In enzymology, a 1,3-beta-D-glucan phosphorylase (EC 2.4.1.97) is an enzyme that catalyzes the chemical reaction
1,3-beta-D-glucan phosphorylase | |||||||||
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Identifiers | |||||||||
EC no. | 2.4.1.97 | ||||||||
CAS no. | 37340-31-1 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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- (1,3-beta-D-glucosyl)n + phosphate (1,3-beta-D-glucosyl)n-1 + alpha-D-glucose 1-phosphate
Thus, the two substrates of this enzyme are (1,3-beta-D-glucosyl)n and phosphate, whereas its two products are (1,3-beta-D-glucosyl)n-1 and alpha-D-glucose 1-phosphate.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is 1,3-beta-D-glucan:phosphate alpha-D-glucosyltransferase. Other names in common use include laminarin phosphoryltransferase, 1,3-beta-D-glucan:orthophosphate glucosyltransferase, and laminarin phosphoryltransferase.
References
edit- Albrecht GJ, Kauss H (1971). "Purification, crystallization and properties of a beta-(1->3)-glucan phosphorylase from Ochromonas malhamensis". Phytochemistry. 10 (6): 1293–1298. doi:10.1016/S0031-9422(00)84330-7.
Gene Ontology (GO) codes
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