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4-nitrophenyl alpha-D-maltohexaoside + H2O
4-nitrophenol + maltohexaose
-
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + D-glucose
poor substrate
-
-
?
4-nitrophenyl maltopyranoside + H2O
4-nitrophenol + maltose
excellent substrate
-
-
?
acarbose + alpha-D-glucose
isoacarbose
acarbose + H2O
acarviosine-glucose + alpha-D-glucose
acarbose + H2O
acarviosine-glucose + D-glucose
-
-
-
-
?
acarbose + H2O
alpha-maltose + ?
acarbose + H2O
D-glucose + acarviosine-glucose
acarbose + H2O
glucose + acarviosine-glucose
-
-
-
-
?
alpha-(1,4)-glycosidic linked cyclodextrins + H2O
maltooligosaccharide
-
main depolymerization of outer amylopectin branches
-
-
?
alpha-cyclodextrin + H2O
?
alpha-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
-
-
molar ratio 10:1
?
alpha-cyclodextrin + H2O
maltose + ?
-
-
-
?
alpha-cyclodextrin + H2O
maltose + D-glucose
-
-
-
?
alpha-Schardinger dextrin + H2O
alpha-maltose + alpha-D-glucose
-
-
-
-
?
amylopectin + H2O
alpha-maltose + ?
-
hydrolytic release of maltose residues, wild-type, double and triple mutant enzymes studied to determine substrate size and geometric shape of catalytic site
-
-
?
amylopectin + H2O
fragments of amylopectin
-
main depolymerization of outer amylopectin branches
mainly short amylopectin chains from degradation of outer branches, inhibiting amylopectin retrogradation, and therefore, amorphous starch network and week amylose network of freshly baked bread are retained
-
?
amylopectin + H2O
fragments of amylopectin + dextrin
-
main depolymerization of outer amylopectin branches
mainly short amylopectin chains from degradation of outer branches, inhibiting amylopectin retrogradation, and therefore, amorphous starch network and week amylose network of freshly baked bread are retained
-
?
amylopectin + H2O
maltose + ?
amylopectin + H2O
maltose + alpha-D-glucose
-
-
in the initial stages of hydrolysis enzyme produces maltotetraose, maltotriose and maltose, as the reaction progresses, the maltotriose and maltotetraose disappears, glucose being formed by the splitting of maltotriose into equimolar amounts of maltose and glucose
?
amylopectin + H2O
maltose + D-glucose
amylopectin + H2O
maltose + maltotriose
amylose + H2O
alpha-maltose + ?
-
substrate size and geometric shape of catalytic site analyzed, wild-type, double and triple mutant enzymes tested, wild-type enzyme hydrolyzed amylose more favourably than amylopectin
-
-
?
amylose + H2O
maltose + ?
amylose + H2O
maltose + D-glucose
azurine cross-linked amylose + H2O
maltose + ?
-
-
-
-
?
beta-cyclodextrin + H2O
?
beta-cyclodextrin + H2O
alpha-maltose + ?
beta-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
beta-cyclodextrin + H2O
alpha-maltose + glucose
beta-cyclodextrin + H2O
D-glucose + maltose + maltotriose + maltooligosaccharides
100% activity
-
-
?
beta-cyclodextrin + H2O
maltooligosaccharide
-
-
-
-
?
beta-cyclodextrin + H2O
maltose + ?
beta-cyclodextrin + H2O
maltose + D-glucose
-
-
-
?
cyclomaltodextrin + H2O
alpha-maltose + alpha-D-glucose
-
-
-
-
?
D-tagatose + maltotriose
maltosyl-tagatose
-
transglycosylation
-
-
?
gamma-cyclodextrin + H2O
?
gamma-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
-
maximal activity (100%)
-
-
?
gamma-cyclodextrin + H2O
maltose + ?
-
-
-
?
gelatinised starch + H2O
maltose + ?
-
-
-
-
?
gelatinised waxy maize starch + H2O
alpha-maltose + ?
-
-
main product
-
?
gelatinized corn starch + H2O
?
-
-
-
-
?
gelatinized rice starch + H2O
maltose + ?
-
-
-
-
?
glycogen + H2O
maltose + ?
maize starch + H2O
maltose + ?
-
-
-
-
?
maltoheptaose + H2O
maltose + ?
-
-
-
-
?
maltoheptaose + H2O
maltose + D-glucose + ?
-
-
mutant enzyme A290I produces mostly maltose, while wild-type enzyme produces glucose (32.8%) as well as maltose
-
?
maltohexaose + H2O
?
-
-
-
-
?
maltohexaose + H2O
maltose + ?
-
-
-
-
?
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
?
-
-
-
-
?
maltopentaose + H2O
alpha-maltose + ?
-
-
-
-
?
maltopentaose + H2O
maltose + D-glucose + ?
-
-
-
?
maltose + H2O
2 D-glucose
-
-
-
-
?
maltotetraose + H2O
2 maltose
maltotetraose + H2O
alpha-maltose + ?
-
-
-
-
?
maltotetraose + H2O
alpha-maltose + alpha-D-glucose
-
-
-
-
?
maltotetraose + H2O
maltose + 2 D-glucose
-
-
mutant enzyme A290I produces mostly maltose, while wild-type enzyme produces glucose (24.8%) as well as maltose
-
?
maltotriose + H2O
alpha-maltose + alpha-D-glucose
maltotriose + H2O
alpha-maltose + glucose
-
-
-
?
maltotriose + H2O
isomaltose + isopanose + panose + branched glucooligosaccharides
-
-
transfer products of transglycosylation
-
?
maltotriose + H2O
maltose + D-glucose
polished rice grain + H2O
maltose + ?
-
-
-
-
?
puerarin + beta-cyclodextrin
daidzein 8-C-glucosyl-(alpha-glucosyl)n-1
-
transglycosylation activity
-
-
?
pullulan + H2O
alpha-maltose + ?
pullulan + H2O
maltose + D-glucose + panose
-
relative hydrolytic activity towards beta-cyclodextrin, soluble starch and pullulan are 8:1:1.9
mainly maltose and glucose with relatively minor quantity of panose and other maltooligosaccharides
-
?
pullulan + H2O
panose + ?
rice meal + H2O
maltose + ?
-
-
-
-
?
simmondsin + acarviosine-glucose
acarviosine-simmondsin + alpha-D-glucose
-
transglycosylation
novel compound in which acarviosine is attached to the glucose-moiety of simmondsin by an alpha-(1,6)-glycosidic linkage, with both antiobesity and hypoglycemic activity
?
soluble starch + H2O
alpha-maltose + ?
-
-
-
-
?
soluble starch + H2O
maltose + ?
starch + H2O
alpha-maltose + ?
starch + H2O
maltooligosaccharide
-
-
-
-
?
wheat starch + H2O
maltose + ?
-
-
-
-
?
additional information
?
-
acarbose + alpha-D-glucose

