In enzymology, a maltose phosphorylase (EC 2.4.1.8) is an enzyme that catalyzes the chemical reaction
| maltose phosphorylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 maltose phosphorylase dimer, Lactobacillus brevis | |||||||||
| Identifiers | |||||||||
| EC no. | 2.4.1.8 | ||||||||
| CAS no. | 9030-19-7 | ||||||||
| 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 | ||||||||
| |||||||||
- maltose + phosphate D-glucose + beta-D-glucose 1-phosphate
Thus, the two substrates of this enzyme are maltose and phosphate, whereas its two products are D-glucose and beta-D-glucose 1-phosphate.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is maltose:phosphate 1-beta-D-glucosyltransferase. This enzyme participates in starch and sucrose metabolism.
Structural studies edit
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1H54.
References edit
- Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 5, Academic Press, New York, 1961, p. 229-236.
- FITTING C, DOUDOROFF M (1952). "Phosphorolysis of maltose by enzyme preparations from Neisseria meningitidis". J. Biol. Chem. 199 (1): 153–63. PMID 12999827.
- Putman EW, Litt CF, Hassid WZ (1955). "The structure of D-glucose-D-xylose synthesized by maltose phosphorylase". J. Am. Chem. Soc. 77 (16): 4351–4353. doi:10.1021/ja01621a050.
- Wood BJ, Rainbow C (1961). "The maltophosphorylase of beer lactobacilli". Biochem. J. 78: 204–209. PMC 1205197. PMID 13786484.
