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2-alpha-D-glucosyl-D-glucose + phosphate
D-glucose + beta-D-glucose 1-phosphate
3-O-alpha-D-glucopyranosyl-D-glucopyranose + phosphate
D-glucose + beta-D-glucose 1-phosphate
low activity, reaction of nigerose phosphorylase, EC 2.4.1.279
-
-
?
3-O-alpha-D-glucosyl-D-glucose + phosphate
D-glucose + beta-D-glucose 1-phosphate
alpha,alpha-trehalose + phosphate
D-glucose + beta-D-glucose 1-phosphate
very low activity, reaction of trehalose phosphorylase, EC 2.4.1.64
-
-
?
beta-D-glucose + beta-D-glucose 1-phosphate
2-alpha-D-glucosyl-D-glucose + phosphate
beta-D-glucose 1-phosphate + D-glucose
2-alpha-D-glucosyl-D-glucose + phosphate
-
-
-
-
?
beta-D-glucose 1-phosphate + glycerol
O-alpha-D-glucopyranosyl-(1,1)-glycerol + O-alpha-glucopyranosyl-(1,2)-O-alpha-D-glucopyranosyl-(1,1)-glycerol + phosphate
-
0.27% of the activity with D-glucose
-
-
?
beta-D-glucose 1-phosphate + myo-inositol
O-alpha-D-glucopyranosyl-(1,1)-myo-inositol + O-alpha-D-glucopyranosyl-(1,5)-myo-inositol + O-alpha-D-glucopyranosyl-(1,2)-O-alpha-D-glucopyranosyl-(1,1)-myo-inositol + O-alpha-D-glucopyranosyl-(1,2)-O-alpha-D-glucopyranosyl-(1,1)-myo-inositol
-
6.2% of the activity with D-glucose
-
-
?
beta-D-glucose 1-phosphate + raffinose
2-alpha-D-glucopyranosyl-raffinose + 2G(2-alpha-D-glucopyranosyl)2-raffinose + 2G(2-alpha-D-glucopyranosyl)3-raffinose
-
-
-
-
?
beta-D-glucose 1-phosphate + stachyose
2-alpha-D-glucopyranosyl-stachyose + 2G(2-alpha-D-glucopyranosyl)2-stachyose + 2G(2-alpha-D-glucopyranosyl)3-stachyose
-
-
-
-
?
beta-D-glucose-1-phosphate + 1,5-anhydro-D-glucitol
? + phosphate
cyclo-[(-6)-alpha-D-Glcp-(1-3)-alpha-D-Glcp-(1-6)-alpha-D-Glcp-(1-3)-alpha-D-Glcp-(1-)] + beta-D-glucose 1-phosphate
cyclo-[(-6)-alpha-D-Glcp-(1-3)-alpha-D-Glcp-(1-6)-[alpha-D-Glcp-(1-2)]-alpha-D-Glcp-(1-3)-alpha-D-Glcp-(1-)] + phosphate
-
i.e. CTS
major product, i.e. 2-O-alpha-D-glucopyranosyl-CTS
-
?
D-glucose + beta-D-glucose 1-phosphate
2-alpha-D-glucosyl-D-glucose + phosphate
D-glucose + O-beta-D-fructofuranosyl-(2-1)-O-beta-D-fructofuranosyl-(2-1)-O-beta-D-fructofuranosyl-(2-1)-glucopyranoside
[O-alpha-D-glucopyranosyl-1(1-2)]n-O-[beta-D-fructofuranosyl-(2-1)]3-alpha-D-glucopyranoside + phosphate
-
-
n = 1 or 2
?
D-sorbitol + 1,5-anhydro-D-glucitol
? + phosphate
kojibiose + phosphate
beta-D-glucose-1-phosphate + D-glucose
kojitetraose + phosphate
beta-D-glucose 1-phosphate + kojitriose
kojitriose + phosphate
beta-D-glucose 1-phosphate + 2-alpha-D-glucosyl-D-glucose
L-iditol + 1,5-anhydro-D-glucitol
? + phosphate
L-sorbose + 1,5-anhydro-D-glucitol
? + phosphate
maltose + phosphate
D-glucose + beta-D-glucose 1-phosphate
very low, activity, reaction of maltose phosphorylase, EC 2.4.1.8
-
-
?