isoacarbose
-
transglycosylation
-
-
?
acarbose + alpha-D-glucose
isoacarbose
-
-
-
-
?
acarbose + alpha-D-glucose
isoacarbose
-
transglycosylation
-
-
?
acarbose + H2O

acarviosine-glucose + alpha-D-glucose
-
-
-
-
?
acarbose + H2O
acarviosine-glucose + alpha-D-glucose
-
-
-
-
?
acarbose + H2O
acarviosine-glucose + alpha-D-glucose
-
-
-
-
?
acarbose + H2O
acarviosine-glucose + alpha-D-glucose
-
hydrolysis
-
-
?
acarbose + H2O
acarviosine-glucose + alpha-D-glucose
-
-
-
-
?
acarbose + H2O
acarviosine-glucose + alpha-D-glucose
-
hydrolysis
-
-
?
acarbose + H2O

alpha-maltose + ?
-
-
-
-
?
acarbose + H2O
alpha-maltose + ?
-
-
-
-
?
acarbose + H2O

D-glucose + acarviosine-glucose
-
-
-
-
?
acarbose + H2O
D-glucose + acarviosine-glucose
-
-
-
-
?
acarbose + H2O
D-glucose + acarviosine-glucose
-
-
-
?
alpha-cyclodextrin + H2O

?
80% activity compared to beta-cyclodextrin
-
-
?
alpha-cyclodextrin + H2O
?
high specificity for alpha-cyclodextrin
-
-
?
alpha-cyclodextrin + H2O
?
-
-
-
?
alpha-cyclodextrin + H2O
?
-
-
-
?
alpha-cyclodextrin + H2O
?
-
64.7% activity compared to gamma-cyclodextrin
-
-
?
amylopectin + H2O

?
less than 2% activity compared to beta-cyclodextrin
-
-
?
amylopectin + H2O
?
less than 2% activity compared to beta-cyclodextrin
-
-
?
amylopectin + H2O
?
-
-
-
?
amylopectin + H2O
?
-
the maltogenic Bacillus stearothermophilus alpha-amylase preferentially hydrolyses the exterior chains of amylopectin. However, during the later phases, the enzyme also hydrolyses inner chains, presumably with a high multiple attack action
-
-
?
amylopectin + H2O

maltose + ?
-
-
-
-
?
amylopectin + H2O
maltose + ?
-
-
-
?
amylopectin + H2O
maltose + ?
the enzyme recognized maltose units with alpha-1,4 and alpha-1,6 linkages in polysaccharides (e.g., starch, amylopectin, and glycogen) and hydrolyzes pullulan very poorly. Branched cyclodextrin is only hydrolyzed along its branched maltooligosaccharides. 6-O-D-glucosyl-beta-cyclodextrin and beta-cyclodextrin are resistant. Exo-type glucan hydrolase with alpha-1,4- and alpha-1,6-glucan hydrolytic activities
maltose is the primary end product of hydrolysis
-
?
amylopectin + H2O
maltose + ?
the enzyme recognized maltose units with alpha-1,4 and alpha-1,6 linkages in polysaccharides (e.g., starch, amylopectin, and glycogen) and hydrolyzes pullulan very poorly. Branched cyclodextrin is only hydrolyzed along its branched maltooligosaccharides. 6-O-D-glucosyl-beta-cyclodextrin and beta-cyclodextrin are resistant. Exo-type glucan hydrolase with alpha-1,4- and alpha-1,6-glucan hydrolytic activities
maltose is the primary end product of hydrolysis
-
?
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 + ?
-
-
-
-
?
amylopectin + H2O
maltose + ?
-
-
-
?
amylopectin + H2O

