EC number:2.7.1.27

Enzyme

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     2. Transferases
        2.7 Transferring phosphorus-containing groups
            2.7.1 Phosphotransferases with an alcohol group as acceptor
ID:2.7.1.27
Description:Erythritol kinase (D-erythritol 4-phosphate-forming).

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.7.1.27
BRENDA Enzyme Link: BRENDA 2.7.1.27
KEGG Enzyme Link: KEGG2.7.1.27
BioCyc Enzyme Link: BioCyc 2.7.1.27
ExPASy Enzyme Link: ExPASy2.7.1.27
EC2PDB Enzyme Link: EC2PDB 2.7.1.27
ExplorEnz Enzyme Link: ExplorEnz 2.7.1.27
PRIAM enzyme-specific profiles Link: PRIAM 2.7.1.27
IntEnz Enzyme Link: IntEnz 2.7.1.27
MEDLINE Enzyme Link: MEDLINE 2.7.1.27

EC number:2.7.1.27

MSA:

2.7.1.27;
Phylogenetic Tree:

2.7.1.27;
Uniprot:
M-CSA:
RHEA:20708 ATP + erythritol = ADP + D-erythritol 4-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
Purification and properties of erythritol kinase from Propionibacterium pentosaceum.HOLTEN D, FROMM HJ1961 Oct13908588
Functional expression and characterization of EryA, the erythritol kinase of Brucella abortus, and enzymatic synthesis of L-erythritol-4-phosphate.Lillo AM, Tetzlaff CN, Sangari FJ, Cane DE2003 Feb 2412639570