EC number:2.7.1.175

Enzyme

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EC Tree
     2. Transferases
        2.7 Transferring phosphorus-containing groups
            2.7.1 Phosphotransferases with an alcohol group as acceptor
ID:2.7.1.175
Description:Maltokinase.
Cath: 3.90.1200.10;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.7.1.175
BRENDA Enzyme Link: BRENDA 2.7.1.175
KEGG Enzyme Link: KEGG2.7.1.175
BioCyc Enzyme Link: BioCyc 2.7.1.175
ExPASy Enzyme Link: ExPASy2.7.1.175
EC2PDB Enzyme Link: EC2PDB 2.7.1.175
ExplorEnz Enzyme Link: ExplorEnz 2.7.1.175
PRIAM enzyme-specific profiles Link: PRIAM 2.7.1.175
IntEnz Enzyme Link: IntEnz 2.7.1.175
MEDLINE Enzyme Link: MEDLINE 2.7.1.175

EC number:2.7.1.175

MSA:

2.7.1.175;
Phylogenetic Tree:

2.7.1.175;
Uniprot:
M-CSA:
RHEA:31915 ATP + maltose = ADP + alpha-maltose 1-phosphate + H(+)
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:7]-[*:8]>>[*:8]-[OH;+0:7].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:2]-[*:1]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Maltokinase (ATP:maltose 1-phosphotransferase) from Actinoplanes sp.: demonstration of enzyme activity and characterization of the reaction product.Drepper A, Peitzmann R, Pape H1996 Jun 178690081
Structure of mycobacterial maltokinase, the missing link in the essential GlgE-pathway.Fraga J, Maranha A, Mendes V, Pereira PJ, Empadinhas N, Macedo-Ribeiro S2015 Jan 2625619172
Homotypic dimerization of a maltose kinase for molecular scaffolding.Li J, Guan X, Shaw N, Chen W, Dong Y, Xu X, Li X, Rao Z2014 Sep 2325245657
Biochemical characterization of the maltokinase from Mycobacterium bovis BCG.Mendes V, Maranha A, Lamosa P, da Costa MS, Empadinhas N2010 May 2720507595