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(alpha-1,4 glucan)m + (alpha-1,4 glucan)n
(alpha-1,4 glucan)m-x + (alpha-1,4 glucan)n+x
B7A9X4
-
-
-
r
(alpha-1,4-D-glucan)m + (alpha-1,4-D-glucan)m
cyclic(alpha-1,4-glucan)x + (alpha-1,4-D-glucan)m-x
(alpha-1,4-D-glucan)m + (alpha-1,4-D-glucan)n
(alpha-1,4-D-glucan)m-x + (alpha-1,4-D-glucan)n+x
(alpha-1,4-D-glucan)m + H2O
(alpha-1,4-D-glucan)x + (alpha-1,4-D-glucan)m-x
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharide
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharides
1,4-alpha-D-glucan + glucose
maltooligosaccharides
2-chloro-4-nitrophenyl 4'''',6''''-O-(3-oxobutylidene)maltopentaoside + D-glucose
?
-
the disproportionation reaction of the enzyme involves a ping-pong bi-bi mechanism. On the basis of this reaction mechanism, the glycosyl-enzyme intermediate, in which a donor substrate is covalently bound to the catalytic nucleophile, is trapped by treating the enzyme with 3-ketobutylidene-beta-2-chloro-4-nitrophenyl maltopentaoside in the absence of an acceptor and is detected by matrix-assisted laser desorption ionization time-of-flight mass spectrometry after peptic digestion
-
-
?
6-O-alpha-D-glucosyl-cyclodextrins + H2O
D-glucose + cyclodextrins
-
-
-
?
6-O-alpha-D-glucosyl-cyclomalto-octaose + H2O
D-glucose + cyclodextrins
-
-
-
?
6-O-alpha-D-glucosyl-cyclomaltoheptaose + H2O
D-glucose + cyclodextrins
64-O-alpha-maltooligosyl-pyridylamino-maltooctaose + maltohexaose
64-O-alpha-D-glucosyl-pyridylamino-maltooctaose + ?
-
4-alpha-glucanotransferase action of porcine liver GDE on four 64-O-alpha-maltooligosyl-pyridylamino-maltooctaoses, in the presence or absence of an acceptor, maltohexaose, overview
-
-
?
amylomaize V + glycosyl acceptor
cycloamylose + ?
-
-
-
-
?
amylopectin + D-glucose
small oligosaccharides
-
without maltose
?
amylopectin + maltopentaose
maltooligosaccharides
amylopectin + maltose
?
-
Gtase
-
-
?
amylose
cycloamylose
-
the enzyme produces a cycloamylose with a minimum degree of polymerization of 16
-
-
?
amylose + ?
cycloamylose + ?
-
-
-
-
?
amylose + D-glucose
low molecular mass oligosaccharides
amylose + glycosyl acceptor
?
-
-
-
?
amylose + maltopentaose
cyclic alpha-1,4-glucan
amylose + maltopentaose
maltooligosaccharides
amylose + maltose
?
-
Gtase
-
-
?
barley starch + glycosyl acceptor
?
-
transgenic barley amylose-only starch which consists of more than 99% amylose
-
-
?
cassava starch + glycosyl acceptor
?
-
-
-
-
?
cassava starch + glycosyl acceptor
large ring-cyclodextrins 25-80
-
-
-
-
?
cassava starch + glycosyl acceptor
large-ring cyclodextrins 24-29
-
-
-
-
?
cassava starch + glycosyl acceptor
maltooligosaccharides
-
-
-
-
?
corn starch + glycosyl acceptor
?
-
-
-
?
corn starch + glycosyl acceptor
large-ring cyclodextrins
cycloamylose + D-glucose
?
-
-
-
-
?
dodecyl-beta-maltoside + alpha-cyclodextrin
dodecyl-beta-maltooctaoside + ?
-
-
-
-
?
dodecyl-beta-maltoside + starch
dodecyl-beta-maltooctaoside + ?
-
when starch is used as glycosyl donor in the CGTase catalyzed alkyl glycoside elongation reaction, it is important to choose reaction conditions under which the cyclization of starch to alpha-cyclodextrin is efficient, since alpha-cyclodextrin may form low reactivity complexes with dodecyl-beta-maltoside
-
-
?
Glc-alpha-(1,4)-Glc-alpha-(1,4)-Glc-alpha(1,4)(Glc-alpha-(1,4)-Glc-alpha-(1,4)Glc-alpha-(1,4)-Glc-alpha-(1,6))Glc-alpha-(1,4)-Glc-alpha(1,4)-Glc-alpha-(1,4)-Glc-alpha-(1,4)-(1-deoxy-1-[(2-pyridyl)amino]-D-glucitol)
Glc-alpha-(1,4)-Glc-alpha-(1,4)-Glc-alpha-(1,4)(Glc-alpha-(1,6))Glc-alpha-(1,4)-Glc-alpha-(1,4)-Glc-alpha-(1,4)-Glc-alpha-(1,4)-(1-deoxy-1-[(2-pyridyl)amino]-D-glucitol) + Glc-alpha-(1,4)-Glc-alpha-(1,4)-Glc-alpha-(1,4)-Glc-alpha-(1,4)-Glc-alpha-(1,4)-Glc-alpha-(1,4)-Glc-alpha-(1,4)-(1-deoxy-1-[(2-pyridyl)amino]-D-glucitol)
-
i.e. B5/84 + G6PA
-
-
?
Glcalpha(1,4)Glcalpha(1,4)Glcalpha(1,4)(Glcalpha(1,4)Glcalpha(1,4)Glcalpha(1,4)Glcalpha(1,6))Glcalpha(1,4)Glcalpha(1,4)Glcalpha(1,4)Glcalpha(1,4)Glc-pyridylamine + H2O
maltotriose + Glcalpha(1,4)Glcalpha(1,4)Glcalpha(1,4)(Glcalpha(1,6))Glcalpha(1,4)Glcalpha(1,4)Glcalpha(1,4)Glcalpha(1,4)Glc-pyridylamine
-
-
-
-
?
glutinous-rice starch + glycosyl acceptor
large-ring cyclodextrins
glycogen + glycosyl acceptor
maltooligosaccharides
-
-
-
-
?
glycogen + maltooligosaccharides
D-glucose + ?
-
-
-
?
linear maltooligosaccharides + starch
?
maize starch + glycosyl acceptor
?
-
100% amylopectin waxy maize starch
-
-
?
maltodextrin + D-glucose
maltooligosaccharides
-
-
-
?
maltodextrin + maltodextrin
maltooligosaccharides
maltodextrin + maltose
maltooligosaccharides
maltodextrin + maltose
maltooligosaccharides + alpha-D-glucose
-
-
-
?
maltoheptaose
maltodextrin + D-glucose
-
-
-
?
maltoheptaose + glycosyl acceptor
maltose + D-glucose + maltooligosaccharides
-
worst substrate
-
-
?
maltoheptaose + maltoheptaose
?
maltoheptaose + maltoheptaose
D-glucose + maltooligosaccharides
maltoheptaose + maltoheptaose
maltooligosaccharides
-
-
-
-
?
maltoheptaose + maltopentaose
maltooligosaccharides
maltoheptaose + maltotriose
maltononaose + D-glucose
-
D-enzyme
-
?
maltohexaose + glycosyl acceptor
maltose + D-glucose + maltooligosaccharides
maltohexaose + maltodextrin
D-glucose + maltopentaose
-
only amylomaltase, no polymers larger than the initial maltodextrin substrate, maltohexaose is a good donor substrate, but unable to function as an acceptor
-
?
maltohexaose + maltohexaose
?
maltohexaose + maltohexaose
D-glucose + maltooligosaccharides
maltohexaose + maltohexaose
maltooligosaccharide
maltohexaose + maltohexaose
maltooligosaccharides
-
-
-
-
?
maltohexaose + maltopentaose
maltooligosaccharides
maltohexaose + maltotriose
D-glucose + maltooligosaccharides
-
-
-
?
maltohexaose + maltotriose
maltodextrins
maltononaose + maltotriose
maltoundecaose + D-glucose
-
D-enzyme
-
?
maltooligosaccharides
maltooligosaccharides + D-glucose
-
-
-
?
maltopentaitol
maltohexaitol + ?
maltopentaose + glycosyl acceptor
maltose + D-glucose + maltooligosaccharides
maltopentaose + maltodextrin
maltose + higher dextrins
-
-
-
?
maltopentaose + maltopentaose
?
maltopentaose + maltopentaose
D-glucose + maltooligosaccharides
maltopentaose + maltopentaose
maltooligosaccharides
maltopentaose + maltopentaose
new oligosaccharides
maltopentaose + maltotriose
D-glucose + maltooligosaccharides
maltopentaose + maltotriose
homologous 1,4-alpha-D-glucans
-
amylomaltose
-
?
maltopentaose + maltotriose
maltodextrins
maltopentaose + maltotriose
maltoheptaose + D-glucose
-
D-enzyme
-
?
maltose + (1,4-alpha-glucan)n+1
D-glucose + (1,4-alpha-glucan)n+1
maltose + beta-cyclodextrin
6-O-alpha-maltosyl-beta-cyclodextrin
maltose + D-glucose
maltodextrin + D-glucose
-
-
-
?
maltose + glycosyl acceptor
?
maltose + glycosyl acceptor
D-glucose
efficient transglycosylation activity
-
-
?
maltose + maltose
?
-
worst substrate
-
-
?
maltose + maltose
maltooligosaccharides
maltose + maltose
maltooligosaccharides + D-glucose
-
-
-
?
maltose + maltose
maltotriose + glucose
maltose + maltosyl-beta-cyclodextrin
?
maltosyl-alpha-(1->6)-puerarin
?