O-alpha-D-xylopyranosyl-(1-2)-beta-D-fructofuranoside + 2 beta-D-glucose 1-phosphate
O-alpha-D-glucopyranosyl-(1-[2-O-alpha-D-glucopyranosyl-1]1-2)-O-alpha-D-xylopyranosyl-(1-2)-beta-D-fructofuranoside + 2 phosphate
-
-
-
r
O-alpha-D-xylopyranosyl-(1-2)-beta-D-fructofuranoside + 3 beta-D-glucose 1-phosphate
O-alpha-D-glucopyranosyl-(1-[2-O-alpha-D-glucopyranosyl-1]2-2)-O-alpha-D-xylopyranosyl-(1-2)-beta-D-fructofuranoside + 3 phosphate
-
-
-
r
O-alpha-D-xylopyranosyl-(1-2)-beta-D-fructofuranoside + beta-D-glucose 1-phosphate
O-alpha-D-glucopyranosyl-(1-[2-O-alpha-D-glucopyranosyl-1]0-2)-O-alpha-D-xylopyranosyl-(1-2)-beta-D-fructofuranoside + phosphate
-
-
-
r
palatinose + 2 beta-D-glucose 1-phosphate
2G(2-alpha-D-glucopyranosyl)2-palatinose + 2 phosphate
-
-
-
r
palatinose + 2 beta-D-glucose 1-phosphate
O-alpha-D-glucopyranosyl-(1-2)-O-alpha-D-glucopyranosyl-(1-2)-O-alpha-D-glucopyranosyl-(1-6)-D-fructofuranose + 2 phosphate
-
-
-
r
palatinose + beta-D-glucose 1-phosphate
2G-alpha-D-glucopyranosyl-palatinose + phosphate
-
-
-
r
palatinose + beta-D-glucose 1-phosphate
O-alpha-D-glucopyranosyl-(1-2)-O-alpha-D-glucopyranosyl-(1-6)-D-fructofuranose + phosphate
-
-
-
r
additional information
?
-
2-alpha-D-glucosyl-D-glucose + phosphate
D-glucose + beta-D-glucose 1-phosphate
-
-
-
-
r
2-alpha-D-glucosyl-D-glucose + phosphate
D-glucose + beta-D-glucose 1-phosphate
-
-
-
r
2-alpha-D-glucosyl-D-glucose + phosphate
D-glucose + beta-D-glucose 1-phosphate
-
-
-
-
r
2-alpha-D-glucosyl-D-glucose + phosphate
D-glucose + beta-D-glucose 1-phosphate
-
-
-
?
2-alpha-D-glucosyl-D-glucose + phosphate
D-glucose + beta-D-glucose 1-phosphate
-
-
-
?
2-alpha-D-glucosyl-D-glucose + phosphate
D-glucose + beta-D-glucose 1-phosphate
-
activity of a LaMP loop 3 maltose phosphorylase mutant, no activity with wild-type maltose phosphorylase, which is strictly specific for maltose
-
-
r
2-alpha-D-glucosyl-D-glucose + phosphate
D-glucose + beta-D-glucose 1-phosphate
-
activity of a LaMP loop 3 maltose phosphorylase mutant, no activity with wild-type maltose phosphorylase, which is strictly specific for maltose
-
-
r
2-alpha-D-glucosyl-D-glucose + phosphate
D-glucose + beta-D-glucose 1-phosphate
2-alpha-D-glucosyl-D-glucose i.e. kojibiose. The enzyme is involved in conversion of kojibiose into beta-D-glucose 6-phosphate, a substrate of the glycolytic pathway. Disaccharide utilization pathway via phosphorolysis in hyperthermophilic archaea
-
-
?
2-alpha-D-glucosyl-D-glucose + phosphate
D-glucose + beta-D-glucose 1-phosphate
2-alpha-D-glucosyl-D-glucose i.e. kojibiose
-
-
r
2-alpha-D-glucosyl-D-glucose + phosphate
D-glucose + beta-D-glucose 1-phosphate
2-alpha-D-glucosyl-D-glucose i.e. kojibiose. The enzyme is involved in conversion of kojibiose into beta-D-glucose 6-phosphate, a substrate of the glycolytic pathway. Disaccharide utilization pathway via phosphorolysis in hyperthermophilic archaea
-
-
?
