Laminaribiose phosphorylase
| 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 | ||||||||
| |||||||||
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
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]
References
- ↑ "UniProt". UniProt. Retrieved 2025-12-04.
- ↑ Goldemberg SH, Marechal LR, De Souza BC (1966). "Beta-1,3-oligoglucan: orthophosphate glucosyltransferase from Euglena gracilis". Journal of Biological Chemistry. 241 (1): 45–50. doi:10.1016/S0021-9258(18)96955-3. PMID 5901055.
- ↑ Manners DJ, Taylor DC (1967). "Studies on carbohydrate metabolizing enzymes. XVI. Specificity of laminaribiose phosphorylase from Astasia ocellata". Archives of Biochemistry and Biophysics. 121 (2): 443–51. doi:10.1016/0003-9861(67)90099-9. PMID 6057111.
- ↑ Enzyme 2.4.1.31 at KEGG Pathway Database.
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