maltohexaose + H2O
?
-
-
-
-
?
maltohexaose + H2O
?
-
-
-
-
?
maltohexaose + H2O
?
-
23.3% of the activity with amylose
-
-
?
maltopentaose + H2O
?
-
-
-
-
?
maltopentaose + H2O
?
-
beta-amylase is an exo-enzyme that catalyzes the hydrolysis of the alpha-1,4-glucosidic linkage of the substrate liberating beta-maltose from the non-reducing end, Glu-172 and Glu-367 are catalytic residues, binding mode of substrate, substrate recognition mechanism, enzyme structure
-
-
?
maltopentaose + H2O
?
-
beta-amylase is an inverting enzyme that hydrolyzes the alpha-1,4-glucosidic linkage of the substrate liberating beta-maltose from the non-reducing end, catalytic mechanism, Glu-172 acts as general acid, Glu-367 acts as general base
-
-
?
maltopentaose + H2O
?
-
binding mode of substrate in the active site
-
-
?
maltopentaose + H2O
?
hydrolyzes the alpha-1,4-glucosidic linkage liberating beta-maltose from the non-reducing end of substrate, good substrate, mode of binding in the active site, catalytic mechanism, enzyme/domain structure
-
-
?
maltopentaose + H2O
?
-
-
-
-
?
maltopentaose + H2O
?
-
13.8% of the activity with amylose
-
-
?
maltopentose + H2O
?
-
40% of the activity with starch, exo-acting enzyme, no production of glucose
-
-
?
maltopentose + H2O
?
-
40% of the activity with starch, exo-acting enzyme, no production of glucose
-
-
?
maltotetraose + H2O
2 maltose
the enzyme displays dual hydrolysis activity toward alpha-1,4- and alpha-1,6-glycosidic linkages, the catalytic efficiency of 6-O-maltosyl-beta-cyclodextrin is 16fold higher than that of maltotriose. Compared to the kcat/Km value toward maltotriose, the values for longer substrates such as maltotetraose and maltopentaose are negligible
-
-
?
maltotetraose + H2O
2 maltose
the enzyme displays dual hydrolysis activity toward alpha-1,4- and alpha-1,6-glycosidic linkages, the catalytic efficiency of 6-O-maltosyl-beta-cyclodextrin is 16fold higher than that of maltotriose. Compared to the kcat/Km value toward maltotriose, the values for longer substrates such as maltotetraose and maltopentaose are negligible
-
-
?
maltotetraose + H2O
?
-
-
-
-
?
maltotetraose + H2O
?
-
-
-
-
?
maltotetraose + H2O
?
-
7.6% of the activity with amylose
-
-
?
maltotetraose + H2O
?
-
37% of the activity with starch, exo-acting enzyme, no production of glucose
-
-
?
maltotetraose + H2O
?
-
37% of the activity with starch, exo-acting enzyme, no production of glucose
-
-
?
maltotriose + H2O
maltose + D-glucose
the enzyme displays dual hydrolysis activity toward alpha-1,4- and alpha-1,6-glycosidic linkages, the catalytic efficiency of 6-O-maltosyl-beta-cyclodextrin is 16fold higher than that of maltotriose. Compared to the kcat/Km value toward maltotriose, the values for longer substrates such as maltotetraose and maltopentaose are negligible
-
-
?
maltotriose + H2O
maltose + D-glucose
the enzyme displays dual hydrolysis activity toward alpha-1,4- and alpha-1,6-glycosidic linkages, the catalytic efficiency of 6-O-maltosyl-beta-cyclodextrin is 16fold higher than that of maltotriose. Compared to the kcat/Km value toward maltotriose, the values for longer substrates such as maltotetraose and maltopentaose are negligible
-
-
?
p-nitrophenylmaltopentaoside + H2O
?
-
-
-
-
?
p-nitrophenylmaltopentaoside + H2O
?
catalyzes the release of maltose
-
-
?
p-nitrophenylmaltopentaoside + H2O
?
-
catalyzes the release of maltose
-
-
?
p-nitrophenylmaltopentaoside + H2O
?
-
-
-
-
?
soluble starch + H2O
?