2-alpha-D-glucosyl-D-glucose + phosphate
D-glucose + beta-D-glucose 1-phosphate
2-alpha-D-glucosyl-D-glucose i.e. kojibiose
-
-
r
2-alpha-D-glucosyl-D-glucose + phosphate
D-glucose + beta-D-glucose 1-phosphate
-
-
-
-
?
2-alpha-D-glucosyl-D-glucose + phosphate
D-glucose + beta-D-glucose 1-phosphate
-
-
-
r
2-alpha-D-glucosyl-D-glucose + phosphate
D-glucose + beta-D-glucose 1-phosphate
-
-
-
-
?
3-O-alpha-D-glucosyl-D-glucose + phosphate
D-glucose + beta-D-glucose 1-phosphate
1-alpha-D-glucosyl-D-glucose i.e. nigerose, at 0.23% of the activity with kojibiose
-
-
?
3-O-alpha-D-glucosyl-D-glucose + phosphate
D-glucose + beta-D-glucose 1-phosphate
1-alpha-D-glucosyl-D-glucose i.e. nigerose, at 0.23% of the activity with kojibiose
-
-
?
beta-D-glucose + beta-D-glucose 1-phosphate
2-alpha-D-glucosyl-D-glucose + phosphate
-
-
-
-
r
beta-D-glucose + beta-D-glucose 1-phosphate
2-alpha-D-glucosyl-D-glucose + phosphate
-
-
-
-
r
beta-D-glucose-1-phosphate + 1,5-anhydro-D-glucitol
? + phosphate
-
-
-
?
beta-D-glucose-1-phosphate + 1,5-anhydro-D-glucitol
? + phosphate
-
-
-
?
D-glucose + beta-D-glucose 1-phosphate
2-alpha-D-glucosyl-D-glucose + phosphate
-
-
-
r
D-glucose + beta-D-glucose 1-phosphate
2-alpha-D-glucosyl-D-glucose + phosphate
-
-
kojioligosaccharides having only the alpha-1,2-linkage are synthesized and the average degree of polymerization of oligosaccharides increases with decreasing proportions of glucose
?
D-glucose + beta-D-glucose 1-phosphate
2-alpha-D-glucosyl-D-glucose + phosphate
-
-
[O-alpha-D-glucopyranosyl-(1-2)]m-O-[beta-D-fructofuranosyl-(2-1)]2-alpha-D-glucopyranoside with m = 1, 2 or 3
?
D-sorbitol + 1,5-anhydro-D-glucitol
? + phosphate
-
-
-
?
D-sorbitol + 1,5-anhydro-D-glucitol
? + phosphate
-
-
-
?
kojibiose + phosphate
beta-D-glucose-1-phosphate + D-glucose
-
-
-
-
?
kojibiose + phosphate
beta-D-glucose-1-phosphate + D-glucose
-
-
-
-
r
kojibiose + phosphate
beta-D-glucose-1-phosphate + D-glucose
-
-
-
-
r
kojitetraose + phosphate
beta-D-glucose 1-phosphate + kojitriose
-
-
-
-
r
kojitetraose + phosphate
beta-D-glucose 1-phosphate + kojitriose
-
-
-
-
r
kojitriose + phosphate
beta-D-glucose 1-phosphate + 2-alpha-D-glucosyl-D-glucose
-
-
-
-
r
kojitriose + phosphate
beta-D-glucose 1-phosphate + 2-alpha-D-glucosyl-D-glucose
-
-
-
-
r
L-iditol + 1,5-anhydro-D-glucitol
? + phosphate
-
-
-
?
L-iditol + 1,5-anhydro-D-glucitol
? + phosphate
-
-
-
?
L-sorbose + 1,5-anhydro-D-glucitol
? + phosphate
-
-
-
?
L-sorbose + 1,5-anhydro-D-glucitol
? + phosphate
-
-
-
?
additional information
?
