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1H54

Maltose phosphorylase from Lactobacillus brevis

Summary for 1H54
Entry DOI10.2210/pdb1h54/pdb
DescriptorMALTOSE PHOSPHORYLASE, POTASSIUM ION, PHOSPHATE ION, ... (4 entities in total)
Functional Keywordshydrolase, maltose metabolism
Biological sourceLACTOBACILLUS BREVIS
Total number of polymer chains2
Total formula weight171832.56
Authors
Van Tilbeurgh, H.,Egloff, M.-P. (deposition date: 2001-05-18, release date: 2001-09-05, Last modification date: 2024-05-08)
Primary citationEgloff, M.-P.,Uppenberg, J.,Haalck, L.,Van Tilbeurgh, H.
Crystal Structure of Maltose Phosphorylase from Lactobacillus Brevis: Unexpected Evolutionary Relationship with Glucoamylases.
Structure, 9:689-, 2001
Cited by
PubMed Abstract: Maltose phosphorylase (MP) is a dimeric enzyme that catalyzes the conversion of maltose and inorganic phosphate into beta-D-glucose-1-phosphate and glucose without requiring any cofactors, such as pyridoxal phosphate. The enzyme is part of operons that are involved in maltose/malto-oligosaccharide metabolism. Maltose phosphorylases have been classified in family 65 of the glycoside hydrolases. No structure is available for any member of this family.
PubMed: 11587643
DOI: 10.1016/S0969-2126(01)00626-8
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.15 Å)
Structure validation

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