EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
2.4.1.97 | (1,3-beta-D-glucosyl)n + phosphate |
- |
Ochromonas malhamensis |
(1,3-beta-D-glucosyl)n-1 + alpha-D-glucose 1-phosphate |
- |
? |
2.4.1.97 | (1,3-beta-D-glucosyl)n + phosphate |
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 |
Acacia verek |
(1,3-beta-D-glucosyl)n-1 + alpha-D-glucose 1-phosphate |
- |
r |
2.4.1.97 | (1,3-beta-D-glucosyl)n + phosphate |
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 |
Acacia verek |
(1,3-beta-D-glucosyl)n-1 + alpha-D-glucose 1-phosphate |
- |
? |
2.4.1.97 | alpha-D-glucose + glucose 1-phosphate |
- |
Euglena gracilis var. saccharophila |
phosphate + laminaribiose |
- |
r |
2.4.1.97 | laminaribiose + glucose 1-phosphate |
- |
Ochromonas malhamensis |
phosphate + laminarin |
- |
? |
2.4.1.97 | laminaribiose + glucose 1-phosphate |
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 |
Acacia verek |
phosphate + laminarin |
- |
r |
2.4.1.97 | laminaribiose + glucose 1-phosphate |
- |
Euglena gracilis var. saccharophila |
phosphate + laminaritriose |
- |
r |
2.4.1.97 | laminarihexaose + alpha-D-glucose 1-phosphate |
- |
Euglena gracilis var. saccharophila |
laminariheptaose + phosphate |
- |
r |
2.4.1.97 | laminarihexaose + 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 |
Ochromonas danica |
laminaripentaose + alpha-D-glucose 1-phosphate |
- |
r |
2.4.1.97 | laminarihexaose + 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 |
Ochromonas danica NIES-2142 |
laminaripentaose + alpha-D-glucose 1-phosphate |
- |
r |