Maltose phosphorylase
| 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 | ||||||||
| |||||||||
In enzymology, a maltose phosphorylase (EC 2.4.1.8) is an enzyme that catalyzes the chemical reaction
- 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. doi:10.1016/S0021-9258(18)44822-3. 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 (1): 204–209. doi:10.1042/bj0780204. PMC 1205197. PMID 13786484.
