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4-nitrophenyl alpha-isomaltoside + H2O
4-nitrophenol + alpha-isomaltose
alpha-linked gluco-oligosaccharide + H2O
isomaltose + D-glucose
-
-
-
?
dextran + 1-butanol
1-butyl alpha-isomaltoside + H2O
-
-
-
r
dextran + 1-propanol
1-propyl alpha-isomaltoside + H2O
-
-
-
r
dextran + ethanol
ethyl alpha-isomaltoside + H2O
-
-
-
r
dextran + H2O
alpha-isomaltose + O-alpha-D-Glcp-(1-3)-O-alpha-D-Glcp-(1-6)-D-Glc + O-alpha-D-Glcp-(1-4)-O-alpha-D-Glcp-(1-6)-D-Glc + O-alpha-D-Glcp-(1-2)-O-alpha-D-Glcp-(1-6)-D-Glc
dextran + methanol
methyl alpha-isomaltoside + H2O
-
-
-
r
dextran + sucrose
6G-alpha-isomaltosylsucrose + H2O
-
-
-
r
dextran + trehalose
6-alpha-isomaltosyltrehalose + H2O
-
-
-
r
dextran T2000 + H2O
isomaltose + ?
glucooligosaccharides + H2O
isomaltose + D-glucose
isomaltoheptaose + H2O
?
-
-
-
-
?
isomaltohexaose + H2O
?
-
-
-
-
?
isomaltohexatiol + H2O
isomaltose + Isomaltitol
-
-
-
?
isomaltooctaose + H2O
?
-
-
-
-
?
isomaltooligosaccharide + H2O
isomaltose + glucose
isomaltopentaose + H2O
?
-
-
-
-
?
isomaltotetraose + H2O
?
-
-
-
-
?
isomaltotriitol + H2O
isomaltose + sorbitol
isomaltotriose + H2O
alpha-isomaltose + D-glucose
panose + H2O
alpha-isomaltose + D-glucose
panose + H2O
isomaltose + D-glucose
additional information
?
-
4-nitrophenyl alpha-isomaltoside + H2O
4-nitrophenol + alpha-isomaltose
-
-
-
?
4-nitrophenyl alpha-isomaltoside + H2O
4-nitrophenol + alpha-isomaltose
-
-
-
?
dextran + H2O
alpha-isomaltose + O-alpha-D-Glcp-(1-3)-O-alpha-D-Glcp-(1-6)-D-Glc + O-alpha-D-Glcp-(1-4)-O-alpha-D-Glcp-(1-6)-D-Glc + O-alpha-D-Glcp-(1-2)-O-alpha-D-Glcp-(1-6)-D-Glc
-
-
-
?
dextran + H2O
alpha-isomaltose + O-alpha-D-Glcp-(1-3)-O-alpha-D-Glcp-(1-6)-D-Glc + O-alpha-D-Glcp-(1-4)-O-alpha-D-Glcp-(1-6)-D-Glc + O-alpha-D-Glcp-(1-2)-O-alpha-D-Glcp-(1-6)-D-Glc
-
-
-
?
dextran + H2O
alpha-isomaltose + O-alpha-D-Glcp-(1-3)-O-alpha-D-Glcp-(1-6)-D-Glc + O-alpha-D-Glcp-(1-4)-O-alpha-D-Glcp-(1-6)-D-Glc + O-alpha-D-Glcp-(1-2)-O-alpha-D-Glcp-(1-6)-D-Glc
-
-
-
?
dextran + H2O
alpha-isomaltose + O-alpha-D-Glcp-(1-3)-O-alpha-D-Glcp-(1-6)-D-Glc + O-alpha-D-Glcp-(1-4)-O-alpha-D-Glcp-(1-6)-D-Glc + O-alpha-D-Glcp-(1-2)-O-alpha-D-Glcp-(1-6)-D-Glc
-
-
-
?
dextran + H2O
alpha-isomaltose + O-alpha-D-Glcp-(1-3)-O-alpha-D-Glcp-(1-6)-D-Glc + O-alpha-D-Glcp-(1-4)-O-alpha-D-Glcp-(1-6)-D-Glc + O-alpha-D-Glcp-(1-2)-O-alpha-D-Glcp-(1-6)-D-Glc
-
-
-
?
dextran + H2O
alpha-isomaltose + O-alpha-D-Glcp-(1-3)-O-alpha-D-Glcp-(1-6)-D-Glc + O-alpha-D-Glcp-(1-4)-O-alpha-D-Glcp-(1-6)-D-Glc + O-alpha-D-Glcp-(1-2)-O-alpha-D-Glcp-(1-6)-D-Glc
-
-
-
?