-
starch granules from various sources
-
-
?
soluble starch + H2O
?
-
-
-
-
?
soluble starch + H2O
maltose + ?
the enzyme only releases maltose from polymers such as soluble starch, amylopectin, and glycogen, while maltose is rarely detected from reaction with amylose and pullulan
-
-
?
soluble starch + H2O
maltose + ?
the enzyme only releases maltose from polymers such as soluble starch, amylopectin, and glycogen, while maltose is rarely detected from reaction with amylose and pullulan
-
-
?
starch + H2O
?
in vitro breakdown of semicrystalline starch particles by beta-amylases increases significantly if they act together with glucan, water dikinase
-
-
?
starch + H2O
?
-
starch substrate of different sources, e.g. wheat, wheat bran, rice bran, the enzyme from strain MNU82 utilizes raw and cooked starch
-
-
?
starch + H2O
?
-
starch substrate of different sources, e.g. wheat, wheat bran, rice bran
-
-
?
starch + H2O
?
-
beta-amylase hydrolyzes alpha-1,4-linkage, raw starch granules from potato, wheat, rice and corn, with the granules from rice being the best substrate, beta-amylase attacks very slowly on the starch granules, hydrolyzes corn granules efficiently at 45°C
-
-
?
starch + H2O
?
-
beta-amylase is an exo-enzyme that catalyzes the hydrolysis of the alpha-1,4-glucosidic linkage of the substrate liberating beta-maltose from the non-reducing end, Glu-172 and Glu-367 are catalytic residues, substrate recognition mechanism, enzyme structure
-
-
?
starch + H2O
?
-
beta-amylase is an inverting enzyme that hydrolyzes the alpha-1,4-glucosidic linkage of the substrate liberating beta-maltose from the non-reducing end, catalytic mechanism, Glu-172 acts as general acid, Glu-367 acts as general base
-
-
?
starch + H2O
?
-
catalyzes the hydrolysis of alpha-1,4-glucosidic linkages of soluble starch, and liberates beta-anomeric maltose from the nonreducing ends, exo-acting enzyme, composed of two functional domains, a catalytic domain: domains A and B, and starch-binding domain: domain C, beta-amylase has three carbohydrate-binding sites aside from the active site: two in domain B named Site2 and Site3, one in domain C named Site1, roles of these sites in the catalytic reaction and raw starch-binding, beta-amylase hardly hydrolyzes raw starch from wheat, corn, potato or sweet potato, but binds to it strongly
-
-
?
starch + H2O
?
hydrolyzes the alpha-1,4-glucosidic linkage liberating beta-maltose from the non-reducing end of substrate, enzyme/domain structure, starch binding site in domain C, catalytic mechanism
-
-
?
starch + H2O
?
-
starch substrate of different sources, e.g. wheat, wheat bran, rice bran
-
-
?
starch + H2O
?
Debaryomyces sp.
-
-
-
-
?
starch + H2O
?
Debaryomyces sp.
-
starch substrate of different sources, e.g. wheat, wheat bran, rice bran
-
-
?
starch + H2O
?
active site structure, Glu-186 and Glu-380 play important roles as general acid and base catalyst, catalyzes the liberation of beta-anomeric maltose from the non-reducing ends
-
-
?
starch + H2O
?
-
beta-amylase hydrolyzes alpha-1,4-linkage, raw starch granules from potato, wheat, rice and corn, with the granules from rice being the best substrate, no efficient hydrolysis of raw starch granules, very slow enzymic attack
-
-
?
starch + H2O
?
-
catalyzes the release of maltose from soluble starch, three-dimensional structures of Sd2L and V233A mutant of Sd1
-
-
?
starch + H2O
?
from potato, catalyzes the release of maltose from the non-reducing ends of starch, three-dimensional structure of Sd2L
-
-
?
starch + H2O
?
-
starch substrate of different sources, e.g. wheat, wheat bran, rice bran
-
-
?
starch + H2O
?
-
starch substrate of different sources, e.g. wheat, wheat bran, rice bran
-
-
?
starch + H2O
?
-
starch substrate of different sources, e.g. wheat, wheat bran, rice bran
-
-
?
starch + H2O
?