-
-
the enzyme is absolutely specific for kojioligosaccharides in the phosphorolysis reaction, no activity with lactose, sucrose, trehalose, cellobiose, isomaltose, maltose, nigerose, and neotrehalose. For the synthesis reaction, the enzyme is specific for D-glucose, followed by kojibiose and kojitriose, overview
-
-
?
additional information
?
-
nigerose, maltose, and trehalose are minor substrates for the wild-type enzyme, substrate specificity of wild-type and mutant enzymes, overview
-
-
?
additional information
?
-
-
nigerose, maltose, and trehalose are minor substrates for the wild-type enzyme, substrate specificity of wild-type and mutant enzymes, overview
-
-
?
additional information
?
-
-
the enzyme is absolutely specific for kojioligosaccharides in the phosphorolysis reaction, no activity with lactose, sucrose, trehalose, cellobiose, isomaltose, maltose, nigerose, and neotrehalose. For the synthesis reaction, the enzyme is specific for D-glucose, followed by kojibiose and kojitriose, overview
-
-
?
additional information
?
-
no activity with trehalose or cellobiose. Activity with maltose or isomaltose es less than 0.001% of the activity with kojibiose
-
-
?
additional information
?
-
-
no activity with trehalose or cellobiose. Activity with maltose or isomaltose es less than 0.001% of the activity with kojibiose
-
-
?
additional information
?
-
no activity with trehalose or cellobiose. Activity with maltose or isomaltose es less than 0.001% of the activity with kojibiose
-
-
?
additional information
?
-
-
enzyme also catalyzes the chain-extending reaction of the side chain of 2-O-alpha-D-glucopyranosyl-CTS
-
-
?
additional information
?
-
-
no activity with ethanol, ethyleneglycol, 1-propanol, propyleneglycol, 1-butanol and 1,2-butanediol as acceptor
-
-
?
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evolution
-
the enzyme belongs to the glycoside hydrolase family 65, GH65
evolution
-
the enzyme is a member of glycoside hydrolase family 65, GH65
evolution
-
the enzyme is a member of glycoside hydrolase family 65, GH65
evolution
the kojibiose phosphorylase belongs to the glycoside hydrolase (GH) family 65, that contains phosphorylases acting on maltose (Glc-alpha1,4-Glc), kojibiose (Glc-alpha1,2-Glc), trehalose (Glc-alpha1,alpha1,-Glc), and nigerose (Glc-alpha1,3-Glc). The loop 3 region comprising the active site of kojibiose phosphorylase is significantly longer than the active sites of other enzymes, and three residues around this loop, Trp391, Glu392, and Thr417, recognize kojibiose
evolution
-
the enzyme is a member of glycoside hydrolase family 65, GH65
-
evolution
-
the enzyme belongs to the glycoside hydrolase family 65, GH65
-
evolution
-
the enzyme is a member of glycoside hydrolase family 65, GH65
-
physiological function
the enzyme is involved in conversion of kojibiose into beta-D-glucose 6-phosphate, a substrate of the glycolytic pathway. Disaccharide utilization pathway via phosphorolysis in hyperthermophilic archaea
physiological function
-
the enzyme is involved in conversion of kojibiose into beta-D-glucose 6-phosphate, a substrate of the glycolytic pathway. Disaccharide utilization pathway via phosphorolysis in hyperthermophilic archaea
-
additional information
-
structure-function relationship analysis, homology modelling, overview. Substitution of maltose phosphorylase, EC 2.4.1.8, His413-Glu421, His413-Ile418 and His413-Glu415 from loop 3, that include His413 and Glu415 presumably recognising the alpha-anomeric O-1 group of the glucose moiety at subsite 1+, by corresponding to segments from Ser426-Ala431 in trehalose phosphorylase, EC 2.4.1.64, and Thr419-Phe427 in kojibiose phosphorylase, EC 2.4.1.230, thus confers the maltose phosphorylase with phosphorolytic activity towards trehalose and kojibiose, respectively. The loop 3 in GH65 disaccharide phosphorylase is a key determinant for specificity both in phosphorolysis and in regiospecific reverse phosphorolysis
additional information
-