dextran + H2O
alpha-isomaltose + O-alpha-D-Glcp-(1-3)-O-alpha-D-Glcp-(1-6)-D-Glc + O-alpha-D-Glcp-(1-4)-O-alpha-D-Glcp-(1-6)-D-Glc + O-alpha-D-Glcp-(1-2)-O-alpha-D-Glcp-(1-6)-D-Glc
-
-
-
-
?
dextran + H2O
alpha-isomaltose + O-alpha-D-Glcp-(1-3)-O-alpha-D-Glcp-(1-6)-D-Glc + O-alpha-D-Glcp-(1-4)-O-alpha-D-Glcp-(1-6)-D-Glc + O-alpha-D-Glcp-(1-2)-O-alpha-D-Glcp-(1-6)-D-Glc
-
enzyme hydrolyzes alpha-1,6-glucosidic linkages of dextran or isomalto-oligosaccharides to release exolytically alpha-isomaltose from the non-reducing ends
-
-
?
dextran T2000 + H2O
isomaltose + ?
the enzyme liberates isomaltose from the non-reducing end of a polymer of dextran. It does not show alpha-N-galactosidase or alpha-N-acetylgalactosaminidase activities
-
-
?
dextran T2000 + H2O
isomaltose + ?
the enzyme liberates isomaltose from the non-reducing end of a polymer of dextran. It does not show alpha-N-galactosidase or alpha-N-acetylgalactosaminidase activities
-
-
?
glucooligosaccharides + H2O
isomaltose + D-glucose
-
-
-
?
glucooligosaccharides + H2O
isomaltose + D-glucose
-
-
-
?
isomaltooligosaccharide + H2O
isomaltose + glucose
-
-
glucose not with isomaltotetraose and isomaltohexaose
r
isomaltooligosaccharide + H2O
isomaltose + glucose
-
condensation of isomaltose to isomaltotetraose
-
-
r
isomaltotriitol + H2O
isomaltose + sorbitol
-
-
-
-
?
isomaltotriitol + H2O
isomaltose + sorbitol
-
-
-
-
?
isomaltotriitol + H2O
isomaltose + sorbitol
-
-
-
-
?
isomaltotriitol + H2O
isomaltose + sorbitol
-
-
-
?
isomaltotriose + H2O
alpha-isomaltose + D-glucose
-
-
-
?
isomaltotriose + H2O
alpha-isomaltose + D-glucose
-
-
-
?
isomaltotriose + H2O
alpha-isomaltose + D-glucose
-
-
-
?
isomaltotriose + H2O
alpha-isomaltose + D-glucose
-
-
-
?
isomaltotriose + H2O
alpha-isomaltose + D-glucose
-
-
-
-
?
isomaltotriose + H2O
alpha-isomaltose + D-glucose
-
hydrolyzes alpha-1,6-glucosidic linkage
-
-
?
panose + H2O
alpha-isomaltose + D-glucose
-
-
-
?
panose + H2O
alpha-isomaltose + D-glucose
-
-
-
?
panose + H2O
alpha-isomaltose + D-glucose
-
-
-
?
panose + H2O
alpha-isomaltose + D-glucose
-
-
-
?
panose + H2O
alpha-isomaltose + D-glucose
-
-
-
-
?
panose + H2O
alpha-isomaltose + D-glucose
-
hydrolyzes alpha-1,4-glucosidic linkage
-
-
?
panose + H2O
isomaltose + D-glucose
-
-
-
-
?
panose + H2O
isomaltose + D-glucose
-
-
-
-
?
panose + H2O
isomaltose + D-glucose
-
-
-
-
?
panose + H2O
isomaltose + D-glucose
-
-
-
?
pullulan + H2O
isopanose
-
-
-
?
pullulan + H2O
isopanose
-
enzyme also has a weak isopullulanase activity
-
-
?
pullulan + H2O
isopanose
-
-
-
?
additional information
?
-
-
enzyme also hydrolyzes oligosaccharides with alpha-isomaltosyl unit in their non-reducing ends, no substrates are isopanose and maltotriose
-
-
?
additional information
?
-
-
enzyme is highly specific for the glucosyl moiety in both hydrolysis and transglycosylation
-
-
?