-
beta-amylase should be a key enzyme in starch degradation during the germination of millet seeds, enzyme activity increases during days 1-4 of germination
-
-
?
starch + H2O
?
-
106.9% of the activity with amylose, soluble starch, amylose and amylopectin are the most suitable substrates, some activity against native starch, exo-hydrolase that releases beta-maltose from the non-reducing end of alpha-1,4-linked poly- and oligoglucans until the first alpha-1,6-branching point along the substrate molecule is encountered
-
-
?
starch + H2O
?
-
starch substrate of different sources, e.g. wheat, wheat bran, rice bran
-
-
?
starch + H2O
?
the enzyme is specific for short alpha-glucans. Similar responses to maltose, glycogen, and starch but not to pullulan
-
-
?
starch + H2O
?
-
starch substrate of different sources, e.g. wheat, wheat bran, rice bran
-
-
?
starch + H2O
?
-
starch substrate of different sources, e.g. wheat, wheat bran, rice bran
-
-
?
starch + H2O
?
-
starch substrate of different sources, e.g. wheat, wheat bran, rice bran
-
-
?
starch + H2O
?
-
starch substrate of different sources, e.g. wheat, wheat bran, rice bran
-
-
?
starch + H2O
?
-
starch substrate of different sources, e.g. wheat, wheat bran, rice bran
-
-
?
starch + H2O
?
-
starch substrate of different sources, e.g. wheat, wheat bran, rice bran
-
-
?
starch + H2O
?
-
starch substrate of different sources, e.g. wheat, wheat bran, rice bran
-
-
?
starch + H2O
?
-
highest activity, exo-acting enzyme, no production of glucose
-
-
?
starch + H2O
?
-
highest activity, exo-acting enzyme, no production of glucose
-
-
?
starch + H2O
beta-maltose
-
-
-
-
?
starch + H2O
beta-maltose
-
best substrate, pure and low quality starches, maize starch, tapioca starch
maltose is the major end product, traces of maltooligosaccharides, no glucose as product
-
?
starch + H2O
beta-maltose
-
best substrate, pure and low quality starches, maize starch, tapioca starch
maltose is the major end product, traces of maltooligosaccharides, no glucose as product
-
?
starch + H2O
beta-maltose
-
-
-
-
?
starch + H2O
beta-maltose
-
-
-
?
starch + H2O
beta-maltose
-
beta-amylase is involved in starch degradation during mango ripening, which is clearly triggered by detachment from the mother-plant
-
-
?
starch + H2O
maltose
-
-
-
-
?
starch + H2O
maltose
-
-
-
?
starch + H2O
maltose
-
-
-
?
starch + H2O
maltose
soluble starch
-
-
?
starch + H2O
maltose
enzyme induction upon a cold shock at 4°C leads to starch-dependent maltose accumulation, which might be required for protection of the photosynthetic electron transport chain and sensitization of PSII during freezing, maltose influences the carbohydrate metabolism, overview
-
-
?
starch + H2O
maltose
-
role of beta-amylase in starch breakdown during temperature stress, product maltose acts as a cryoprotectant and precursor of soluble sugar metabolism, overview
-
-
?
starch + H2O
maltose
the isozyme is involved in leaf starch degradation
-
-
?
starch + H2O
maltose
-
-
-
?
starch + H2O
maltose
-
soluble
-
-
?
starch + H2O
maltose
-
-
-
-
?
starch + H2O
maltose
-
soluble
beta-maltose
?
starch + H2O
maltose
-
-
-
-
?
starch + H2O
maltose
-
-
-
-
?
starch + H2O
maltose
-
millet starch, gelatinization temperature is 61.1-68.7°C
-
-
?
starch + H2O
maltose
-
-
-
-
?
starch + H2O
maltose
-
in roots during storage, the starch hydrolysis at low temperatures is required for improvement of gustative quality of roots from tuberous-rooted chervil, at higher storage temperature the alpha-amylase activity is increased
-
-
?
starch + H2O
maltose
-
soluble
-
-
?
starch + H2O
maltose
-
raw starch from wheat, corn, potato and rice
-
-
?
starch + H2O
maltose
Dioscorea batatus
-
soluble
beta-maltose
?
