Enzyme

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     2. Transferases
        2.4 Glycosyltransferases
            2.4.1 Hexosyltransferases
ID:2.4.1.8
Description:Maltose phosphorylase.

3D structure

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References

External Links

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
MSA:

2.4.1.8;

Phylogenetic Tree:

2.4.1.8;

Uniprot:
M-CSA:
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 More

References

TitleAuthorsDatePubMed ID
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 J2013 Apr23490043
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 H2012 Oct 122940176
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 EJ1990 Aug 152143366
Phosphorolysis of maltose by enzyme preparations from Neisseria meningitidis.FITTING C, DOUDOROFF M1952 Nov12999827