-
i.e. maltosyl-daidzein 8-C-glucoside
combined action of maltogenic amylase reactions from Bacillus stearothermophilus and 4-alpha-glucanotransferase from Thermus scotoductus increases the water solubility of puerarin, an isoflavonoid derived from Radix puerariae
-
?
maltotetraitol
maltopentaitol + ?
maltotetraose + glycosyl acceptor
maltose + D-glucose + maltooligosaccharides
maltotetraose + maltodextrin
maltose + higher dextrins
-
-
-
?
maltotetraose + maltopentaose
maltooligosaccharides
maltotetraose + maltotetraose
?
-
-
-
?
maltotetraose + maltotetraose
D-glucose + maltooligosaccharides
maltotetraose + maltotetraose
maltooligosaccharides
maltotetraose + maltotriose
D-glucose + maltooligosaccharides
maltotetraose + maltotriose
glucose + maltoheptaose + maltodecaose
-
D-enzyme
-
?
maltotetraose + maltotriose
homologous 1,4-alpha-glucans
-
amylomaltose
-
?
maltotetraose + maltotriose
maltodextrins
maltotheptaose + maltotriose
D-glucose + maltooligosaccharides
-
-
-
?
maltotheptaose + maltotriose
maltodextrins
maltotriose
maltodextrin + D-glucose
-
-
-
?
maltotriose
maltooligosaccharides
maltotriose + amylopectin
?
-
-
-
-
?
maltotriose + glycosyl acceptor
D-glucose + maltooligosaccharides
maltotriose + glycosyl acceptor
D-glucose + maltose + maltotetraose + maltopentaose + maltohexaose
-
-
-
?
maltotriose + glycosyl acceptor
maltose + D-glucose + maltooligosaccharides
maltotriose + maltodextrin
maltopentaose + ?
maltotriose + maltodextrin
maltose + higher dextrins
maltotriose + maltotriose
?
-
-
-
-
?
maltotriose + maltotriose
D-glucose + maltooligosaccharides
maltotriose + maltotriose
D-glucose + maltopentaose
-
-
-
-
?
maltotriose + maltotriose
D-glucose + maltopentaose + maltoheptaose + maltononaose + maltoundecaose
-
D-enzyme
-
?
maltotriose + maltotriose
glucose + maltooligosaccharides
-
-
-
?
maltotriose + maltotriose
homologous alpha-1,4-D-glucans
-
amylomaltose
-
?
maltotriose + maltotriose
maltodextrins
maltotriose + maltotriose
maltooligosaccharides
maltotriose + maltotriose
maltooligosaccharides + D-glucose
-
-
-
?
maltotriose + maltotriose
maltopentaose + D-glucose
maltotriose + maltotriose
maltopentaose + maltotetraose
pea starch + glycosyl acceptor
?
-
-
-
-
?
pea starch + glycosyl acceptor
cycloamylose + ?
-
-
-
?
pea starch + glycosyl acceptor
large ring-cyclodextrins 23-26
-
-
-
-
?
pea starch + glycosyl acceptor
large ring-cyclodextrins 29-33
-
-
-
-
?
pea starch + glycosyl acceptor
large-ring cyclodextrins
pea starch + glycosyl acceptor
large-ring cyclodextrins 24-29
-
-
-
-
?
potato amylose + glycosyl acceptor
cycloamylose
potato amylose + glycosyl acceptor
cycloamylose + ?
-
-
-
-
?
potato starch + glycosyl acceptor
?
-
-
-
?
potato starch + maltose
large-ring cyclodextrins
rice starch + glycosyl acceptor
large-ring cyclodextrins
soluble potato starch + glycosyl acceptor
?
-
-
-
-
?
soluble potato starch + maltose
?
-
-
-
-
?
starch + 2-deoxy-D-glucose
?
starch + cellobiose
?
-
-
-
-
?
starch + D-allose
oligosaccharides terminated by 4-O-alpha-D-glucopyranosyl-D-allose
-
-
-
?
starch + D-glucosamine
?
-
-
-
-
?
starch + D-glucose
low molecular mass oligosaccharides
starch + D-glucose
oligosaccharides
starch + D-mannose
oligosaccharides terminated by 4-O-alpha-D-glucopyranosyl-D-mannose
-
-
-
?
starch + D-sucrose
?
-
-
-
-
?
starch + D-xylose
oligosaccharides terminated by 4-O-alpha-D-glucopyranosyl-D-xylose
-
-
-
?
starch + glucose
maltotriose + ?
starch + glycosyl acceptor
D-glucose + maltose + glucan oligosaccharides
-
-
-
?
starch + isomaltose
?
-
-
-
-
?
starch + L-sorbose
?
-
-
-
-
?
starch + maltopentaose
alpha-1,4-D-glucans
starch + maltose
?
-
Gtase
-
-
?
starch + methyl-alpha-D-glucoside
?
starch + methyl-beta-D-glucoside
?
-
-
-
-
?
starch + N-acetyl-D-glucosamine
oligosaccharides terminated by 4-O-alpha-D-glucopyranosyl-N-acetyl-D-glucosamine
-
-
-
?
starch + phenyl-alpha-D-glucoside
?
-
-
-
-
?
starch + phenyl-beta-D-glucoside
?
-
-
-
-
?
tapioca starch + glycosyl acceptor
large-ring cyclodextrins
-
-
-
-
?
additional information
?
-
(alpha-1,4-D-glucan)m + (alpha-1,4-D-glucan)m
cyclic(alpha-1,4-glucan)x + (alpha-1,4-D-glucan)m-x
-
-
-
r
(alpha-1,4-D-glucan)m + (alpha-1,4-D-glucan)m
cyclic(alpha-1,4-glucan)x + (alpha-1,4-D-glucan)m-x
-
-
-
r
(alpha-1,4-D-glucan)m + (alpha-1,4-D-glucan)n
(alpha-1,4-D-glucan)m-x + (alpha-1,4-D-glucan)n+x
-
-
-
r
(alpha-1,4-D-glucan)m + (alpha-1,4-D-glucan)n
(alpha-1,4-D-glucan)m-x + (alpha-1,4-D-glucan)n+x
-
-
-
r
(alpha-1,4-D-glucan)m + H2O
(alpha-1,4-D-glucan)x + (alpha-1,4-D-glucan)m-x
-
-
-
r
(alpha-1,4-D-glucan)m + H2O
(alpha-1,4-D-glucan)x + (alpha-1,4-D-glucan)m-x
-
-
-
r
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharide
-
-
-
?
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharide
-
maltose and a highly branched, soluble heteroglycan are excellent substrates for DPE2
-
-
?
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharides
it is proposed that a soluble heteroglycan is the in vivo substrate for DPE2. An alternative route to metabolize the glucan residues in soluble heteroglycane exists in Arabidopsis thaliana
-
-
?
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharides
-
-
-
?
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharides
-
-
-
?
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharides
-
it is proposed that a soluble heteroglycan is the in vivo substrate for DPE2. An alternative route to metabolize the glucan residues in soluble heteroglycan exists in Escherichia coli
-
-
?
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharides
-
-
-
?
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharides
-
-
-
?
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharides
-
-
?
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharides
B7A9X4
-
-
?
1,4-alpha-D-glucan + 1,4-alpha-D-glucan
maltooligosaccharides
-
-
-
?
1,4-alpha-D-glucan + glucose
maltooligosaccharides
-
-
-
?
1,4-alpha-D-glucan + glucose
maltooligosaccharides
-
-
-
?
1,4-alpha-D-glucan + glucose
maltooligosaccharides
-
-
-
?
1,4-alpha-D-glucan + glucose
maltooligosaccharides
-
-
-
?
1,4-alpha-D-glucan + glucose
maltooligosaccharides
-
-
?
1,4-alpha-D-glucan + glucose
maltooligosaccharides
B7A9X4
-
-
?
1,4-alpha-D-glucan + glucose
maltooligosaccharides
-
-
-
?
6-O-alpha-D-glucosyl-cyclomaltoheptaose + H2O
D-glucose + cyclodextrins
-
-
-
?
6-O-alpha-D-glucosyl-cyclomaltoheptaose + H2O
D-glucose + cyclodextrins
-
-
-
-
?
amylopectin
?
incubation of the enzyme with starch or its constituents, i.e. amylose and amylopectin, leads to the formation of a set of multiples of maltose (i.e. maltose, maltotetraose, maltohexaose etc.)
-
-
?
amylopectin
?
incubation of the enzyme with starch or its constituents, i.e. amylose and amylopectin, leads to the formation of a set of multiples of maltose (i.e. maltose, maltotetraose, maltohexaose etc.)
-
-
?
amylopectin + maltopentaose
maltooligosaccharides
-
-
-
?
amylopectin + maltopentaose
maltooligosaccharides
-
-
-
?
amylopectin + maltopentaose
maltooligosaccharides
-
-
?
amylopectin + maltopentaose
maltooligosaccharides
-
-
-
?
amylopectin + maltopentaose
maltooligosaccharides
-
-
-
?
amylose
?
incubation of the enzyme with starch or its constituents, i.e. amylose and amylopectin, leads to the formation of a set of multiples of maltose (i.e. maltose, maltotetraose, maltohexaose etc.)
-
-
?
amylose
?
incubation of the enzyme with starch or its constituents, i.e. amylose and amylopectin, leads to the formation of a set of multiples of maltose (i.e. maltose, maltotetraose, maltohexaose etc.)