starch + H2O
maltose
-
-
-
?
starch + H2O
maltose
-
-
-
-
?
starch + H2O
maltose
-
soluble
-
?
starch + H2O
maltose
-
soluble
-
?
starch + H2O
maltose
-
soluble
-
-
?
starch + H2O
maltose
-
-
main product
-
?
starch + H2O
maltose
-
-
main product
-
?
starch + H2O
maltose
-
-
-
-
?
starch + H2O
maltose
-
soluble
-
?
starch + H2O
maltose
-
soluble
-
-
?
starch + H2O
maltose
-
soluble
beta-maltose
?
starch + H2O
maltose
-
soluble starch, depolymerization, reaction scheme
-
-
?
starch + H2O
maltose
-
waxy from maize
-
-
?
starch + H2O
maltose
-
soluble
-
?
starch + H2O
maltose
-
soluble
-
-
?
starch + H2O
maltose
-
soluble
-
-
?
starch + H2O
maltose
-
soluble
beta-maltose
?
starch + H2O
maltose
-
soluble
-
-
?
starch + H2O
maltose
-
potato starch
-
?
starch + H2O
maltose
-
-
beta-maltose
?
starch + H2O
maltose
-
soluble
-
-
?
starch + H2O
maltose
-
raw starch from corn and potato
-
-
?
starch + H2O
maltose
-
degradation of starch granules by the enzyme alone occurs at the equatorial grooves of lecticular granules
-
-
?
starch + H2O
maltose
Paenibacillus polymyxa No. 26-1
-
soluble
-
-
?
starch + H2O
maltose
Paenibacillus polymyxa No. 26-1
-
raw starch from corn and potato
-
-
?
starch + H2O
maltose
Paenibacillus polymyxa No. 26-1
-
degradation of starch granules by the enzyme alone occurs at the equatorial grooves of lecticular granules
-
-
?
starch + H2O
maltose
Paenibacillus polymyxa No. 72
-
-
beta-maltose
?
starch + H2O
maltose
-
grains
-
-
-
starch + H2O
maltose
-
-
-
?
starch + H2O
maltose
-
-
-
-
?
starch + H2O
maltose
-
potato starch
-
?
starch + H2O
maltose
Sorghum sp.
-
-
-
-
?
starch + H2O
maltose
Sorghum sp.
-
Sorghum starch, gelatinization temperature is 70-75°C
-
-
?
starch + H2O
maltose
-
boiled
-
-
?
starch + H2O
maltose
-
soluble
-
-
?
starch + H2O
maltose
-
gelatinized starch
-
-
?
starch + H2O
maltose
-
-
-
?
starch + H2O
maltose
-
-
-
?
starch + H2O
maltose
-
-
-
-
?
starch + H2O
maltose
-
soluble starch
-
-
?
starch + H2O
maltose
-
soluble
-
-
?
starch + H2O
maltose + ?
-
-
-
?
starch + H2O
maltose + ?
-
-
-
?
starch + H2O
maltose + ?
catalyzes the release of maltose residues, starch and amylopectin are better substrates than amylose
-
-
?
starch + H2O
maltose + ?
-
-
-
-
?
additional information
?
-
-
plants mechanism of cold adaptation, enzyme regulation by phytohormones, light, and by abiotic stess, e.g. by osmotic, cold, salt, and drought stress, the enzyme is also regulated by the circadian clock, detailed overview
-
-
-
additional information
?
-
the isozyme TR-BAMY is redox- and thioredoxin-regulated involving residues C470 and C32 forming a disulfide bridge, the precursor enzyme conatining the transit pepetide is inactive
-
-
-
additional information
?
-
the isozyme TR-BAMY is redox- and thioredoxin-regulated involving residues C470 and C32 forming a disulfide bridge, the precursor enzyme conatining the transit pepetide is inactive
-
-
-
additional information
?
-
-
no hydrolysis of alpha-1,6-glucosidic linkages
-
-
-
additional information
?
-
beta-amylase does not catalyze a transglycosylation reaction
-
-
-
additional information
?
-
-
not: xylan, pullulan, cellulose, carboxymethyl cellulose
-
-
-
additional information
?
