1H54
Maltose phosphorylase from Lactobacillus brevis
Summary for 1H54
Entry DOI | 10.2210/pdb1h54/pdb |
Descriptor | MALTOSE PHOSPHORYLASE, POTASSIUM ION, PHOSPHATE ION, ... (4 entities in total) |
Functional Keywords | hydrolase, maltose metabolism |
Biological source | LACTOBACILLUS BREVIS |
Total number of polymer chains | 2 |
Total formula weight | 171832.56 |
Authors | Van Tilbeurgh, H.,Egloff, M.-P. (deposition date: 2001-05-18, release date: 2001-09-05, Last modification date: 2024-05-08) |
Primary citation | Egloff, 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: 11587643DOI: 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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