structure-function relationship analysis, overview. The sequence Thr419-Phe427 is responsible for substrate specificity of the enzyme for kojibiose. The loop 3 in GH65 disaccharide phosphorylase is a key determinant for specificity both in phosphorolysis and in regiospecific reverse phosphorolysis
additional information
the loop 3 region comprises the active site of kojibiose, three residues around this loop, Trp391, Glu392, and Thr417, recognize kojibiose. Trp391 and Glu392, especially the latter, are required for the kojibiose activity, active site structure and substrate binding, overview. Comparison of substrate recognition by kojibiose phosphorylase CsKP from Caldicellulosiruptor saccharolyticus and maltose phosphorylase LbMP from Lactobacillus brevis, modeling, overview
additional information
-
the loop 3 region comprises the active site of kojibiose, three residues around this loop, Trp391, Glu392, and Thr417, recognize kojibiose. Trp391 and Glu392, especially the latter, are required for the kojibiose activity, active site structure and substrate binding, overview. Comparison of substrate recognition by kojibiose phosphorylase CsKP from Caldicellulosiruptor saccharolyticus and maltose phosphorylase LbMP from Lactobacillus brevis, modeling, overview
additional information
-
structure-function relationship analysis, homology modelling, overview. Substitution of maltose phosphorylase, EC 2.4.1.8, His413-Glu421, His413-Ile418 and His413-Glu415 from loop 3, that include His413 and Glu415 presumably recognising the alpha-anomeric O-1 group of the glucose moiety at subsite 1+, by corresponding to segments from Ser426-Ala431 in trehalose phosphorylase, EC 2.4.1.64, and Thr419-Phe427 in kojibiose phosphorylase, EC 2.4.1.230, thus confers the maltose phosphorylase with phosphorolytic activity towards trehalose and kojibiose, respectively. The loop 3 in GH65 disaccharide phosphorylase is a key determinant for specificity both in phosphorolysis and in regiospecific reverse phosphorolysis
-
additional information
-
structure-function relationship analysis, overview. The sequence Thr419-Phe427 is responsible for substrate specificity of the enzyme for kojibiose. The loop 3 in GH65 disaccharide phosphorylase is a key determinant for specificity both in phosphorolysis and in regiospecific reverse phosphorolysis
-
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E392R
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E392R/T417A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E392R/T417I
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
T417A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
T417F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
T417I
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W391M/E392V
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W391M/E392V/T417A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W391M/E392V/T417I
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D177N
-
106% of wild-type activity
D271N
-
69% of wild-type activity
D340N
-
89% of wild-type activity
D362N
-
complete loss of enzymic activity
D459N
-
increase in Km-values for kojibiose, beta-D-glucose 1-phosphate and glucose
D513N
-
enhanced thermostablility and thermoactivity
E284Q
-
103% of wild-type activity
E642Q
-
complete loss of enzymic activity
K114Q
-
85% of wild-type activity
K403Q
-
73% of wild-type activity
K614Q
-
complete loss of enzymic activity
K749Q
-
78% of wild-type activity
R137Q
-
61% of wild-type activity
R33Q
-
31% of wild-type activity
R476Q
-
50% of wild-type activity
R48Q
-
62% of wild-type activity
D177N
-
106% of wild-type activity
-
D362N
-
complete loss of enzymic activity
-
E642Q
-
complete loss of enzymic activity
-
K403Q
-
73% of wild-type activity
-
K614Q
-
complete loss of enzymic activity
-
additional information
-
substitution of maltose phosphorylase, EC 2.4.1.8, His413-Glu421, His413-Ile418 and His413-Glu415 from loop 3, that include His413 and Glu415 presumably recognising the alpha-anomeric O-1 group of the glucose moiety at subsite 1+, by corresponding to segments from Ser426-Ala431 in trehalose phosphorylase, EC 2.4.1.64, and Thr419-Phe427 in kojibiose phosphorylase, EC 2.4.1.230, thus confers the maltose phosphorylase with phosphorolytic activity towards trehalose and kojibiose, respectively