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D107A
-
activity similar to wild-type enzyme
D163A
-
activity similar to wild-type enzyme
D198N
-
0.003% of wild-type activity, largely increased Kd-value
D207A
4fold decrease in kcat/Km for 4-nitrophenyl alpha-isomaltoside as compared to wild-type value. 28fold decrease in kcat/Km for dextran T2000 as compared to wild-type value
D207A/N209A
4.2fold decrease in kcat/Km for 4-nitrophenyl alpha-isomaltoside as compared to wild-type value. 17.8fold decrease in kcat/Km for dextran T2000 as compared to wild-type value
D227A
-
no activity of dextran hydrolysis
D227E
-
decreased activity of dextran hydrolysis
D227N
-
decreased activity of dextran hydrolysis
D227Q
-
decreased activity of dextran hydrolysis
D266N
-
0.011% of wild-type activity, without change in substrate binding ability
D295A
-
activity similar to wild-type enzyme
D313N
-
0.002% of wild-type activity, largely increased Kd-value
D340A
-
activity similar to wild-type enzyme
D342A
-
no activity of dextran hydrolysis
D342E
-
decreased activity of dextran hydrolysis
D342N
-
decreased activity of dextran hydrolysis
D342Q
-
decreased activity of dextran hydrolysis
D373A
-
activity similar to wild-type enzyme
D396A
-
activity similar to wild-type enzyme
E420A
-
activity similar to wild-type enzyme
M243A
233fold decrease in kcat/Km for 4-nitrophenyl alpha-isomaltoside as compared to wild-type value. 334fold decrease in kcat/Km for dextran T2000 as compared to wild-type value
D207A
-
4fold decrease in kcat/Km for 4-nitrophenyl alpha-isomaltoside as compared to wild-type value. 28fold decrease in kcat/Km for dextran T2000 as compared to wild-type value
-
D207A/N209A
-
4.2fold decrease in kcat/Km for 4-nitrophenyl alpha-isomaltoside as compared to wild-type value. 17.8fold decrease in kcat/Km for dextran T2000 as compared to wild-type value
-
M243A
-
233fold decrease in kcat/Km for 4-nitrophenyl alpha-isomaltoside as compared to wild-type value. 334fold decrease in kcat/Km for dextran T2000 as compared to wild-type value
-
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Okada, G.; Takayanagi, T.; Miyahara, S.; Sawai, T.
An isomalto-dextranase accompanied by isopullulanase activity from Arthrobacter globiformis T6
Agric. Biol. Chem.
52
829-836
1988
Arthrobacter globiformis, Arthrobacter globiformis T6
-
brenda
Okada, G.; Takayanagi, T.; Sawai, T.
Improved purification and further characterization of an isomaltodextranase from Arthrobacter globiformis T6
Agric. Biol. Chem.
52
495-501
1988
Arthrobacter globiformis
-
brenda
Takayanagi, T.; Okada, G.; Chiba, S.
Quantitative study of the anomeric forms of isomaltose and glucose produced by isomalto-dextranase and glucodextranase
Agric. Biol. Chem.
51
2337-2341
1987
Arthrobacter globiformis
-
brenda
Sawai, T.; Ohara, S.; Ichimi, Y.; Okaji, S.; Hisada, K.; Fukaya, N.
Purification and some properties of the isomaltodextranase of Actinomadura strain R10 and comparison with that of Arthrobacter globiformis T6
Carbohydr. Res.
89
289-299
1981
Actinomadura sp., Arthrobacter globiformis, Actinomadura sp. R10
-
brenda
Sawai, T.; Tohyama, T.; Natsumi, T.
Hydrolysis of fourteen native dextrans by Arthrobacter isomaltodextranase and correlation with dextran structure
Carbohydr. Res.
66
195-205
1978
Arthrobacter globiformis
-
brenda
Sawai, T.; Ukigai, Y.; Nawa, A.
Identification of an isomalto-dextranase producing bacterium, Arthrobacter globiformis
Agric. Biol. Chem.
40
1249-1250
1976
Arthrobacter globiformis
-
brenda
Torii, M.; Sakakibara, K.; Misaki, A.; Sawai, T.
Degradation of alpha-linked D-gluco-oligosaccharides and dextrans by an isomalto-dextranase preparation from Arthrobacter globiformis T6
Biochem. Biophys. Res. Commun.
70
459-464
1976
Arthrobacter globiformis
brenda
Sawai, T.; Niwa, Y.
Transisomaltosylation activity of a bacterial isomalto-dextranase
Agric. Biol. Chem.
39
1077-1083
1975
Arthrobacter globiformis
-
brenda
Sawai, T.; Toriyama, K.; Yano, K.
A bacterial dextranase releasing only isomaltose from dextrans
J. Biochem.
75
105-112
1974
Arthrobacter globiformis
brenda
Kim, Y.K.; Tsumuraya, Y.; Sakano, Y.