-
-
?
amylose + D-glucose
low molecular mass oligosaccharides
-
-
-
?
amylose + D-glucose
low molecular mass oligosaccharides
-
-
?
amylose + D-glucose
low molecular mass oligosaccharides
-
synthetic amylose AS-320
-
?
amylose + maltopentaose
cyclic alpha-1,4-glucan
-
-
-
?
amylose + maltopentaose
cyclic alpha-1,4-glucan
-
-
cycloamylose
?
amylose + maltopentaose
cyclic alpha-1,4-glucan
-
-
cycloamylose
?
amylose + maltopentaose
cyclic alpha-1,4-glucan
-
-
cycloamylose
?
amylose + maltopentaose
cyclic alpha-1,4-glucan
-
-
cycloamylose
?
amylose + maltopentaose
cyclic alpha-1,4-glucan
-
-
-
-
?
amylose + maltopentaose
cyclic alpha-1,4-glucan
-
-
cycloamylose
?
amylose + maltopentaose
cyclic alpha-1,4-glucan
-
-
cycloamylose
?
amylose + maltopentaose
cyclic alpha-1,4-glucan
-
-
cycloamylose
?
amylose + maltopentaose
cyclic alpha-1,4-glucan
-
cycloamylose
?
amylose + maltopentaose
cyclic alpha-1,4-glucan
B7A9X4
-
cycloamylose
?
amylose + maltopentaose
cyclic alpha-1,4-glucan
-
-
cycloamylose
?
amylose + maltopentaose
cyclic alpha-1,4-glucan
-
-
cycloamylose
?
amylose + maltopentaose
maltooligosaccharides
-
-
?
amylose + maltopentaose
maltooligosaccharides
-
-
-
?
amylose + maltopentaose
maltooligosaccharides
-
-
-
?
corn starch + glycosyl acceptor
large-ring cyclodextrins
-
-
-
-
?
corn starch + glycosyl acceptor
large-ring cyclodextrins
-
-
-
-
?
glutinous-rice starch + glycosyl acceptor
large-ring cyclodextrins
-
-
-
-
?
glutinous-rice starch + glycosyl acceptor
large-ring cyclodextrins
-
-
-
-
?
linear maltooligosaccharides + starch
?
-
-
-
r
linear maltooligosaccharides + starch
?
-
-
-
-
r
maltodextrin + maltodextrin
maltooligosaccharides
-
-
-
?
maltodextrin + maltodextrin
maltooligosaccharides
-
-
-
?
maltodextrin + maltodextrin
maltooligosaccharides
-
-
-
?
maltodextrin + maltose
maltooligosaccharides
-
-
-
?
maltodextrin + maltose
maltooligosaccharides
-
catabolic processing of glycogen and maltodextrins
-
?
maltodextrin + maltose
maltooligosaccharides
-
-
-
?
maltodextrin + maltose
maltooligosaccharides
-
catabolic processing of glycogen and maltodextrins
-
?
maltodextrin + maltose
maltooligosaccharides
-
-
?
maltodextrin + maltose
maltooligosaccharides
-
catabolic processing of glycogen and maltodextrins
-
?
maltodextrin + maltose
maltooligosaccharides
-
catabolic processing of glycogen and maltodextrins
-
?
maltoheptaose + maltoheptaose
?
-
-
-
-
?
maltoheptaose + maltoheptaose
?
-
-
-
-
?
maltoheptaose + maltoheptaose
?
chain length distribution of the transfer products ranges from DP2 to about DP20, which is the upper size limit of oligosaccharides resolved with the TLC system used, but presumably even larger oligomers are also formed. Glucose is not observed as a product. The transfer products exclusively contain 1,4-glucosidic linkages
-
-
?
maltoheptaose + maltoheptaose
?
chain length distribution of the transfer products ranges from DP2 to about DP20, which is the upper size limit of oligosaccharides resolved with the TLC system used, but presumably even larger oligomers are also formed. Glucose is not observed as a product. The transfer products exclusively contain 1,4-glucosidic linkages
-
-
?
maltoheptaose + maltoheptaose
?
-
-
-
?
maltoheptaose + maltoheptaose
?
-
-
-
?
maltoheptaose + maltoheptaose
D-glucose + maltooligosaccharides
-
-
-
-
?
maltoheptaose + maltoheptaose
D-glucose + maltooligosaccharides
-
-
-
-
?
maltoheptaose + maltopentaose
maltooligosaccharides
-
-
-
?
maltoheptaose + maltopentaose
maltooligosaccharides
-
-
-
?
maltoheptaose + maltopentaose
maltooligosaccharides
-
-
-
?
maltoheptaose + maltopentaose
maltooligosaccharides
-
-
-
?
maltoheptaose + maltopentaose
maltooligosaccharides
-
-
-
?
maltoheptaose + maltopentaose
maltooligosaccharides
-
-
-
?
maltohexaose + glycosyl acceptor
maltose + D-glucose + maltooligosaccharides
-
-
-
-
?
maltohexaose + glycosyl acceptor
maltose + D-glucose + maltooligosaccharides
-
-
-
-
?
maltohexaose + maltohexaose
?
chain length distribution of the transfer products ranges from DP2 to about DP20, which is the upper size limit of oligosaccharides resolved with the TLC system used, but presumably even larger oligomers are also formed. Glucose is not observed as a product. The transfer products exclusively contain 1,4-glucosidic linkages
-
-
?
maltohexaose + maltohexaose
?
chain length distribution of the transfer products ranges from DP2 to about DP20, which is the upper size limit of oligosaccharides resolved with the TLC system used, but presumably even larger oligomers are also formed. Glucose is not observed as a product. The transfer products exclusively contain 1,4-glucosidic linkages
-
-
?
maltohexaose + maltohexaose
?
-
-
-
?
maltohexaose + maltohexaose
?
-
-
-
?
maltohexaose + maltohexaose
D-glucose + maltooligosaccharides
-
-
-
-
?
maltohexaose + maltohexaose
D-glucose + maltooligosaccharides
-
-
-
-
?
maltohexaose + maltohexaose
maltooligosaccharide
-
-
-
-
?
maltohexaose + maltohexaose
maltooligosaccharide
-
-
-
-
?
maltohexaose + maltopentaose
maltooligosaccharides
-
-
-
?
maltohexaose + maltopentaose
maltooligosaccharides
-
-
-
?
maltohexaose + maltopentaose
maltooligosaccharides
-
-
-
?
maltohexaose + maltopentaose
maltooligosaccharides
-
-
-
?
maltohexaose + maltotriose
maltodextrins
-
-
-
-
?
maltohexaose + maltotriose
maltodextrins
-
-
-
-
?
maltohexaose + maltotriose
maltodextrins
-
-
-
-
?
maltohexaose + maltotriose
maltodextrins
-
-
-
-
?
maltopentaitol
maltohexaitol + ?
-
-
-
-
?
maltopentaitol
maltohexaitol + ?
-
-
-
-
?
maltopentaitol
maltohexaitol + ?
-
-
-
-
?
maltopentaose + glycosyl acceptor
maltose + D-glucose + maltooligosaccharides
-
-
-
-
?
maltopentaose + glycosyl acceptor
maltose + D-glucose + maltooligosaccharides
-
-
-
-
?
maltopentaose + maltopentaose
?
-
-
-
?
maltopentaose + maltopentaose
?
-
-
-
?
maltopentaose + maltopentaose
D-glucose + maltooligosaccharides
-
-
-
-
?
maltopentaose + maltopentaose
D-glucose + maltooligosaccharides
-
-
-
-
?
maltopentaose + maltopentaose
maltooligosaccharides
-
-
-
-
?
maltopentaose + maltopentaose
maltooligosaccharides
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
-
-
-
-
?
maltopentaose + maltopentaose
maltooligosaccharides
-
-
-
-
?
maltopentaose + maltopentaose
maltooligosaccharides
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
maltooligosaccharides
-
metabolism of starch in the bacterium
-
?
maltopentaose + maltopentaose
new oligosaccharides
-
-
-
-
?
maltopentaose + maltopentaose
new oligosaccharides
-
-
-
-
?
maltopentaose + maltopentaose
new oligosaccharides
-
capable of transferring segments of 2 to 5 glucose residues linked by alpha-D-1-4 linkages from maltopentaose, higher molecular weight maltohomologues and starch to maltopentaose and other maltooligosaccharides
-
-
?
maltopentaose + maltopentaose
new oligosaccharides
-
-
-
-
?
maltopentaose + maltopentaose
new oligosaccharides
-
-
-
-
?
maltopentaose + maltopentaose
new oligosaccharides
-
-
-
-
?
maltopentaose + maltopentaose
new oligosaccharides
-
-
-
-
?
maltopentaose + maltotriose
D-glucose + maltooligosaccharides
-
-
-
?
maltopentaose + maltotriose
D-glucose + maltooligosaccharides
-
-
?
maltopentaose + maltotriose
maltodextrins
-
-
-
?
maltopentaose + maltotriose
maltodextrins
-
-
-
?
maltopentaose + maltotriose
maltodextrins
-
-
-
?
maltose + (1,4-alpha-glucan)n+1
D-glucose + (1,4-alpha-glucan)n+1
-
-
-
?
maltose + (1,4-alpha-glucan)n+1
D-glucose + (1,4-alpha-glucan)n+1
-
-
-
?
maltose + beta-cyclodextrin
6-O-alpha-maltosyl-beta-cyclodextrin
-
condensation reaction mechanism, overview
mass spectrometric product identification
-
?
maltose + beta-cyclodextrin
6-O-alpha-maltosyl-beta-cyclodextrin
-
condensation reaction mechanism, overview
mass spectrometric product identification
-
?
maltose + glycosyl acceptor
?
-
lowest activity
-
-
?
maltose + glycosyl acceptor
?
-
lowest activity
-
-
?
maltose + maltose
maltooligosaccharides
-
-
-
-
?
maltose + maltose
maltooligosaccharides
-
-
-
?
maltose + maltose
maltotriose + glucose
-
-
-
-
?
maltose + maltose
maltotriose + glucose
-
-
-
-
?
maltose + maltose
maltotriose + glucose
-
-
-
-
?
maltose + maltose
maltotriose + glucose
-
D-enzyme
-
-
?
maltose + maltose
maltotriose + glucose
-
D-enzyme
-
-
?
maltose + maltose
maltotriose + glucose
-
-
-
-
?
maltose + maltose
maltotriose + glucose
-
-
-
-
?
maltose + maltose
maltotriose + glucose
-
-
-
-
r
maltose + maltose
maltotriose + glucose
-
-
-
-
?
maltose + maltose
maltotriose + glucose
key role in maltose metabolism
-
-
?
maltose + maltosyl-beta-cyclodextrin
?