-
-
not: xylan, pullulan, cellulose, carboxymethyl cellulose
-
-
-
additional information
?
-
-
rhizome beta-amylase is a cytoplasmic vegetative storage protein
-
-
-
additional information
?
-
rhizome beta-amylase is a cytoplasmic vegetative storage protein
-
-
-
additional information
?
-
-
beta-amylase exclusively catalyzes the release of beta-maltose from the non-reducing ends of alpha-1,4-linked oligo- and polyglucans, three-dimensional structure
-
-
-
additional information
?
-
beta-amylase exclusively catalyzes the release of beta-maltose from the non-reducing ends of alpha-1,4-linked oligo- and polyglucans, three-dimensional structure
-
-
-
additional information
?
-
Dioscorea batatus
-
no activity with cyclodextrins
-
-
-
additional information
?
-
-
no activity with pullulan
-
-
-
additional information
?
-
-
soybean trypsin inhibitor and beta-amylase induce rat alveolar macrophages to release nitrogen oxides
-
-
-
additional information
?
-
-
maltose is the main product of soluble starch hydrolysis
-
-
-
additional information
?
-
-
maltose is the main product of soluble starch hydrolysis
-
-
-
additional information
?
-
-
germination markedly increases the beta-amylase
-
-
-
additional information
?
-
-
starch gelatinization assay, overview
-
-
-
additional information
?
-
-
beta-amylase is an exo-enzyme that specifically binds to a double (1-4-alpha-D-glucopyranosyl-1-4-alpha-D-glucopyranosyl-) unit from the non-reducing ends of polymaltosidic polysaccharides, and sequentially cleaves glucose disaccharidic units until it encounters any structural variation, producing maltose as sole hydrolysis product
-
-
-
additional information
?
-
-
no hydrolysis of beta-limit dextrin
-
-
-
additional information
?
-
-
no activity with pullulan
-
-
-
additional information
?
-
-
no hydrolysis of beta-limit dextrin
-
-
-
additional information
?
-
-
no activity with maltotriose and cycloheptaose
-
-
-
additional information
?
-
-
moderately branched glucans are better substrates than less branched or non-branched or highly branched glucans
-
-
-
additional information
?
-
-
no hydrolysis of beta-limit dextrin
-
-
-
additional information
?
-
-
the enzyme does not hydrolyze starch, glycogen, pullulan or large maltooligosaccharides
-
-
-
additional information
?
-
the enzyme does not hydrolyze starch, glycogen, pullulan or large maltooligosaccharides
-
-
-
additional information
?
-
-
germination markedly increases the beta-amylase
-
-
-
additional information
?
-
-
no activity with pullulan
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
cysteine, tryptophan and serine are essential amino acids for catalysis, not: maltotriose
-
-
-
additional information
?
-
-
cysteine, tryptophan and serine are essential amino acids for catalysis, not: maltotriose
-
-
-
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2,3-epoxypropyl-alpha-D-glucopyranoside
-
affinity-labeling reagent, mode of binding, covalently bound to the catalytic residue Glu-172, inactivation mechanism
3,4-epoxybutyl-alpha-D-glucopyranoside
-
affinity-labeling reagent, mode of binding, covalently bound to the catalytic residue Glu-172
4-chloromercuribenzoate
-
inactivation, the enzyme can be reactivated by L-cysteine
5,5'-dithiobis-(2-nitrobenzoic acid)
-
chemical modification of the exposed sulfhydryl groups in beta-amylase from unmalted seeds with 5,5'-dithiobis-(2-nitrobenzoic acid) results in loss of activity. In the beta-amylase from malted seed the 5,5'-dithiobis-(2-nitrobenzoic acid) chemical modification results in the increase in the KM from 2.81 to 4.14 mg/ml
5,5'-dithiobis-2-nitrobenzoate
-
weak
AgNO3
-
1 mM, 94% inhibition
Al2(SO4)3
-
1 mM, 57% inhibition
alpha-cyclohexaamylose
-
-
Bi(NO3)3
-
1 mM, 54% inhibition
Ca2+
-
binds at the active site
CuCl2
-
1 mM, 93% inhibition
D-mannose
125 mM, 6% inhibition, p-nitrophenylmaltopentaoside hydrolysis
diethyl dicarbonate
-
complete inhibition
FeCl3
-
1 mM, 16% inhibition
maltitol
-