Enzymatic preparation of novel non-reducing oligosaccharides having an isomaltosyl residue by using the transfer action of isomaltodextranase from Arthrobacter globiformis T6
Biosci. Biotechnol. Biochem.
59
1367-1369
1995
Arthrobacter globiformis
-
brenda
Iwai, A.; Ito, H.; Mizuno, T.; Mori, H.; Matsui, H.; Honma, M.; Okada, G.; Chiba, S.
Molecular cloning and expression of an isomalto-dextranase gene from Arthrobacter globiformis T6
J. Bacteriol.
176
7730-7734
1994
Arthrobacter globiformis
brenda
Takayanagi, T.; Kimura, A.; Okada, G.; Chiba, S.
Identification of ionizable groups essential to the activity of isomalto-dextranase from Arthrobacter globiformis
Biosci. Biotechnol. Biochem.
58
1995-1999
1994
Arthrobacter globiformis
-
brenda
Akita, M.; Mizuno, M.; Tonozuka, T.; Sakano, Y.; Matsui, H.; Hidaka, Y.; Hatada, Y.; Ito, S.; Horikoshi, K.
Crystallization and preliminary X-ray study of isomaltodextranase from Arthrobacter globiformis
Acta Crystallogr. Sect. D
60
572-573
2004
Arthrobacter globiformis
brenda
Hatada, Y.; Hidaka, Y.; Nogi, Y.; Uchimura, K.; Katayama, K.; Li, Z.; Akita, M.; Ohta, Y.; Goda, S.; Ito, H.; Matsui, H.; Ito, S.; Horikoshi, K.
Hyper-production of an isomalto-dextranase of an Arthrobacter sp. by a proteases-deficient Bacillus subtilis: sequencing, properties, and crystallization of the recombinant enzyme
Appl. Microbiol. Biotechnol.
65
583-592
2004
Arthrobacter dextranolyticus (Q6BE01)
brenda
Tochihara, T.; Sasaki, K.; Araki, O.; Morimoto, N.; Watanabe, K.; Hatada, Y.; Ito, S.; Ito, H.; Matsui, H.
Site-directed mutagenesis establishes aspartic acids-227 and -342 as essential for enzyme activity in an isomalto-dextranase from Arthrobacter globiformis
Biotechnol. Lett.
26
659-664
2004
Arthrobacter globiformis
brenda
Takayanagi, T.; Kimura, A.; Matsui, H.; Okada, G.; Chiba, S.
Evidence for a single active site on isomalto-dextranase with hydrolysis activities of alpha-1,6- and alpha-1,4-glucosidic linkages
J. Appl. Glycosci.
48
55-61
2001
Arthrobacter globiformis
-
brenda
Takayanagi, T.; Kimura, A.; Matsui, H.
Evaluation of subsite affinities of isomalto-dextranase from Arthrobacter globiformis
J. Appl. Glycosci.
49
123-127
2002
Arthrobacter globiformis
-
brenda
Takayanagi, T.
Enzymological studies on isomalto-dextranase from Arthrobacter globiformis
J. Appl. Glycosci.
49
57-62
2002
Arthrobacter globiformis
-
brenda
Tonozuka, T.; Suzuki, S.; Ikehara, Y.; Mizuno, M.; Kim, Y.K.; Nishikawa, A.; Sakano, Y.
Heterologous production and characterization of Arthrobacter globiformis T6 isomalto-dextranase
J. Appl. Glycosci.
51
27-32
2004
Arthrobacter globiformis
-
brenda
Nihira, T.; Mizuno, M.; Tonozuka, T.; Sakano, Y.; Mori, T.; Okahata, Y.
Kinetic studies of site-directed mutational isomalto-dextranase-catalyzed hydrolytic reactions on a 27 MHz quartz-crystal microbalance
Biochemistry
44
9456-9461
2005
Arthrobacter globiformis
brenda
Kikuchi, Y.; Date, M.; Itaya, H.; Matsui, K.; Wu, L.F.
Functional analysis of the twin-arginine translocation pathway in Corynebacterium glutamicum ATCC 13869
Appl. Environ. Microbiol.
72
7183-7192
2006
Arthrobacter globiformis
brenda
Okazawa, Y.; Miyazaki, T.; Yokoi, G.; Ishizaki, Y.; Nishikawa, A.; Tonozuka, T.
Crystal structure and mutational analysis of isomalto-dextranase, a member of glycoside hydrolase family 27
J. Biol. Chem.
290
26339-26349
2015
Arthrobacter globiformis (Q7WSN5), Arthrobacter globiformis T6 (Q7WSN5), Arthrobacter globiformis T6
brenda