-
-
-
-
?
maltose + maltosyl-beta-cyclodextrin
?
-
-
-
-
?
maltosylsucrose
?
-
-
-
-
?
maltosylsucrose
?
-
-
-
-
?
maltosylsucrose
?
-
-
-
-
?
maltotetraitol
maltopentaitol + ?
-
-
-
-
?
maltotetraitol
maltopentaitol + ?
-
-
-
-
?
maltotetraitol
maltopentaitol + ?
-
-
-
-
?
maltotetraose + glycosyl acceptor
maltose + D-glucose + maltooligosaccharides
-
second best substrate
-
-
?
maltotetraose + glycosyl acceptor
maltose + D-glucose + maltooligosaccharides
-
second best substrate
-
-
?
maltotetraose + maltopentaose
maltooligosaccharides
-
-
-
?
maltotetraose + maltopentaose
maltooligosaccharides
-
-
-
?
maltotetraose + maltopentaose
maltooligosaccharides
-
-
-
?
maltotetraose + maltopentaose
maltooligosaccharides
-
-
?
maltotetraose + maltopentaose
maltooligosaccharides
-
-
-
?
maltotetraose + maltopentaose
maltooligosaccharides
-
-
-
?
maltotetraose + maltopentaose
maltooligosaccharides
-
-
-
?
maltotetraose + maltotetraose
D-glucose + maltooligosaccharides
-
-
-
-
?
maltotetraose + maltotetraose
D-glucose + maltooligosaccharides
-
-
-
-
?
maltotetraose + maltotetraose
maltooligosaccharides
-
-
-
-
?
maltotetraose + maltotetraose
maltooligosaccharides
-
-
-
-
?
maltotetraose + maltotetraose
maltooligosaccharides
-
-
-
-
?
maltotetraose + maltotriose
D-glucose + maltooligosaccharides
-
amylomaltose, most active with maltotetraose
-
?
maltotetraose + maltotriose
D-glucose + maltooligosaccharides
-
-
-
?
maltotetraose + maltotriose
D-glucose + maltooligosaccharides
-
-
-
?
maltotetraose + maltotriose
D-glucose + maltooligosaccharides
-
-
?
maltotetraose + maltotriose
maltodextrins
-
-
-
?
maltotetraose + maltotriose
maltodextrins
-
-
-
?
maltotetraose + maltotriose
maltodextrins
-
-
-
?
maltotetraose + maltotriose
maltodextrins
-
-
-
?
maltotetraose + maltotriose
maltodextrins
-
-
?
maltotheptaose + maltotriose
maltodextrins
-
-
-
-
?
maltotheptaose + maltotriose
maltodextrins
-
-
-
-
?
maltotheptaose + maltotriose
maltodextrins
-
-
-
-
?
maltotheptaose + maltotriose
maltodextrins
-
-
-
-
?
maltotriose
maltooligosaccharides
-
-
-
-
?
maltotriose
maltooligosaccharides
-
-
-
?
maltotriose + glycosyl acceptor
D-glucose + maltooligosaccharides
efficient transglycosylation activity
-
-
?
maltotriose + glycosyl acceptor
D-glucose + maltooligosaccharides
-
-
-
-
?
maltotriose + glycosyl acceptor
maltose + D-glucose + maltooligosaccharides
-
best substrate
-
-
?
maltotriose + glycosyl acceptor
maltose + D-glucose + maltooligosaccharides
the wild type enzyme prefers maltotriose for disproportionation reaction
-
-
?
maltotriose + glycosyl acceptor
maltose + D-glucose + maltooligosaccharides
-
best substrate
-
-
?
maltotriose + glycosyl acceptor
maltose + D-glucose + maltooligosaccharides
the wild type enzyme prefers maltotriose for disproportionation reaction
-
-
?
maltotriose + maltodextrin
maltopentaose + ?
-
amylomaltase
-
?
maltotriose + maltodextrin
maltopentaose + ?
-
amylomaltase
-
?
maltotriose + maltodextrin
maltose + higher dextrins
-
-
-
?
maltotriose + maltodextrin
maltose + higher dextrins
-
-
-
?
maltotriose + maltotriose
D-glucose + maltooligosaccharides
-
-
-
?
maltotriose + maltotriose
D-glucose + maltooligosaccharides
-
-
-
?
maltotriose + maltotriose
D-glucose + maltooligosaccharides
-
-
-
?
maltotriose + maltotriose
maltodextrins
-
-
-
?
maltotriose + maltotriose
maltodextrins
-
-
-
?
maltotriose + maltotriose
maltodextrins
-
-
-
?
maltotriose + maltotriose
maltodextrins
-
-
-
?
maltotriose + maltotriose
maltodextrins
-
Mtase
-
?
maltotriose + maltotriose
maltooligosaccharides
-
-
-
-
?
maltotriose + maltotriose
maltooligosaccharides
-
-
-
?
maltotriose + maltotriose
maltooligosaccharides
-
-
-
?
maltotriose + maltotriose
maltooligosaccharides
-
most efficient substrate
-
-
?
maltotriose + maltotriose
maltooligosaccharides
-
most efficient substrate
-
-
?
maltotriose + maltotriose
maltooligosaccharides
-
-
-
-
?
maltotriose + maltotriose
maltopentaose + D-glucose
-
-
-
?
maltotriose + maltotriose
maltopentaose + D-glucose
-
-
-
?
maltotriose + maltotriose
maltopentaose + D-glucose
-
-
-
?
maltotriose + maltotriose
maltopentaose + D-glucose
-
-
-
?
maltotriose + maltotriose
maltopentaose + D-glucose
-
D-enzyme
-
?
maltotriose + maltotriose
maltopentaose + maltotetraose
-
-
-
?
maltotriose + maltotriose
maltopentaose + maltotetraose
-
-
-
?
maltotriose + maltotriose
maltopentaose + maltotetraose
-
-
-
?
pea starch + glycosyl acceptor
large-ring cyclodextrins
-
-
-
-
?
pea starch + glycosyl acceptor
large-ring cyclodextrins
-
-
-
?
pea starch + glycosyl acceptor
large-ring cyclodextrins
-
-
-
-
?
pea starch + glycosyl acceptor
large-ring cyclodextrins
-
-
-
?
potato amylose + glycosyl acceptor
cycloamylose
-
the enzyme can produce cycloamyloses in the range 1650 glucose residues
-
?
potato amylose + glycosyl acceptor
cycloamylose
-
-
the enzyme can produce cycloamyloses in the range 16 to more than 60 glucose residues
-
?
potato starch + maltose
large-ring cyclodextrins
-
-
-
-
?
potato starch + maltose
large-ring cyclodextrins
-
-
-
-
?
rice starch + glycosyl acceptor
large-ring cyclodextrins
-
-
-
-
?
rice starch + glycosyl acceptor
large-ring cyclodextrins
-
-
-
-
?
starch
?
incubation of the enzyme with starch or its constituents, i.e. amylose and amylopectin, leads to the formation of a set of multiples of maltose (i.e. maltose, maltotetraose, maltohexaose etc.)
-
-
?
starch
?
incubation of the enzyme with starch or its constituents, i.e. amylose and amylopectin, leads to the formation of a set of multiples of maltose (i.e. maltose, maltotetraose, maltohexaose etc.)
-
-
?
starch + 2-deoxy-D-glucose
?
-
-
-
-
?
starch + 2-deoxy-D-glucose
?
-
-
-
-
?
starch + 2-deoxy-D-glucose
?
-
-
-
-
?
starch + D-glucose
low molecular mass oligosaccharides
-
-
-
?
starch + D-glucose
low molecular mass oligosaccharides
-
-
?
starch + D-glucose
low molecular mass oligosaccharides
-
soluble starch
-
?
starch + D-glucose
oligosaccharides
-
-
-
?
starch + D-glucose
oligosaccharides
-
-
-
?
starch + D-glucose
oligosaccharides
-
-
-
?
starch + glucose
maltotriose + ?
-
-
-
?
starch + glucose
maltotriose + ?
-
-
-
?
starch + glucose
maltotriose + ?
-
-
-
?
starch + glucose
maltotriose + ?
-
-
-
?
starch + maltopentaose
alpha-1,4-D-glucans
-
-
-
?
starch + maltopentaose
alpha-1,4-D-glucans
-
-
-
?
starch + maltopentaose
alpha-1,4-D-glucans
-
-
?
starch + maltopentaose
alpha-1,4-D-glucans
-
starch can serve as acceptor molecule in glycosyl transfer reactions
-
?
starch + maltopentaose
alpha-1,4-D-glucans
-
starch can serve as acceptor molecule in glycosyl transfer reactions
-
?
starch + maltopentaose
alpha-1,4-D-glucans
-
-
-
?
starch + methyl-alpha-D-glucoside
?
-
-
-
-
?
starch + methyl-alpha-D-glucoside
?
-
-
-
-
?
starch + methyl-alpha-D-glucoside
?
-
-
-
-
?
additional information
?
-
-
the smallest acceptor is glucose, the smallest donor is maltose
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
2 major forms, D1 and D2
-
-
?
additional information
?
-
-
glucose is the major product of the D-enzyme reaction
-
-
?
additional information
?
-
-
glucose is the major product of the D-enzyme reaction
-
-
?
additional information
?
-
-
amylopectin is no substrate, maltose is not a product
-
-
?
additional information
?
-
-
amylomaltase is involved in the conversion of maltose to sucrose in the cytosol
-
-
?
additional information
?
-
4-alpha-glucanotransferase is essential for maltose metabolism in photosynthetic leaves
-
-
?
additional information
?
