ID: | 2.4.1.8 |
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Description: | Maltose phosphorylase. |
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Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.UniProtKB Enzyme Link: | UniProtKB 2.4.1.8 |
BRENDA Enzyme Link: | BRENDA 2.4.1.8 |
KEGG Enzyme Link: | KEGG2.4.1.8 |
BioCyc Enzyme Link: | BioCyc 2.4.1.8 |
ExPASy Enzyme Link: | ExPASy2.4.1.8 |
EC2PDB Enzyme Link: | EC2PDB 2.4.1.8 |
ExplorEnz Enzyme Link: | ExplorEnz 2.4.1.8 |
PRIAM enzyme-specific profiles Link: | PRIAM 2.4.1.8 |
IntEnz Enzyme Link: | IntEnz 2.4.1.8 |
MEDLINE Enzyme Link: | MEDLINE 2.4.1.8 |
RHEA:21116 | maltose + phosphate = beta-D-glucose 1-phosphate + D-glucose |
RULE(radius=1) | [*:1]-[CH;+0:2](-[*:3])-[O;H0;+0:4]-[*:5].[*:6]-[OH;+0:7]>>[*:1]-[CH;+0:2](-[*:3])-[O;H0;+0:7]-[*:6].[*:5]-[OH;+0:4] |
Reaction | ![]() |
Core-to-Core |
Title | Authors | Date | PubMed ID |
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Enterococcus faecalis utilizes maltose by connecting two incompatible metabolic routes via a novel maltose 6'-phosphate phosphatase (MapP). | Mokhtari A, Blancato VS, Repizo GD, Henry C, Pikis A, Bourand A, de Fátima Álvarez M, Immel S, Mechakra-Maza A, Hartke A, Thompson J, Magni C, Deutscher J | 2013 Apr | 23490043 |
Identification of Bacillus selenitireducens MLS10 maltose phosphorylase possessing synthetic ability for branched α-D-glucosyl trisaccharides. | Nihira T, Saito Y, Kitaoka M, Otsubo K, Nakai H | 2012 Oct 1 | 22940176 |
Substrate-induced activation of maltose phosphorylase: interaction with the anomeric hydroxyl group of alpha-maltose and alpha-D-glucose controls the enzyme's glucosyltransferase activity. | Tsumuraya Y, Brewer CF, Hehre EJ | 1990 Aug 15 | 2143366 |
Phosphorolysis of maltose by enzyme preparations from Neisseria meningitidis. | FITTING C, DOUDOROFF M | 1952 Nov | 12999827 |