maltose + D-glucose
-
-
-
?
amylopectin + H2O
maltose + D-glucose
-
-
-
?
amylopectin + H2O

maltose + maltotriose
-
-
wild-type enzyme produces 93% maltose (2 homomers) and 5% maltotriose compared to 66% maltose and 20% maltotriose of mutant F188L/D261G/T288P, wild-type enzyme produces 93% maltose (2 homomers) and 5% maltotriose compared to 66% maltose and 20% matotriose of mutant F188L/D261G/T288P
-
?
amylopectin + H2O
maltose + maltotriose
-
-
wild-type enzyme produces 93% maltose (2 homomers) and 5% maltotriose compared to 66% maltose and 20% maltotriose of mutant F188L/D261G/T288P, wild-type enzyme produces 93% maltose (2 homomers) and 5% maltotriose compared to 66% maltose and 20% matotriose of mutant F188L/D261G/T288P
-
?
amylose + H2O

?
45% activity compared to beta-cyclodextrin
-
-
?
amylose + H2O
?
45% activity compared to beta-cyclodextrin
-
-
?
amylose + H2O

maltose + ?
-
-
-
-
?
amylose + H2O
maltose + ?
-
-
-
?
amylose + H2O
maltose + ?
-
high preference toward amylose compared to amylopectin
-
-
?
amylose + H2O
maltose + ?
-
-
-
?
amylose + H2O

maltose + D-glucose
-
-
-
?
amylose + H2O
maltose + D-glucose
-
-
-
?
beta-cyclodextrin + H2O

?
-
-
-
?
beta-cyclodextrin + H2O
?
-
-
-
-
?
beta-cyclodextrin + H2O
?
-
-
-
?
beta-cyclodextrin + H2O
?
-
-
-
?
beta-cyclodextrin + H2O
?
-
-
-
?
beta-cyclodextrin + H2O
?
-
-
-
?
beta-cyclodextrin + H2O
?
-
-
-
?
beta-cyclodextrin + H2O
?
-
-
-
?
beta-cyclodextrin + H2O
?
-
78.1% activity compared to gamma-cyclodextrin
-
-
?
beta-cyclodextrin + H2O

alpha-maltose + ?
main product alpha-maltose
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + ?
main product alpha-maltose
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + ?
-
recombinant rLGMA, expressed in Escherichia coli and in Lactococcus lactis MG1363
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + ?
-
recombinant rLGMA, expressed in Escherichia coli and in Lactococcus lactis MG1363
-
-
?
beta-cyclodextrin + H2O

alpha-maltose + alpha-D-glucose
highest catalytic efficiency
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
highest catalytic efficiency
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
-
-
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
-
-
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
-
-
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
-
-
molar ratio 3:1
?
beta-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
-
hydrolytic activity
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
-
high thermostability, substrate preference dependent on oligomeric state
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
-
high thermostability, substrate preference dependent on oligomeric state
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
-
-
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + alpha-D-glucose
-
prefers cyclodextrins to starch or pullulan as substrate
-
-
?
beta-cyclodextrin + H2O

alpha-maltose + glucose
substrate determination for recombinant enzyme MAUS149
-
-
?
beta-cyclodextrin + H2O
alpha-maltose + glucose
substrate determination for recombinant enzyme MAUS149
-
-
?
beta-cyclodextrin + H2O

maltose + ?
the main subsites for substrate stabilization in the active site are -2, -1, +1 and +2. A bulky residue, Trp359 at the +2 subsite is identified to cause steric interference to the bound linear malto-oligosaccharides thus prevented it to occupy subsite +3, which can only be reached by a highly bent glucose molecule such as beta-cyclodextrin
-
-
?
beta-cyclodextrin + H2O
maltose + ?
the main subsites for substrate stabilization in the active site are -2, -1, +1 and +2. A bulky residue, Trp359 at the +2 subsite is identified to cause steric interference to the bound linear malto-oligosaccharides thus prevented it to occupy subsite +3, which can only be reached by a highly bent glucose molecule such as beta-cyclodextrin
-
-
?
beta-cyclodextrin + H2O
maltose + ?
-
-
mainly hydrolyzed to maltose
-
?
beta-cyclodextrin + H2O
maltose + ?
-
-
mainly hydrolyzed to maltose
-
?