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(1,3-beta-D-glucosyl)n + phosphate
(1,3-beta-D-glucosyl)n-1 + alpha-D-glucose 1-phosphate
alpha-D-glucose + glucose 1-phosphate
phosphate + laminaribiose
-
-
-
r
laminaribiose + glucose 1-phosphate
phosphate + laminarin
laminaribiose + glucose 1-phosphate
phosphate + laminaritriose
-
-
-
r
laminarihexaose + alpha-D-glucose 1-phosphate
laminariheptaose + phosphate
-
-
-
r
laminarihexaose + phosphate
laminaripentaose + alpha-D-glucose 1-phosphate
laminaripentaose + alpha-D-glucose 1-phosphate
laminarihexaose + phosphate
-
-
-
r
laminaripentaose + phosphate
laminaritetraose + alpha-D-glucose 1-phosphate
laminaritetraose + alpha-D-glucose 1-phosphate
laminaripentaose + phosphate
-
-
-
r
laminaritetraose + phosphate
laminaritriose + alpha-D-glucose 1-phosphate
laminaritriose + alpha-D-glucose 1-phosphate
laminaritetraose + phosphate
-
-
-
r
laminaritriose + phosphate
laminaribiose + alpha-D-glucose 1-phosphate
additional information
?
-
(1,3-beta-D-glucosyl)n + phosphate
(1,3-beta-D-glucosyl)n-1 + alpha-D-glucose 1-phosphate
Acacia verek
-
in 50 mM citrate-phosphate buffer, pH 6.5, the phosphorolytic cleavage of laminarin and laminaribiose can be observed. In 0.02 M imidazole buffer, pH 6.5, the phosphorylase equilibrium lies in the direction of the synthesis reaction, alpha-D-glucose-1-phosphate as glucosyl donor is incorporated into laminaribiose
-
-
r
(1,3-beta-D-glucosyl)n + phosphate
(1,3-beta-D-glucosyl)n-1 + alpha-D-glucose 1-phosphate
Acacia verek
-
enzyme may be a key factor in the regulation of cell-wall extension and build up by switching hydrolase and synthase activity in a balance dependent manner
-
-
?
(1,3-beta-D-glucosyl)n + phosphate
(1,3-beta-D-glucosyl)n-1 + alpha-D-glucose 1-phosphate
Ochromonas malhamensis
-
-
-
-
?
laminaribiose + glucose 1-phosphate
phosphate + laminarin
Acacia verek
-
in 50 mM citrate-phosphate buffer, pH 6.5, the phosphorolytic cleavage of laminarin and laminaribiose can be observed. In 0.02 M imidazole buffer, pH 6.5, the phosphorylase equilibrium lies in the direction of the synthesis reaction, alpha-D-glucose-1-phosphate as glucosyl donor is incorporated into laminaribiose
-
-
r
laminaribiose + glucose 1-phosphate
phosphate + laminarin
Ochromonas malhamensis
-
-
-
-
?
laminarihexaose + phosphate
laminaripentaose + alpha-D-glucose 1-phosphate
-
the enzyme can catalyze reactions in both synthetic and phosphorolytic directions. Equilibrium studies indicate that the enzyme favors the reaction in the synthetic direction
-
-
r
laminarihexaose + phosphate
laminaripentaose + alpha-D-glucose 1-phosphate
-
the enzyme can catalyze reactions in both synthetic and phosphorolytic directions. Equilibrium studies indicate that the enzyme favors the reaction in the synthetic direction
-
-
r
laminaripentaose + phosphate
laminaritetraose + alpha-D-glucose 1-phosphate
-
the enzyme can catalyze reactions in both synthetic and phosphorolytic directions. Equilibrium studies indicate that the enzyme favors the reaction in the synthetic direction
-
-
r
laminaripentaose + phosphate
laminaritetraose + alpha-D-glucose 1-phosphate
-
the enzyme can catalyze reactions in both synthetic and phosphorolytic directions. Equilibrium studies indicate that the enzyme favors the reaction in the synthetic direction
-
-
r
laminaritetraose + phosphate
laminaritriose + alpha-D-glucose 1-phosphate
-
the enzyme can catalyze reactions in both synthetic and phosphorolytic directions. Equilibrium studies indicate that the enzyme favors the reaction in the synthetic direction
-
-
r
laminaritetraose + phosphate
laminaritriose + alpha-D-glucose 1-phosphate
-
the enzyme can catalyze reactions in both synthetic and phosphorolytic directions. Equilibrium studies indicate that the enzyme favors the reaction in the synthetic direction
-
-
r
laminaritriose + phosphate
laminaribiose + alpha-D-glucose 1-phosphate
-
-
-
?
