Laminaribiose phosphorylase
Class of enzymes
From Wikipedia, the free encyclopedia
Laminaribiose phosphorylase (EC 2.4.1.31) is an enzyme coded for by the IbpA gene found in Paenibacillus.[1] The enzyme catalyzes the chemical reaction
| Laminaribiose phosphorylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 3D model of Laminaribiose phosphrylase protein | |||||||||
| Identifiers | |||||||||
| EC no. | 2.4.1.31 | ||||||||
| CAS no. | 37257-29-7 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
The two substrates of this enzyme are laminaribiose and orthophosphate (Pi). Its products are α-D-glucose 1-phosphate and D-glucose. It was originally characterised from Euglena gracilis and Astasia ocellata. The reaction can also proceed in the opposite direction, to give laminaribiose.[2][3]
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is 3-beta-D-glucosyl-D-glucose:phosphate alpha-D-glucosyltransferase.[4]