behaves as a mixed-type or competitive inhibitor depending on the chain length of the substrate, inhibition mechanism, binds to Site2 in domain B and forms an abortive ESI complex when amylose is used as substrate
O-alpha-D-glucopyranosyl(1-4)O-alpha-D-glucopyranosyl(1-4)D-xylopyranose
-
mode of binding in the active site cleft
O-alpha-D-xylopyranosyl(1-4)O-alpha-D-glucopyranosyl(1-4)O-alpha-D-glucopyranoside
-
mixed-type inhibition, two molecules bind to enzyme
p-Chloromercuriphenyl sulfonic acid
-
-
p-hydroxymercuribenzoate
-
0.5 mM, 96% inhibition
p-methylsulfonylfluoride
-
3 mM, 100% inhibition
Phenylarsine oxide
-
complete inhibition
Phenylglyoxal
-
3 mM, 27% inhibition
potassium ferricyanide
-
oxidation of the sulfhydryl groups of the enzyme from malted seed in presence of urea results in formation of a dimeric enzyme. The oxidative dimerization leads to inactivation of the enzyme
Schardinger maltodextrins
-
partial
-
Sodium deoxycholate
-
0.001%, 15% inhibition
Sodium dodecyl sulfate
-
0.001%, 57% inhibition
starch
-
at high concentration s
Tween 20
-
0.001%, 16% inhibition
Tween 40
-
0.001%, 15% inhibition
ZnSO4
-
1 mM, 54% inhibition
Ag+
-
-
Ag+
-
1 mM, almost complete inhibition of mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S
Ag+
-
1 mM, almost complete inhibition of recombinant enzyme
alpha-cyclodextrin
-
-
beta-amylase-inhibitor
-
several strains of Streptomyces produce a beta-amylase inhibitor when grown on a medium containing starch and deoxynojirimycin
-
beta-amylase-inhibitor
-
several strains of Streptomyces produce a beta-amylase inhibitor when grown on a medium containing starch and deoxynojirimycin
-
beta-amylase-inhibitor
-
several strains of Streptomyces produce a beta-amylase inhibitor when grown on a medium containing starch and deoxynojirimycin
-
beta-amylase-inhibitor
-
several strains of Streptomyces produce a beta-amylase inhibitor when grown on a medium containing starch and deoxynojirimycin
-
beta-amylase-inhibitor
-
several strains of Streptomyces produce a beta-amylase inhibitor when grown on a medium containing starch and deoxynojirimycin
-
beta-cyclodextrin
-
-
Cd2+
-
-
Cd2+
-
1 mM, almost complete inhibition of barley enzyme and recombinant enzyme, less inhibitory towards mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S
Cd2+
-
1 mM, almost complete inhibition of recombinant enzyme
Cu2+
-
-
Cu2+
-
1 mM, almost complete inhibition of mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S
Cu2+
-
1 mM, almost complete inhibition of recombinant enzyme
Cu2+
-
1 mM CuSO4, 50% inhibition
Cu2+
-
5 mM, 37°C, 30 min, about 80% inhibition
cyclohexaamylose
-
alpha-CD, competitive inhibitor
cyclohexaamylose
iodine staining method, competitive inhibition
D-glucose
-
mode of binding in the active site cleft
D-glucose
p-nitrophenylmaltopentaoside hydrolysis: 125 mM, 87.5% inhibition, iodine staining method: mixed-type, weak inhibition compared with maltose and cyclohexaamylose
D-maltose
-
mode of binding in the active site cleft
EDTA
-
-
EDTA
-
non-competitive, Ca2+ fully restores activity
Fe3+
-
-
Hg2+
-
HgCl2
Hg2+
-
1 mM, almost complete inhibition of mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S
Hg2+
-
1 mM, almost complete inhibition of recombinant enzyme
Hg2+
-
0.001-0.1 mM HgCl2
Hg2+
-
5 mM, 37°C, 30 min, about 80% inhibition
HgCl2
-
1 mM, 93% inhibition
HgCl2
-
10 mM, 100% inhibition
iodoacetamide
-
-
iodoacetic acid
-
-
iodoacetic acid
-
partial
maltose
p-nitrophenylmaltopentaoside hydrolysis: 125 mM, 87.5% inhibition, iodine staining method: competitive inhibition
maltose
-
inhibits light amylase
Mg2+
-
mild inhibitor
Mg2+
-
binds at the active site
Mn2+
-
mild inhibitor
Mn2+
-
5 mM, 37°C, 30 min, about 80% inhibition
N-bromosuccinimide
-
0.4 mM
N-bromosuccinimide
-
1 mM, 84% inhibition
N-ethylmaleimide
-
remarkably reduces activity
N-ethylmaleimide
-
10 mM, 73% inhibition
NEM
-
partial
p-chloromercuribenzoate
-
1 mM, 97% inhibition, exogenous thiols like dithiothreitol, 2-mercaptoethanol or cysteine HCl reactivate
