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Catalytic Site Atlas Version 2.2.12
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CSA entry for 1h54
Original Entry
Title:
Hydrolase
Compound:
Maltose phosphorylase
Mutant:
No
UniProt/Swiss-Prot:
Q7SIE1-Q7SIE1
EC Class:
2.4.1.8
Other CSA Entries:
Overview of all sites for 1h54
Homologues of 1h54
Entries for UniProt/Swiss-Prot: Q7SIE1
Entries for EC: 2.4.1.8
Other Databases:
PDB entry: 1h54
PDBsum entry: 1h54
UniProt/Swiss-Prot: Q7SIE1
IntEnz entry: 2.4.1.8
Literature Report:
Introduction:
Maltose phosphorylase(MP) catalyses the conversion of maltose and inorganic phosphate into beta-D-glucose-1-phosphate and glucose without a cofactor. It belongs to family 65 of glycoside hydrolases.
Mechanism:
By analogy to the catalytic domain of glucoamylase, Glu487 of MP acts as an acid to protonate the glycosidic bond oxygen and one of the phosphate oxygen performs a nucleophilic attack at the C1 anomeric carbon of the substrate to yield glucose-1-phosphate and glucose.
Sites:

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Found by:
Literature reference 

ResidueChainNumberUniProt numberFunctional part FunctionTargetDescription
GLUA 487 0Sidechain
Acid/baseSubstrate
It acts as an acid to protonate the glycosidic bond.
Evidence from paper Evidence concerns Evidence type
PubMed ID 11587643 Current protein Residue is positioned appropriately (ligand position hypothetical)
PubMed ID 11587643 Current protein Structural similarity to homologue of known mechanism
PubMed ID 11587643 Current protein Conservation of residue
References:
1
Crystal structure of maltose phosphorylase from Lactobacillus brevis: unexpected evolutionary relationship with glucoamylases.
M. P. Egloff and J. Uppenberg and L. Haalck and H. van Tilbeurgh
Structure (Camb) 9, (8) 689-97, (2001).
11587643
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