laminaritriose + phosphate
laminaribiose + alpha-D-glucose 1-phosphate
-
the enzyme can catalyze reactions in both synthetic and phosphorolytic directions. Equilibrium studies indicate that the enzyme favors the reaction in the synthetic direction
products analysed by thin layer chromatography TLC
-
r
laminaritriose + phosphate
laminaribiose + alpha-D-glucose 1-phosphate
-
the enzyme can catalyze reactions in both synthetic and phosphorolytic directions. Equilibrium studies indicate that the enzyme favors the reaction in the synthetic direction
products analysed by thin layer chromatography TLC
-
r
additional information
?
-
protein is able to catalyze the conversion of glucose and glucose 1-phosphate into oligosaccharides with degree of polymerization up to 12 glucose units. Tps3 acts exclusively on glucose-beta-1,3-glucose oligosaccharides.The activity is dependent on both glucose and glucose 1-phosphate as substrates, excluding either from the reaction mixture completely abolishes oligosaccharide production
-
-
-
additional information
?
-
-
no phosphorolytic reaction with glucose, laminaribiose, cellobiose, celltriose, cellotetraose, cellopentaose, sohorose, gentiobiose, trehalose, kojibiose, nigerise, maltose, isomaltose, methyl alpha-D-glucopyranoside, methyl beta-D-glucopyranoside, p-nitrophenyl alpha-D-glucopyranoside, and p-nitrophenyl beta-D-glucopyranoside
-
-
?
additional information
?
-
-
no phosphorolytic reaction with glucose, laminaribiose, cellobiose, celltriose, cellotetraose, cellopentaose, sohorose, gentiobiose, trehalose, kojibiose, nigerise, maltose, isomaltose, methyl alpha-D-glucopyranoside, methyl beta-D-glucopyranoside, p-nitrophenyl alpha-D-glucopyranoside, and p-nitrophenyl beta-D-glucopyranoside
-
-
?
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250000
-
by gel filtration, indicating a homodimer and/or a heterodimer
113000
-
x * 113000, x * 118000, x * 124000, and/or heterodimer, native enzyme 250000 Da, SDS-PAGE, the three bands can not be separated
113000
-
x * 113000, x * 118000, x * 124000, and/or homodimer, native enzyme 250000 Da, SDS-PAGE, the three bands can not be separated
118000
-
x * 113000, x * 118000, x * 124000, and/or heterodimer, native enzyme 250000 Da, SDS-PAGE, the three bands can not be separated
118000
-
x * 113000, x * 118000, x * 124000, and/or homodimer, native enzyme 250000 Da, SDS-PAGE, the three bands can not be separated
124000
-
x * 113000, x * 118000, x * 124000, and/or heterodimer, native enzyme 250000 Da, SDS-PAGE, the three bands can not be separated
124000
-
x * 113000, x * 118000, x * 124000, and/or homodimer, native enzyme 250000 Da, SDS-PAGE, the three bands can not be separated
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Albrecht, G.J.; Kauss, H.
Purification, crystallization and properties of a beta-(1->3)-glucan phosphorylase from Ochromonas malhamensis
Phytochemistry
10
1293-1298
1971
Ochromonas malhamensis
-
brenda
Lienart, Y.; Comtat, J.; Barnoud, F.
Wall-bound 1,3-beta-D-glucan:orthophosphate glucosyltransferase activity from Acacia cultured cells
Plant Sci.
58
165-170
1988
Acacia verek
-
brenda
Yamamoto, Y.; Kawashima, D.; Hashizume, A.; Hisamatsu, M.; Isono, N.
Purification and characterization of 1,3-beta-D-glucan phosphorylase from Ochromonas danica
Biosci. Biotechnol. Biochem.
77
1949-1954
2013
Ochromonas danica, Ochromonas danica NIES-2142
brenda
Kuhaudomlarp, S.; Patron, N.; Henrissat, B.; Rejzek, M.; Saalbach, G.; Field, R.
Identification of Euglena gracilis beta-1,3-glucan phosphorylase and establishment of a new glycoside hydrolase (GH) family GH149
J. Biol. Chem.
293
2865-2876
2018
Euglena gracilis var. saccharophila (A0A2I6SUQ9)
brenda