additional information
-
substitution of maltose phosphorylase, EC 2.4.1.8, His413-Glu421, His413-Ile418 and His413-Glu415 from loop 3, that include His413 and Glu415 presumably recognising the alpha-anomeric O-1 group of the glucose moiety at subsite 1+, by corresponding to segments from Ser426-Ala431 in trehalose phosphorylase, EC 2.4.1.64, and Thr419-Phe427 in kojibiose phosphorylase, EC 2.4.1.230, thus confers the maltose phosphorylase with phosphorolytic activity towards trehalose and kojibiose, respectively
-
additional information
-
chimeric phosphorylases are constructed of the kojibiose phosphorylase gene and the trehalose phosphorylase gene from Thermoanaerobacter brockii. Chimera V-III show not trehalose phosphorylase, but kojibiose phosphorylase activity, although only 125 amino acid residues in 785 residues of chimera VIII are from that of kojibiose phosphorylase. Chimera V-III have 1% of the specific activity of the wild-type kojibiose phosphorylase. The temperature profile and kinetic parameters of chimera V-III are remarkably changed as compared to those of the wild-type kojibiose phosphorylase. Chimera VIII protein exists as a monomer in solution, whereas wild-type kojibiose phosphorylase and trehalose phosphorylase are hexamer and dimer structures, respectively. The chimera acts on nigerose, sophorose and laminaribiose, in addition to kojibiose. Chimera VIII is also able to act on sophorose and laminaribiose in the absence of inorganic phosphate, and produces two trisaccharides, beta-D-glucosyl-(1,6)-laminaribiose and laminaritriose, from laminaribiose
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Chaen, H.; Yamamoto, T.; Nishimoto, T.; Nakada, T.; Fukuda, S.; Sugimoto, T.; Kurimoto, M.; Tsujisaka, Y.
Purification and characterization of a novel phosphorylase, kojibiose phosphorylase, from Thermoanaerobium brockii
J. Appl. Glycosci.
46
423-429
1999
Thermoanaerobacter brockii
-
brenda
Chaen, H.; Nishimoto, T.; Nakada, T.; Fukuda, S.; Kurimoto, M.; Tsujisaka, Y.
Enzymatic synthesis of kojioligosaccharides using kojibiose phosphorylase
J. Biosci. Bioeng.
92
177-182
2001
Thermoanaerobacter brockii
brenda
Okada, H.; Fukushi, E.; Onodera, S.; Nishimoto, T.; Kawabata, J.; Kikuchi, M.; Shiomi, N.
Synthesis and structural analysis of five novel oligosaccharides prepared by glucosyltransfer from beta-D-glucose 1-phosphate to isokestose and nystose using Thermoanaerobacter brockii kojibiose phosphorylase
Carbohydr. Res.
338
879-885
2003
Thermoanaerobacter brockii
brenda
Watanabe, H.; Higashiyama, T.; Aga, H.; Nishimoto, T.; Kubota, M.; Fukuda, S.; Kurimoto, M.; Tsujisaka, Y.
Enzymatic synthesis of a 2-O-alpha-D-glucopyranosyl cyclic tetrasaccharide by kojibiose phosphorylase
Carbohydr. Res.
340
449-454
2005
Thermoanaerobacter brockii
brenda
Yamamoto, T.; Mukai, K.; Yamashita, H.; Kubota, M.; Fukuda, S.; Kurimoto, M.; Tsujisaka, Y.
Enhancement of thermostability of kojibiose phosphorylase from Thermoanaerobacter brockii ATCC35047 by random mutagenesis
J. Biosci. Bioeng.
100
212-215
2005
Thermoanaerobacter brockii
brenda
Yamamoto, T.; Maruta, K.; Mukai, K.; Yamashita, H.; Nishimoto, T.; Kubota, M.; Fukuda, S.; Kurimoto, M.; Tsujisaka, Y.
Cloning and sequencing of kojibiose phosphorylase gene from Thermoanaerobacter brockii ATCC35047
J. Biosci. Bioeng.
98
99-106
2004
Thermoanaerobacter brockii, Thermoanaerobacter brockii ATCC 35047
brenda
Takahashi, N.; Okada, H.; Fukushi, E.; Onodera, S.; Nishimoto, T.; Kawabata, J.; Shiomi, N.
Structural analysis of six novel oligosaccharides synthesized by glucosyl transfer from beta-D-glucose 1-phosphate to raffinose and stachyose using Thermoanaerobacter brockii kojibiose phosphorylase
Tetrahedron
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57-63
2005
Thermoanaerobacter brockii
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brenda
Yamamoto, T.; Yamashita, H.; Mukai, K.; Watanabe, H.; Kubota, M.; Chaen, H.; Fukuda, S.