p-chloromercuribenzoate
-
0.01 mM, 100% inhibition
PCMB
-
cysteine reactivates
PCMB
-
0.5 mM, 75% loss of activity after 30 min at 22°C, cysteine reactivates
PCMB
-
restored by mercaptoethanol or dithiothreitol
PCMB
-
0.1 mM, complete inhibition of mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S
PCMB
-
0.1 mM, complete inhibition of recombinant enzyme
PCMB
-
0.001-0.1 mM, inactivation is partly reversed by adding 10fold to 20fold excess of glutathione or 1,2-dithiopropanol
PCMB
-
cysteine reactivates
Zn2+
-
mild inhibitor
Zn2+
-
1 mM, almost complete inhibition of barley enzyme and recombinant enzyme, less inhibitory towards mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S
Zn2+
-
1 mM, almost complete inhibition of recombinant enzyme
Zn2+
-
binds at the active site
additional information
the 41 amino acid transit peptide inhibits isozyme TR-BAMY
-
additional information
the 41 amino acid transit peptide inhibits isozyme TR-BAMY
-
additional information
-
not inhibited by 250 mM lactose
-
additional information
not inhibited by 250 mM lactose
-
additional information
-
PMSF and 2-mercaptoethanol have no significant effect on the amylase activity
-
additional information
-
no inhibition by 4-chloromercuribenzoate, heavy metal ions, nor Schardinger dextrins
-
additional information
-
the synthesis of beta-amylase is repressed by glucose, fructose or sucrose as carbon source, not inhibited by EDTA
-
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0.0827
4-nitrophenyl alpha-maltopyranoside
pH 7.0, 90°C
0.13 - 0.17
amylodextrin
-
chain lengths geater than 50
-
1.02 - 16.2
maltopentaose
4.17 - 18.2
maltotetraose
4.25
maltotriose
pH 5.0, 85°C
0.73
p-nitrophenylmaltopentaoside
-
-
additional information
additional information
0.26
amylopectin
-
pH 5.4, 37°C, recombinant mutant T342A
0.39
amylopectin
-
pH 5.4, 37°C, recombinant mutant T342S
0.47
amylopectin
37°C, recombinant mutant T47M/Y164E/T328N
0.73
amylopectin
37°C, recombinant wild-type enzyme
0.92
amylopectin
37°C, recombinant mutant Y164F
1.22
amylopectin
37°C, recombinant mutant Y164Q
1.24
amylopectin
37°C, recombinant mutant Y164E
1.84
amylopectin
-
pH 5.4, 37°C, recombinant mutant T342V
1.94
amylopectin
-
pH 5.4, 37°C, recombinant wild-type enzyme
2.63
amylopectin
37°C, recombinant mutant Y164H
0.491
amylose
-
DP = 17, mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S
0.6
amylose
-
pH 7, 25°C, DPn: 16, S235A/Y249A/W449F/W495F quadruple mutant
0.61
amylose
-
pH 7, 25°C, DPn: 16, W449F/W495F double mutant
0.65
amylose
-
pH 7, 25°C, DPn: 16, S235A/Y249A double mutant
0.7
amylose
-
pH 7, 25°C, DPn: 16, S235A mutant
0.71
amylose
-
pH 7, 25°C, DPn: 16, Y249A mutant
0.72
amylose
-
pH 7, 25°C, DPn: 16, wild-type enzyme
0.16
maltodextrin
-
with 50 glucose equivalents per chain
0.17
maltodextrin
-
with 98 glucose equivalents per chain
0.36
maltodextrin
-
with 31 glucose equivalents per chain
0.67
maltodextrin
-
with 16 glucose equivalents per chain
1.3
maltodextrin
-
with 9 glucose equivalents per chain
0.9
maltoheptaose
-
-
1.83
maltoheptaose
-
mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S
0.89
maltohexaose
-
-
2
maltohexaose
-
mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S
1.02
maltopentaose
-
-
1.94
maltopentaose
-
pH 5.4, 37°C, wild-type enzyme
2.02
maltopentaose
-
pH 5.4, 37°C, mutant E380Q
2.15
maltopentaose
-
pH 5.4, 37°C, mutant E186Q
2.83
maltopentaose
-
mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S
16.2
maltopentaose
pH 5.0, 85°C
4.17
maltotetraose
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mutant enzyme M185L/S295A/I297V/S350P/S351P/Q352D/A376S
18.2
maltotetraose
pH 5.0, 85°C
0.00317
starch
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pH 5, 40°C, soluble starch, V233A mutant of Sd1
0.0033
starch
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pH 5, 40°C, soluble starch, wild-type Sd1
0.0036
starch
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pH 5, 40°C, soluble starch, R115C mutant of Sd2L
0.00825
starch
