Biology:Maltose phosphorylase
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Short description: Class of enzymes
| Maltose phosphorylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 maltose phosphorylase dimer, Lactobacillus brevis | |||||||||
| Identifiers | |||||||||
| EC number | 2.4.1.8 | ||||||||
| CAS number | 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 phosphorylase (EC 2.4.1.8) is an enzyme that catalyzes the chemical reaction
- REDIRECT Template:Chemical reaction
The two substrates of this enzyme characterised from Neisseria meningitidis[1] and lactobacilli in beer[2] are maltose and orthophosphate (Pi). Its products are D-glucose and β-D-glucose 1-phosphate.[3]
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.[4][5]
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1H54.
References
- ↑ "Phosphorolysis of maltose by enzyme preparations from Neisseria meningitidis". J. Biol. Chem. 199 (1): 153–63. 1952. doi:10.1016/S0021-9258(18)44822-3. PMID 12999827.
- ↑ "The maltophosphorylase of beer lactobacilli". Biochem. J. 78 (1): 204–209. 1961. doi:10.1042/bj0780204. PMID 13786484.
- ↑ "The structure of D-glucose-D-xylose synthesized by maltose phosphorylase". J. Am. Chem. Soc. 77 (16): 4351–4353. 1955. doi:10.1021/ja01621a050. Bibcode: 1955JAChS..77.4351P.
- ↑ Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 5, Academic Press, New York, 1961, p. 229-236
- ↑ Enzyme 2.4.1.8 at KEGG Pathway Database.
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