-
DPE2 transfers the non-reducing glucosyl unit from maltose to glycogen by a ping-pong mechanism. The forward reaction, i.e. consumption of maltose, is specific for the beta-anomer of maltose, while the reverse reaction, i.e. production of maltose, is not stereospecific for the acceptor glucose
-
-
?
additional information
?
-
-
both isozymes AgtA and AgtB show transglycosylation activity on donor substrates with alpha-(1,4)-glycosidic bonds and at least five anhydroglucose units forming alpha-(1,4)-glycosidic bonds. Their reaction products reach a degree of polymerization of at least 30. Maltose and larger maltooligosaccharides are the most efficient acceptor substrates, although AgtA also uses small nigerooligosaccharides containing alpha-(1,3)-glycosidic bonds as acceptor substrate, reaction products, overview. The enzyme also shows hydrolyzing activity with potato starch
-
-
?
additional information
?
-
-
glucose, maltose, maltotriose and maltotetraose are not acceptor molecules
-
-
?
additional information
?
-
-
does not use maltose, maltotriose or maltotetraose as acceptor substrates in maltodextrinyltransfer reactions
-
-
?
additional information
?
-
MalQ is able to hydrolyse malto-oligosaccharides as well as to form their longer transglycosylation products and shows activity towards glucose, G1, and a series of malto-oligosaccharides, G2-G7, i.e. maltose, maltotriose, maltotetraose, maltopentaose, maltohexaose and maltoheptaose
-
-
?
additional information
?
-
-
MalQ is able to hydrolyse malto-oligosaccharides as well as to form their longer transglycosylation products and shows activity towards glucose, G1, and a series of malto-oligosaccharides, G2-G7, i.e. maltose, maltotriose, maltotetraose, maltopentaose, maltohexaose and maltoheptaose
-
-
?
additional information
?
-
-
maltose is not a product
-
-
?
additional information
?
-
-
glucose, maltose and maltotriose can act as acceptor, only maltotriose can act as donor
-
-
?
additional information
?
-
-
glucose, maltose and maltotriose can act as acceptor, only maltotriose can act as donor
-
-
?
additional information
?
-
the enzyme displays weak hydrolytic activity against sucrose and alpha-aryl glucoside and fails to act on trehalose and isomaltose
-
-
-
additional information
?
-
-
the enzyme displays weak hydrolytic activity against sucrose and alpha-aryl glucoside and fails to act on trehalose and isomaltose
-
-
-
additional information
?
-
-
glucose is the major product of the D-enzyme reaction
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
acts in concert with EC 2.4.1.1
-
-
?
additional information
?
-
-
acts in concert with EC 2.4.1.1
-
-
?
additional information
?
-
-
strain ML308, D-glucose, D-mannose, methyl-alpha-D-glucoside, phenyl-alpha-D-glucoside, methyl-alpha-D-mannoside and cellobiose have no activity as acceptors
-
-
?
additional information
?
-
-
maltose is inable to serve as a donor substrate, serving only as an acceptor substrate
-
-
?
additional information
?
-
-
D-galactose, sugar alcohols such as sorbitol and xylitol and glycerol are not effective as acceptors
-
-
?
additional information
?
-
-
does not act on maltitol, maltotriitol, glucosylsucrose, isomaltose, panose, isopanose or isomaltosylmaltose, enzyme does not catalyze hydrolytic action on maltotetraitol, maltopentaitol or maltosylsucrose, sorbitol and maltitol are not produced
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-
?
additional information
?
-
-
maltose is inable to serve as a donor substrate, serving only as an acceptor substrate
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
does not act on maltitol, maltotriitol, glucosylsucrose, isomaltose, panose, isopanose or isomaltosylmaltose, enzyme does not catalyze hydrolytic action on maltotetraitol, maltopentaitol or maltosylsucrose, sorbitol and maltitol are not produced
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-
?
additional information
?
-
-
strain ML308, D-glucose, D-mannose, methyl-alpha-D-glucoside, phenyl-alpha-D-glucoside, methyl-alpha-D-mannoside and cellobiose have no activity as acceptors
-
-
?
additional information
?
-
-
D-galactose, sugar alcohols such as sorbitol and xylitol and glycerol are not effective as acceptors
-
-
?
additional information
?
-
-
does not act on maltitol, maltotriitol, glucosylsucrose, isomaltose, panose, isopanose or isomaltosylmaltose, enzyme does not catalyze hydrolytic action on maltotetraitol, maltopentaitol or maltosylsucrose, sorbitol and maltitol are not produced
-
-
?
additional information
?
-
-
strain ML308, D-glucose, D-mannose, methyl-alpha-D-glucoside, phenyl-alpha-D-glucoside, methyl-alpha-D-mannoside and cellobiose have no activity as acceptors
-
-
?
additional information
?
-
-
D-galactose, sugar alcohols such as sorbitol and xylitol and glycerol are not effective as acceptors
-
-
?
additional information
?
-
-
does not act on 6-O-alpha-maltosyl cyclomaltoheptaose
-
-
?
additional information
?
-
-
2 different enzyme activities, oligo-1,4-1,4-glucan-4-glycosyltransferase EC 2.4.1.25 and amylo-1,6-glucosidase EC 3.2.1.33 reside on the same polypeptide chain
-
-
?
additional information
?
-
-
2 different enzyme activities, oligo-1,4-1,4-glucan-4-glycosyltransferase EC 2.4.1.25 and amylo-1,6-glucosidase EC 3.2.1.33 reside on the same polypeptide chain
-
-
?
additional information
?
-
-
glucose is the major product of the D-enzyme reaction
-
-
?
additional information
?
-
-
major pathway for starch degradation in chloroplasts
-
-
?
additional information
?
-
-
cannot use maltose or cyclohexaamylose as a substrate
-
-
?
additional information
?
-
-
D-enzyme, maltohexaose is no initial substrate
-
-
?
additional information
?
-
-
2 glycosyltransferases, amylomaltase and D-enzyme
-
-
?
additional information
?
-
-
D-enzyme, maltohexaose is no initial substrate
-
-
?
additional information
?
-
-
2 glycosyltransferases, amylomaltase and D-enzyme
-
-
?
additional information
?
-
-
acting on gelatinized food-grade potato starch, PyAMase produced a thermoreversible starch product with gelatin-like properties
-
-
?
additional information
?
-
-
acting on gelatinized food-grade potato starch, PyAMase produced a thermoreversible starch product with gelatin-like properties
-
-
?
additional information
?
-
-
the enzyme is involved in glycogen metabolism by selective cleavage of the outer side chain
-
-
?
additional information
?
-
-
synthesis of di-O-alpha-maltosyl-beta-cyclodextrin from 6-O-alpha-maltosyl-beta-cyclodextrin via a transglycosylation reaction, TreX transfers the maltosyl residue of a G2-beta-cyclodextrin to another molecule of G2-beta-cyclodextrin by forming an alpha-1,6-glucosidic linkage. TreX shows specificity for a branched glucosyl chain bigger than DP2 and no activity toward glucosyl-beta-cyclodextrin, transglycosylation reaction mechanism, overview
-
-
?
additional information
?
-
-
the enzyme exhibits hydrolyzing activity toward alpha-1,6-glycosidic linkages of amylopectin, glycogen, pullulan, and other branched substrates, glycogen is the preferred substrate, TreX shows high specificity for hydrolysis of maltohexaosyl alpha-1,6-beta-cyclodextrin, and high activity in 4-alpha-sulfoxide-glucantransferase activity transferring alpha-1,4-glucan oligosaccharides from one chain to another. The enzyme tetramer shows a 4fold higher catalytic activity than the dimer. The enzyme catalyzes intramolecular transglycosylation of maltooligosacchrides, i.e. disproportionation to produce linear alpha-1,4-glucans, as well as intramolecular transglycosylation of glycogen
-
-
?
additional information
?
-
TreX from Sulfolobus solfataricus shows dual activities for alpha-1,4-transferase, EC 2.4.1.25 and alpha-1,6-glucosidase, EC 3.2.1.68, bifunctional mechanism, substrate maltotriose, overview. TreX exhibits two different active-site configurations depending on its oligomeric state
-
-
?
additional information
?
-
-
TreX from Sulfolobus solfataricus shows dual activities for alpha-1,4-transferase, EC 2.4.1.25 and alpha-1,6-glucosidase, EC 3.2.1.68, bifunctional mechanism, substrate maltotriose, overview. TreX exhibits two different active-site configurations depending on its oligomeric state
-
-
?
additional information
?
-
-
synthesis of di-O-alpha-maltosyl-beta-cyclodextrin from 6-O-alpha-maltosyl-beta-cyclodextrin via a transglycosylation reaction, TreX transfers the maltosyl residue of a G2-beta-cyclodextrin to another molecule of G2-beta-cyclodextrin by forming an alpha-1,6-glucosidic linkage. TreX shows specificity for a branched glucosyl chain bigger than DP2 and no activity toward glucosyl-beta-cyclodextrin, transglycosylation reaction mechanism, overview
-
-
?
additional information
?
-
-
the enzyme is involved in glycogen metabolism by selective cleavage of the outer side chain
-
-
?
additional information
?
-
-
the enzyme exhibits hydrolyzing activity toward alpha-1,6-glycosidic linkages of amylopectin, glycogen, pullulan, and other branched substrates, glycogen is the preferred substrate, TreX shows high specificity for hydrolysis of maltohexaosyl alpha-1,6-beta-cyclodextrin, and high activity in 4-alpha-sulfoxide-glucantransferase activity transferring alpha-1,4-glucan oligosaccharides from one chain to another. The enzyme tetramer shows a 4fold higher catalytic activity than the dimer. The enzyme catalyzes intramolecular transglycosylation of maltooligosacchrides, i.e. disproportionation to produce linear alpha-1,4-glucans, as well as intramolecular transglycosylation of glycogen
-
-
?
additional information
?
