EC number:3.1.3.105

Enzyme

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EC Tree
     3. Hydrolases
        3.1 Acting on ester bonds
            3.1.3 Phosphoric-monoester hydrolases
ID:3.1.3.105
Description:N-acetyl-D-muramate 6-phosphate phosphatase.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 3.1.3.105
BRENDA Enzyme Link: BRENDA 3.1.3.105
KEGG Enzyme Link: KEGG3.1.3.105
BioCyc Enzyme Link: BioCyc 3.1.3.105
ExPASy Enzyme Link: ExPASy3.1.3.105
EC2PDB Enzyme Link: EC2PDB 3.1.3.105
ExplorEnz Enzyme Link: ExplorEnz 3.1.3.105
PRIAM enzyme-specific profiles Link: PRIAM 3.1.3.105
IntEnz Enzyme Link: IntEnz 3.1.3.105
MEDLINE Enzyme Link: MEDLINE 3.1.3.105

EC number:3.1.3.105

MSA:

3.1.3.105;
Phylogenetic Tree:

3.1.3.105;
Uniprot:
M-CSA:
RHEA:53728 H2O + N-acetyl-D-muramate 6-phosphate = N-acetyl-D-muramate + phosphate
RULE(radius=1) [*:1]-[O;H0;+0:2]-[P;H0;+0:3](=[*:4])(-[*:5])-[*:6].[OH2;+0:7]>>[*:1]-[OH;+0:2].[*:4]=[P;H0;+0:3](-[*:5])(-[*:6])-[OH;+0:7]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
The <i>N</i>-Acetylmuramic Acid 6-Phosphate Phosphatase MupP Completes the <i>Pseudomonas</i> Peptidoglycan Recycling Pathway Leading to Intrinsic Fosfomycin Resistance.Borisova M, Gisin J, Mayer C2017 Mar 2828351914