Construction and characterization of chimeric enzymes of kojibiose phosphorylase and trehalose phosphorylase from Thermoanaerobacter brockii
Carbohydr. Res.
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2006
Thermoanaerobacter brockii
brenda
Yamamoto, T.; Mukai, K.; Maruta, K.; Watanabe, H.; Yamashita, H.; Nishimoto, T.; Kubota, M.; Chaen, H.; Fukuda, S.
Hyper expression of kojibiose phosphorylase gene and trehalose phosphorylase gene from Thermoanaerobacter brockii ATCC35047 in Bacillus subtilis and selaginose synthesis utilizing two phosphorylases
J. Biosci. Bioeng.
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343-346
2005
Thermoanaerobacter brockii, Thermoanaerobacter brockii TCC35047
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Yamamoto, T.; Watanabe, H.; Nishimoto, T.; Aga, H.; Kubota, M.; Chaen, H.; Fukuda, S.
Acceptor recognition of kojibiose phosphorylase from Thermoanaerobacter brockii: syntheses of glycosyl glycerol and myo-inositol
J. Biosci. Bioeng.
101
427-433
2006
Thermoanaerobacter brockii
brenda
Takahashi, N.; Fukushi, E.; Onodera, S.; Benkeblia, N.; Nishimoto, T.; Kawabata, J.; Shiomi, N.
Three novel oligosaccharides synthesized using Thermoanaerobacter brockii kojibiose phosphorylase
Chem. Cent. J.
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2007
Thermoanaerobacter brockii (Q8L163), Thermoanaerobacter brockii
brenda
Takahashi, N.; Fukushi, E.; Onodera, S.; Nishimoto, T.; Kawabata, J.; Shiomi, N.
Isolation and identification of novel tri- and tetra-saccharides synthesized by Thermoanaerobacter brockii kojibiose phosphorylase
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2007
Thermoanaerobacter brockii (Q8L163)
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Nakai, H.; Petersen, B.O.; Westphal, Y.; Dilokpimol, A.; Abou Hachem, M.; Duus, J.?.; Schols, H.A.; Svensson, B.
Rational engineering of Lactobacillus acidophilus NCFM maltose phosphorylase into either trehalose or kojibiose dual specificity phosphorylase
Protein Eng. Des. Sel.
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781-787
2010
Thermoanaerobacter brockii, Lactobacillus acidophilus, Thermoanaerobacter brockii ATCC 35047
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Yamamoto, T.; Nishio-Kosaka, M.; Izawa, S.; Aga, H.; Nishimoto, T.; Chaen, H.; Fukuda, S.
Enzymatic properties of recombinant kojibiose phosphorylase from Caldicellulosiruptor saccharolyticus ATCC43494
Biosci. Biotechnol. Biochem.
75
1208-1210
2011
Caldicellulosiruptor saccharolyticus, Caldicellulosiruptor saccharolyticus ATCC 43494
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Jung, J.H.; Seo, D.H.; Holden, J.F.; Park, C.S.
Identification and characterization of an archaeal kojibiose catabolic pathway in the hyperthermophilic Pyrococcus sp. strain ST04
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1122-1131
2014
Pyrococcus sp. (I3RFR4), Pyrococcus sp., Pyrococcus sp. ST04 (I3RFR4)
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Okada, S.; Yamamoto, T.; Watanabe, H.; Nishimoto, T.; Chaen, H.; Fukuda, S.; Wakagi, T.; Fushinobu, S.
Structural and mutational analysis of substrate recognition in kojibiose phosphorylase
FEBS J.
281
778-786
2014
Caldicellulosiruptor saccharolyticus (A4XGP2), Caldicellulosiruptor saccharolyticus
brenda
Mukherjee, K.; Narindoshvili, T.; Raushel, F.M.
Discovery of a kojibiose phosphorylase in Escherichia coli K-12
Biochemistry
57
2857-2867
2018
Escherichia coli (P77154), Escherichia coli MG1655 (P77154)
brenda