-
-
appears to be exclusively oligo-1,4-1,4-glucantransferase-amylo 1,6-glucosidase and does not have isoamylase
-
-
?
additional information
?
-
-
does not act on 6-O-alpha-maltosyl cyclomaltoheptaose
-
-
?
additional information
?
-
-
2 different enzyme activities, oligo-1,4-1,4-glucan-4-glycosyltransferase EC 2.4.1.25 and amylo-1,6-glucosidase EC 3.2.1.33 reside on the same polypeptide chain
-
-
?
additional information
?
-
-
glucose is the major product of the D-enzyme reaction
-
-
?
additional information
?
-
-
maltose is not a donor substrate, only weak acceptor activity
-
-
?
additional information
?
-
-
glucose is the major product of the D-enzyme reaction
-
-
?
additional information
?
-
glucose is the major product of the D-enzyme reaction
-
-
?
additional information
?
-
-
D-glucosamine, N-acetyl-D-glucosamine and isomaltose have no activity as acceptors
-
-
?
additional information
?
-
-
maltose is not a product
-
-
?
additional information
?
-
-
maltose is not a product
-
-
?
additional information
?
-
maltose is not a product
-
-
?
additional information
?
-
-
maltose is not a product
-
-
?
additional information
?
-
maltose is no substrate
-
-
?
additional information
?
-
-
maltose is no substrate
-
-
?
additional information
?
-
-
glucose is the major product of the D-enzyme reaction
-
-
?
additional information
?
-
-
acts in concert with EC 2.4.1.1
-
-
?
additional information
?
-
acts in concert with EC 2.4.1.1
-
-
?
additional information
?
-
-
Glcalpha1-4Glcalpha1-4Glcalpha1-4Glcalpha1-4Glcalpha1-4(Glcalpha1-4Glcalpha1-4 Glcalpha1-4Glcalpha1-6)Glcalpha1-4Glcalpha1-4Glc-maltose, Glcalpha1-4Glcalpha1-4 Glcalpha1-4Glcalpha1-4(Glcalpha1-4Glcalpha1-4Glcalpha1-4Glcalpha1-6)Glcalpha1-4 Glcalpha1-4Glcalpha1-4Glc-maltose or Glcalpha1-4Glcalpha1-4Glcalpha1-4(Glcalpha1-4 Glcalpha1-4Glcalpha1-4Glcalpha1-6)Glcalpha1-4Glcalpha1-4Glcalpha1-4Glcalpha1-4Glc-maltose are suitable fluorogenic substrates for assaying debranching enzyme
-
-
?
additional information
?
-
-
the enzyme liberates maltose oligomers from branched dextrins in presence or absence of acceptor maltohexaose, 6_4-O-alpha-glucosyl-pyridylamino-maltooctaose is liberated from 64-O-alpha-maltopentaosyl-pyridylamino-maltooctaose, 64-O-alpha-maltotetraosyl-pyridylamino-maltooctaose and 64-O-alpha-maltotriosyl-pyridylamino-maltooctaose, whereas 64-O-alpha-maltosyl-pyridylamino-maltooctaose is resistant to the enzyme, donor substrate specificity of GDE, GDE 4-alpha-glucanotransferase removes a maltotriosyl residue from the maltotetraosyl branch in a way that the alpha-1,6-linked glucosyl residue is retained, overview
-
-
?
additional information
?
-
-
glucose is the major product of the D-enzyme reaction
-
-
?
additional information
?
-
-
the enzyme displays transglycosylating activity on various maltooligosaccharides, e.g. corn starches consisting of different proportions of amylopectin and amylose, of which the smallest donor and acceptor molecules are determined to be maltose and glucose, respectively, overview. Activity of alphaGTase decreases amylopectin and increases cycloamylose contents in the polymers, product determination by MALDI-TOF-MS analysis, product molecular weight and branch-chain distribution after isoamylolysis of different starches, overview
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
enzyme catalyzes not only intermolecular transglycosylation to produce linear alpha-1,4-glucan, but also intramolecular transglycosylation to produce cyclic alpha-1,4-glucan
-
-
?
additional information
?
-
-
2 different 4-alpha-glucanotransferases, MTAse and Gtase
-
-
?
additional information
?
-
-
unable to use maltotriose as donor sugar or glucose as acceptor sugar
-
-
?
additional information
?
-
-
Gtase, glucose does not function as acceptor sugar, nor does it appear as reaction product
-
-
?
additional information
?
-
-
maltose and maltotriose are not disproportionated, glucose does not function as an acceptor sugar in transfer reactions, glucose also never appears as a reaction product
-
-
?
additional information
?
-
-
alpha-D-glucose, beta-D-fructose, D-ribose, D-arabinose, D-xylose, isomaltose, D-trehalose, D-cellobiose, lactose, sucrose, raffinose and N-acetyl-D-glucosamine cannot participate as acceptor sugars in glucanosyl transfer from amylose
-
-
?
additional information
?
-
-
polysaccharides, such as soluble starch, amylose and amylopectin, and maltooligosaccharides longer than maltose can be effective maltosyl group donors for the enzyme. All maltooligosaccharides are able to act as acceptor molecules in 4-alpha-glucanotransferase-mediated transfer of glucan segments from amylose
-
-
?
additional information
?
-
modification of granular corn starch with 4-alpha-glucanotransferase from Thermotoga maritima without induction of gelatinization, analysis of the morphology of the modified starches with light and scanning electron microscopy, the granule integrity is mostly maintained after enzyme treatment, although some granules are partially fragmented, amylose and amylopectin levels can be altered, solubility and paste clarity of themodified starches are much higher than those of raw starch, and it shows thermoreversibility between 4 and 75°C, X-ray diffraction and relative crystallinity, overview
-
-
?
additional information
?
-
-
modification of granular corn starch with 4-alpha-glucanotransferase from Thermotoga maritima without induction of gelatinization, analysis of the morphology of the modified starches with light and scanning electron microscopy, the granule integrity is mostly maintained after enzyme treatment, although some granules are partially fragmented, amylose and amylopectin levels can be altered, solubility and paste clarity of themodified starches are much higher than those of raw starch, and it shows thermoreversibility between 4 and 75°C, X-ray diffraction and relative crystallinity, overview
-
-
?
additional information
?
-
4-nitrophenyl-alpha-D-glucopyranoside, 4-nitrophenyl-alpha-D-maltotrioside, 4-methylumbelliferyl-alpha-D-glucopyranoside, and 5-bromo-4-chloro-3-indolyl-alpha-D-glucopyranoside are acceptors for GTase
-
-
?
additional information
?
-
GTase displays a broad transfer specificity
-
-
?
additional information
?
-
GTase displays a broad transfer specificity
-
-
?
additional information
?
-
the enzyme catalyses the transfer of maltosyl units from alpha-1,4-linked glucans or malto-oligosaccharides to other alpha-1,4-linked glucans, maltooligosaccharides or glucose
-
-
?
additional information
?
-
the enzyme catalyses the transfer of maltosyl units from alpha-1,4-linked glucans or malto-oligosaccharides to other alpha-1,4-linked glucans, maltooligosaccharides or glucose
-
-
?
additional information
?
-
the enzyme is highly specialised on the transfer of maltosyl residues from aalpha-1,4-linked glucans or malto-oligosaccharides to other alpha-1,4-linked glucans, malto-oligosaccharides, or glucose
-
-
?
additional information
?
-
-
the enzyme is highly specialised on the transfer of maltosyl residues from aalpha-1,4-linked glucans or malto-oligosaccharides to other alpha-1,4-linked glucans, malto-oligosaccharides, or glucose
-
-
?
additional information
?
-
the enzyme catalyses the transfer of maltosyl units from alpha-1,4-linked glucans or malto-oligosaccharides to other alpha-1,4-linked glucans, maltooligosaccharides or glucose
-
-
?
additional information
?
-
the enzyme catalyses the transfer of maltosyl units from alpha-1,4-linked glucans or malto-oligosaccharides to other alpha-1,4-linked glucans, maltooligosaccharides or glucose
-
-
?
additional information
?
-
the enzyme is highly specialised on the transfer of maltosyl residues from aalpha-1,4-linked glucans or malto-oligosaccharides to other alpha-1,4-linked glucans, malto-oligosaccharides, or glucose
-
-
?
additional information
?
-
4-nitrophenyl-alpha-D-glucopyranoside, 4-nitrophenyl-alpha-D-maltotrioside, 4-methylumbelliferyl-alpha-D-glucopyranoside, and 5-bromo-4-chloro-3-indolyl-alpha-D-glucopyranoside are acceptors for GTase
-
-
?
additional information
?
-
GTase displays a broad transfer specificity
-
-
?
additional information
?
-
GTase displays a broad transfer specificity
-
-
?
additional information
?
-
-
maltose and maltotriose are not disproportionated, glucose does not function as an acceptor sugar in transfer reactions, glucose also never appears as a reaction product
-
-
?
additional information
?
-
-
alpha-D-glucose, beta-D-fructose, D-ribose, D-arabinose, D-xylose, isomaltose, D-trehalose, D-cellobiose, lactose, sucrose, raffinose and N-acetyl-D-glucosamine cannot participate as acceptor sugars in glucanosyl transfer from amylose
-
-
?
additional information
?
-
-
TAalphaGT catalyzes the transfer of glucose units from one 1,4-alpha-glucan to another and requires at least maltose units for the disproportionation reaction
-
-
?
additional information
?
-
B7A9X4
amylomaltase from Thermus aquaticus catalyzes three types of transglycosylation reaction, as well as a weak hydrolytic reaction of alpha-1,4 glucan
-
-
?
additional information
?
-
-
amylomaltase from Thermus aquaticus catalyzes three types of transglycosylation reaction, as well as a weak hydrolytic reaction of alpha-1,4 glucan
-
-
?
additional information
?