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pH 5, 40°C, soluble starch, V233A mutant of Sd2L
0.0083
starch
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pH 5, 40°C, soluble starch, wild-type Sd2H and V233A/L347S double mutant of Sd2L
0.00831
starch
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pH 5, 40°C, soluble starch, wild-type Sd2L
0.00834
starch
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pH 5, 40°C, soluble starch, L347S mutant of Sd2L
0.00838
starch
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pH 5, 40°C, soluble starch, V430A mutant of Sd2L
0.00856
starch
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pH 5, 40°C, soluble starch, D165E mutant of Sd2L
additional information
additional information
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Km: 1.67 mg/ml for soluble starch
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additional information
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Km: 2.29 mg/ml for soluble starch at 60°C, 1.68 mg/ml for soluble starch at 75°C
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Km: 1.25 mg/ml for starch
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Km for soluble starch is 0.4%
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5.9 mg/ml for soluble starch, light amylase. 6.8 mg/ml for soluble starch for soluble starch, heavy amylase
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additional information
additional information
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Km: 2.25 mg/ml for amylopectin for isoenzyme 2, Km: 1.65 mg/ml for amylopectin, isoenzyme 6
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additional information
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Km: 3 mg/ml for soluble starch
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the Km-value for linear maltodextrins decreases with chain-lengths up to about 50 glucose units and with longer chain lengths it remains constant at about 0.14 mM
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Km with amylase is 0.24%
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Km for starch is 4.34 mg/ml at 60°C
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additional information
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beta-amylase from germinated barley has a higher substrate binding affinity for starch than enzyme from mature grain, removal of the four C-terminal glycine-rich repeats enhances the substrate binding affinity, kinetic parameters for several deletion mutants
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additional information
additional information
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binding parameters of wild-type and mutant enzymes to raw corn starch
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additional information
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kinetic parameters for wild-type and mutant SBA
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the 3 allelic forms of beta-amylase Sd1, Sd2H and Sd2L exhibit different kinetic properties, an R115C mutation is responsible for this difference
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additional information
additional information
kinetics, recombinant wild-type andmutant enzymes
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kinetics
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additional information
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kinetics, isothermal titration microcalorimetric method
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13.6 mg/l, starch as substrate
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Enzyme Nomenclature
New: Word Map on EC 3.2.1.2
COMMENTARY
3.2.1.2-RECOMMENDED NAME
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains
Sorghum sp.gene At3g23920/F14O13_11, isozyme TR-BAMY; contains six extrachloroplastic isozymes, and three plastid-targeted isozymesSwissProt
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