Maltose-6'-phosphate glucosidase
| maltose-6'-phosphate glucosidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.2.1.122 | ||||||||
| CAS number | 98445-08-0 | ||||||||
| 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 / EGO | ||||||||
| |||||||||
In enzymology, a maltose-6'-phosphate glucosidase (EC 3.2.1.122) is an enzyme that catalyzes the chemical reaction
- maltose 6'-phosphate + H2O D-glucose + D-glucose 6-phosphate
Thus, the two substrates of this enzyme are maltose-6'-phosphate and H2O, whereas its two products are D-glucose and D-glucose 6-phosphate.
This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. This enzyme participates in starch and sucrose metabolism.
Nomenclature
The systematic name of this enzyme class is maltose-6'-phosphate 6-phosphoglucohydrolase. This enzyme is also called phospho-alpha-glucosidase.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1U8X.
References
- Thompson J, Gentry-Weeks CR, Nguyen NY, Folk JE, Robrish SA (1995). "Purification from Fusobacterium mortiferum ATCC 25557 of a 6-phosphoryl-O-alpha-D-glucopyranosyl:6-phosphoglucohydrolase that hydrolyzes maltose 6-phosphate and related phospho-alpha-D-glucosides". J. Bacteriol. 177 (9): 2505–12. PMC 176911
. PMID 7730284.
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