-
B7A9X4
the enzyme contains two substrate binding sites involving residues Y54 or Y101, structure and localization, overview. The binding of glucan substrate to the second glucan binding site through an interaction with the aromatic side chains of Y54 and Y101 is a trigger for the enzyme to take a completely active conformation for all four types of activity, but prevents the cyclization reaction to occur since the flexibility of the glucan is restricted by such binding. Synthesis of cycloamylose, overview
-
-
?
additional information
?
-
-
the enzyme contains two substrate binding sites involving residues Y54 or Y101, structure and localization, overview. The binding of glucan substrate to the second glucan binding site through an interaction with the aromatic side chains of Y54 and Y101 is a trigger for the enzyme to take a completely active conformation for all four types of activity, but prevents the cyclization reaction to occur since the flexibility of the glucan is restricted by such binding. Synthesis of cycloamylose, overview
-
-
?
additional information
?
-
-
modification of rice starch by the enzyme
-
-
?
additional information
?
-
-
the enzyme catalyzes an inter-molecular transglycosylation, by transfer of alpha glucan moiety from one alpha-1,4-glucan molecule to another or to glucose, forming two linear products of different sizes
-
-
?
additional information
?
-
-
the enzyme modifies corn starch with different amylose contents leading to a broader chain-length distribution of the of isoamylolytically debranched products, formation of a variety of cycloamyloses with different sizes, MALDI-TOF-MS analysis of cycloamyloses, overview
-
-
?
additional information
?
-
-
TAalphaGT catalyzes the transfer of glucose units from one 1,4-alpha-glucan to another and requires at least maltose units for the disproportionation reaction
-
-
?
additional information
?
-
-
the enzyme reacts with small oligosaccharides, especially maltotriose, to form various maltooligosaccharides by using its disproportionating activity
-
-
?
additional information
?
-
-
rice cake production using a thermostable 4-alpha-glucanotransferase from Thermus scotoductus, starch molecular fine structure, texture, and retrogradation, the number of shorter side chains increases, whereas the number of longer side chains decreases through the disproportionation reaction of TSalphaGTase, amylose and malto-oligosaccharide contents are altered, molecular weight of rice starch, overview
-
-
?
additional information
?
-
-
the enzyme acts on rice starch and amylopectin, the alpha-1,4 glucosidic linkage of the segment between amylopectin clusters is hydrolyzed with a rearrangement in the side-chain length distribution, the highly branched amylopectin cluster, HBAPC, and highly branched amylose, HBA contain significant numbers of branched maltooligosaccharide side chains, HBAPC and HBA show higher water solubility and stability against retrogradation than amylopectin clusters or branched amylose, overview
-
-
?
additional information
?
-
-
the enzyme acts on rice starch and modulates the starch concerning concentration, flow behavior, gel strength, and melting and gelling kinetics. As the level of enzyme decreases and the starch concentration increases, gelation time decreases and the final gel strength increased significantly. Regardless of treatment variables, all the modified starch gels melt at similar temperature, dynamic rheological behavior of enzyme-treated rice starch paste, overview
-
-
?
additional information
?
-
-
glucose can only be used as acceptor of maltosyl units
-
-
?
additional information
?
-
amylomaltases are capable of the synthesis of large cyclic glucans and the disproportionation of oligosaccharides
-
-
?
additional information
?
-
Thermus thermophilus AMase is among the most efficient 4-alpha-glucanotransferases in the alpha-amylase superfamily
-
-
?
additional information
?
-
glucose transfer/production using maltose and glycogen. Wild-type DPE2 can bind to starch and glycogen has very little, if any, ability to dissociate DPE2 from the starch pellet
-
-
?
additional information
?
-
substrates are maltooligomers, trimer to heptamer, substrate binding mechanism and structure, modeling. The active site contains at least seven substrate binding sites, subsites -2 and +3 favoring substrate binding and subsites -3 and +2 do not, substrate specificity, overview
-
-
?
additional information
?
-
-
preparation of gels from starches of various botanical origin, e.g. potato, high amylose potato, maize, waxy maize, wheat and pea starches, by modification through the enzyme from Thermus thermophilus, thermodynamics and product properties, overview
-
-
?
additional information
?
-
Thermus thermophilus AMase is among the most efficient 4-alpha-glucanotransferases in the alpha-amylase superfamily
-
-
?
additional information
?
-
substrates are maltooligomers, trimer to heptamer, substrate binding mechanism and structure, modeling. The active site contains at least seven substrate binding sites, subsites -2 and +3 favoring substrate binding and subsites -3 and +2 do not, substrate specificity, overview
-
-
?
additional information
?
-
-
glucose is the major product of the D-enzyme reaction
-
-
?
additional information
?
-
-
cannot use maltose or cyclohexaamylose as a substrate
-
-
?
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A406L
-
the mutant shows higher thermostability at 35-40°C, higher intermolecular transglucosylation activity with an upward shift in the optimum temperature and a slight increase in the optimum pH for disproportionation and cyclization reactions compared to the wild type enzyme. The mutant shows higher specific activities for starch transglucosylation (2.1fold) and disproportionation (1.4fold) than those of the wild type
A406V
-
the mutant shows higher thermostability at 50°C, higher intermolecular transglucosylation activity with an upward shift in the optimum temperature and a slight increase in the optimum pH for disproportionation and cyclization reactions compared to the wild type enzyme. The mutant shows higher specific activities for starch transglucosylation (2.8fold) and disproportionation (2.1fold) than those of the wild type
H461A
the mutation leads to a significant (8.6fold) decrease in transglucosylation activity compared to the wild type enzyme, while hydrolysis activity is barely affected. The mutant cannot produce large-ring cyclodextrins from maltotriose and prefers maltose over maltotriose as substrate
H461D
the mutation leads to a significant (3.4fold) decrease in transglucosylation activity compared to the wild type enzyme, while hydrolysis activity is barely affected. The mutant cannot produce large-ring cyclodextrins from maltotriose and prefers maltose over maltotriose as substrate
H461R
the mutation leads to a significant (6fold) decrease in transglucosylation activity compared to the wild type enzyme, while hydrolysis activity is barely affected. The mutant cannot produce large-ring cyclodextrins from maltotriose and prefers maltose over maltotriose as substrate
H461S
the mutation leads to a significant (3.4fold) decrease in transglucosylation activity compared to the wild type enzyme, while hydrolysis activity is barely affected. The mutant cannot produce large-ring cyclodextrins from maltotriose and prefers maltose over maltotriose as substrate
H461W
the mutation leads to a significant (6fold) decrease in transglucosylation activity compared to the wild type enzyme, while hydrolysis activity is barely affected. The mutant cannot produce large-ring cyclodextrins from maltotriose and prefers maltose over maltotriose as substrate
N287Y
-
the mutant shows a significant decrease in all transglucosylation activities including starch transglucosylation, disproportionation, cyclization and coupling compared to the wild type enzyme, while hydrolysis activity is not changed. The mutant shows an increase in thermostability and substrate preference for maltoheptaose in addition to maltotriose
Y172A
-
mutant exhibits lower disproportionation, cyclization, and hydrolysis activities than the wild-type. The kcat/Km of the disproportionation reaction for the Y172A enzyme is 2.8fold lower than that of wild-type. The Y172A enzyme shows a product pattern different from that of wild-type at a long incubation time. The principal large-ring cyclodextrin products of the Y172A mutant are a cycloamylose mixture with a degree of polymerization of 28 or 29
Y418A
-
the mutant shows a significant decrease in starch transglucosylation, disproportionation and cyclization activities compared to the wild type enzyme. The mutant produces large ring-cyclodextrins 36-40 from pea starch
Y418D
-
the mutant shows a significant decrease in starch transglucosylation, disproportionation and cyclization activities compared to the wild type enzyme. The mutant produces large ring-cyclodextrins 36-40 from pea starch
Y418F
-
the mutant shows a significant decrease in starch transglucosylation, disproportionation and cyclization activities compared to the wild type enzyme. The mutant produces large ring-cyclodextrins 29-33 from pea starch
Y418R
-
the mutant shows a significant decrease in starch transglucosylation, disproportionation and cyclization activities compared to the wild type enzyme. The mutant produces large ring-cyclodextrins 36-40 from pea starch
Y418S
-
the mutant shows a significant decrease in starch transglucosylation, disproportionation and cyclization activities compared to the wild type enzyme. The mutant produces large ring-cyclodextrins 36-40 from pea starch
Y418W
-
the mutant shows a significant decrease in starch transglucosylation, disproportionation and cyclization activities compared to the wild type enzyme. The mutant produces large ring-cyclodextrins 36-40 from pea starch
A406L
-
the mutant shows higher thermostability at 35-40°C, higher intermolecular transglucosylation activity with an upward shift in the optimum temperature and a slight increase in the optimum pH for disproportionation and cyclization reactions compared to the wild type enzyme. The mutant shows higher specific activities for starch transglucosylation (2.1fold) and disproportionation (1.4fold) than those of the wild type
-
A406V
-
the mutant shows higher thermostability at 50°C, higher intermolecular transglucosylation activity with an upward shift in the optimum temperature and a slight increase in the optimum pH for disproportionation and cyclization reactions compared to the wild type enzyme. The mutant shows higher specific activities for starch transglucosylation (2.8fold) and disproportionation (2.1fold) than those of the wild type
-
N287Y
-
the mutant shows a significant decrease in all transglucosylation activities including starch transglucosylation, disproportionation, cyclization and coupling compared to the wild type enzyme, while hydrolysis activity is not changed. The mutant shows an increase in thermostability and substrate preference for maltoheptaose in addition to maltotriose
-
H461A
-
the mutation leads to a significant (8.6fold) decrease in transglucosylation activity compared to the wild type enzyme, while hydrolysis activity is barely affected. The mutant cannot produce large-ring cyclodextrins from maltotriose and prefers maltose over maltotriose as substrate
-
H461D
-
the mutation leads to a significant (3.4fold) decrease in transglucosylation activity compared to the wild type enzyme, while hydrolysis activity is barely affected. The mutant cannot produce large-ring cyclodextrins from maltotriose and prefers maltose over maltotriose as substrate
-
H461R
-
the mutation leads to a significant (6fold) decrease in transglucosylation activity compared to the wild type enzyme, while hydrolysis activity is barely affected. The mutant cannot produce large-ring cyclodextrins from maltotriose and prefers maltose over maltotriose as substrate
-
H461S
-
the mutation leads to a significant (3.4fold) decrease in transglucosylation activity compared to the wild type enzyme, while hydrolysis activity is barely affected. The mutant cannot produce large-ring cyclodextrins from maltotriose and prefers maltose over maltotriose as substrate
-
H461W
-
the mutation leads to a significant (6fold) decrease in transglucosylation activity compared to the wild type enzyme, while hydrolysis activity is barely affected. The mutant cannot produce large-ring cyclodextrins from maltotriose and prefers maltose over maltotriose as substrate
-
W229H
-
kcat/KM value of transglycosylation activity significantly decreases to about 15% of wild-type, kcat/Km value of hydrolysis activity changes little
D214N
the specific activity of the D214N mutant is decreased about 10000fold as compared with that of the wild-type enzyme
E123Q
-
the specific activity of the mutant enzyme toward maltotriose is about 15000fold lower than the specific activity of the wild-type enzyme
E129Q
-
the specific activity of the mutant enzyme is almost the same as that of the wild-type enzyme
D214N
-
the specific activity of the D214N mutant is decreased about 10000fold as compared with that of the wild-type enzyme
-
F251G
mutation results in significantly lower glucose production but increased maltose production from maltopentose substrates, showing an altered substrate-binding affinity
Q256G
mutation results in increased Km for maltotriose and a sharp decrease of the transglycosylation factor for maltose
W258G
mutant shows neither cyclization nor coupling activity, suggesting that residue Trp258 plays an essential role in all catalytic activities including hydrolysis and transglycosylation activities
D293A
site-directed mutagenesis of the active site nucleophile, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme
D293N
site-directed mutagenesis of the active site nucleophile, the D293N mutation reduces the pH stability of the enzyme, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme
D294S
site-directed mutagenesis, the mutant shows highly reduced kcat and reduced activity with malto-oligomers compared to the wild-type enzyme
D395A
site-directed mutagenesis of the active site transition stabilizer, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme
D395N
site-directed mutagenesis of the active site transition stabilizer, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme
E340A
site-directed mutagenesis of the active site general acid/base catalyst, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme
E340Q
site-directed mutagenesis of the active site general acid/base catalyst, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme
E758Q
the mutant shows highly reduced activity compared to the wild-type enzyme
F366L
site-directed mutagenesis, the mutant shows reduced kcat compared and reduced activity with malto-oligomers compared to the wild-type enzyme
D293A
-
site-directed mutagenesis of the active site nucleophile, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme
-
D293N
-
site-directed mutagenesis of the active site nucleophile, the D293N mutation reduces the pH stability of the enzyme, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme
-
D395N
-
site-directed mutagenesis of the active site transition stabilizer, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme
-
E340A
-
site-directed mutagenesis of the active site general acid/base catalyst, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme
-
E340Q
-
site-directed mutagenesis of the active site general acid/base catalyst, the mutant shows reduced activity with malto-oligomers compared to the wild-type enzyme
-
Y54A
-
hydrolytic activity is 39% of the wild-type value, cyclization activity is 192% of the wild-type value
Y54A
B7A9X4
site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme
Y54C
-
hydrolytic activity is 48% of the wild-type value, cyclization activity is 122% of the wild-type value
Y54C
B7A9X4
site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme
Y54D
-
hydrolytic activity is 38% of the wild-type value, cyclization activity is 177% of the wild-type value
Y54D
B7A9X4
site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme
Y54E
-
hydrolytic activity is 48% of the wild-type value, cyclization activity is 157% of the wild-type value
Y54E
B7A9X4
site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme
Y54F
-
hydrolytic activity is 96% of the wild-type value, cyclization activity is 91% of the wild-type value
Y54F
B7A9X4
site-directed mutagenesis, the mutant shows increased coupling and disproportionation activities compared to the wild-type enzyme
Y54G
-
hydrolytic activity is 16% of the wild-type value, cyclization activity is 167% of the wild-type value
Y54G
B7A9X4
site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme
Y54H
-
hydrolytic activity is 76% of the wild-type value, cyclization activity is 164% of the wild-type value
Y54H
B7A9X4
site-directed mutagenesis, the mutant shows increased coupling and reduced disproportionation activities compared to the wild-type enzyme
Y54I
-
hydrolytic activity is 33% of the wild-type value, cyclization activity is 157% of the wild-type value
Y54I
B7A9X4
site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme
Y54K
-
hydrolytic activity is 99% of the wild-type value, cyclization activity is 176% of the wild-type value
Y54K
B7A9X4
site-directed mutagenesis, the mutant shows unaltered coupling but reduced disproportionation activities compared to the wild-type enzyme
Y54L
-
hydrolytic activity is 39% of the wild-type value, cyclization activity is 189% of the wild-type value
Y54L
B7A9X4
site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme
Y54M
-
hydrolytic activity is 39% of the wild-type value, cyclization activity is 81% of the wild-type value
Y54M
B7A9X4
site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme
Y54N
-
hydrolytic activity is 30% of the wild-type value, cyclization activity is 159% of the wild-type value
Y54N
B7A9X4
site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme
Y54P
-
hydrolytic activity is 5% of the wild-type value, cyclization activity is 48% of the wild-type value
Y54P
B7A9X4
site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme
Y54Q
-
hydrolytic activity is 70% of the wild-type value, cyclization activity is 168% of the wild-type value
Y54Q
B7A9X4
site-directed mutagenesis, the mutant shows unaltered coupling but reduced disproportionation activities compared to the wild-type enzyme
Y54R
-
hydrolytic activity is 70% of the wild-type value, cyclization activity is 200% of the wild-type value
Y54R
B7A9X4
site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme
Y54S
-
hydrolytic activity is 38% of the wild-type value, cyclization activity is 186% of the wild-type value
Y54S
B7A9X4
site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme
Y54T
-
hydrolytic activity is 22% of the wild-type value, cyclization activity is 149% of the wild-type value
Y54T
B7A9X4
site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme
Y54V
-
hydrolytic activity is 29% of the wild-type value, cyclization activity is 160% of the wild-type value
Y54V
B7A9X4
site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme
Y54W
-
hydrolytic activity is 20% of the wild-type value, cyclization activity is 95% of the wild-type value
Y54W
B7A9X4
site-directed mutagenesis, the mutant shows reduced coupling and disproportionation activities compared to the wild-type enzyme
additional information
the glycosyl hydrolase domain alone provides disproportionating activity with a much higher affinity for short maltodextrins than the complete wild-type enzyme, while absence of the carbohydrate binding modules completely abolishes activity with large complex carbohydrates, reflecting the presumed function of DPE2 in vivo
additional information
-
an agtA knockout of Aspergillus niger shows an increased susceptibility towards the cell wall-disrupting compound, phenotypic characterization of CFW hypersensitive DELTAagtA strain and AgtA/AgtB overexpression strains, overview
additional information
mutations in the N-terminal region result in a sharp increase in alpha-1,4-transferase activity and a reduced level of alpha-1,6-glucosidase activity, overview
additional information
-
mutations in the N-terminal region result in a sharp increase in alpha-1,4-transferase activity and a reduced level of alpha-1,6-glucosidase activity, overview
additional information
-
the starch-binding domains of Bacillus stearothermophilus ET1 CGTase (E and DE) are introduced into the C-terminus of TAalphaGT to enhance the starch utilizing activity. The chimeric enzymes, TAalphaGT-E and TAalphaGT-DE, show no difference in temperature optimum, transglycosylation activity, and amylolytic degradation pattern compared to TAalphaGT wild-type. However, TAalphaGT-DE exhibits the highest molar specific activity toward amylose. TAalphaGT-DE modifies amylopectin molecules by its disproportionating activities to produce modified amylopectin clusters (MW 1000001000000) and produces cyclo-amyloses with DP of 19 through 35 from amylose molecules
additional information
B7A9X4
the amino acid substitution at Y54 or Y101 for removing their aromatic side chain increases cyclization activity, intra-molecular transglycosylation reaction, but decreases disproportionation, coupling and hydrolytic activities, inter-molecular reactions
additional information
-
the amino acid substitution at Y54 or Y101 for removing their aromatic side chain increases cyclization activity, intra-molecular transglycosylation reaction, but decreases disproportionation, coupling and hydrolytic activities, inter-molecular reactions
additional information
-
the starch-binding domains of Bacillus stearothermophilus ET1 CGTase (E and DE) are introduced into the C-terminus of TAalphaGT to enhance the starch utilizing activity. The chimeric enzymes, TAalphaGT-E and TAalphaGT-DE, show no difference in temperature optimum, transglycosylation activity, and amylolytic degradation pattern compared to TAalphaGT wild-type. However, TAalphaGT-DE exhibits the highest molar specific activity toward amylose. TAalphaGT-DE modifies amylopectin molecules by its disproportionating activities to produce modified amylopectin clusters (MW 1000001000000) and produces cyclo-amyloses with DP of 19 through 35 from amylose molecules
-
additional information
-
enzymatic modification of rice starch to produce highly branched amylopectin and amylose using alpha-glucanotransferase and maltogenic amylase, overview
additional information
the deletion mutant DELTAN130 is unable to use glycogen but has high disproportionating activity with maltodextrins
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-
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-
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-
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