Enzyme

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     3. Hydrolases
        3.1 Acting on ester bonds
            3.1.3 Phosphoric-monoester hydrolases
ID:3.1.3.75
Description:Phosphoethanolamine/phosphocholine phosphatase.
Alternative Name: PHOSPHO1.
3X11A.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 3.1.3.75
BRENDA Enzyme Link: BRENDA 3.1.3.75
KEGG Enzyme Link: KEGG3.1.3.75
BioCyc Enzyme Link: BioCyc 3.1.3.75
ExPASy Enzyme Link: ExPASy3.1.3.75
EC2PDB Enzyme Link: EC2PDB 3.1.3.75
ExplorEnz Enzyme Link: ExplorEnz 3.1.3.75
PRIAM enzyme-specific profiles Link: PRIAM 3.1.3.75
IntEnz Enzyme Link: IntEnz 3.1.3.75
MEDLINE Enzyme Link: MEDLINE 3.1.3.75
MSA:

3.1.3.75;

Phylogenetic Tree:

3.1.3.75;

Uniprot:
M-CSA:
RHEA:16089 H2O + phosphoethanolamine = ethanolamine + phosphate
RULE(radius=1) [*:1]=[P;H0;+0:2](-[*:3])(-[*:4])-[O;H0;+0:5]-[*:6].[OH2;+0:7]>>[*:6]-[OH;+0:5].[*:1]=[P;H0;+0:2](-[*:3])(-[*:4])-[OH;+0:7]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Identification and cloning of a novel phosphatase expressed at high levels in differentiating growth plate chondrocytes.Houston B, Seawright E, Jefferies D, Hoogland E, Lester D, Whitehead C, Farquharson C1999 Jan 119990301
Phosphorylcholine Phosphatase: A Peculiar Enzyme of Pseudomonas aeruginosa.Domenech CE, Otero LH, Beassoni PR, Lisa AT201121915373
Probing the substrate specificities of human PHOSPHO1 and PHOSPHO2.Roberts SJ, Stewart AJ, Schmid R, Blindauer CA, Bond SR, Sadler PJ, Farquharson C2005 Aug 3116054448
Human PHOSPHO1 exhibits high specific phosphoethanolamine and phosphocholine phosphatase activities.Roberts SJ, Stewart AJ, Sadler PJ, Farquharson C2004 Aug 1515175005
Comparative modelling of human PHOSPHO1 reveals a new group of phosphatases within the haloacid dehalogenase superfamily.Stewart AJ, Schmid R, Blindauer CA, Paisey SJ, Farquharson C2003 Dec14983068

RHEA:10492 H2O + phosphocholine = choline + phosphate
RULE(radius=1) [*:1]=[P;H0;+0:2](-[*:3])(-[*:4])-[O;H0;+0:5]-[*:6].[OH2;+0:7]>>[*:6]-[OH;+0:5].[*:1]=[P;H0;+0:2](-[*:3])(-[*:4])-[OH;+0:7]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Identification and cloning of a novel phosphatase expressed at high levels in differentiating growth plate chondrocytes.Houston B, Seawright E, Jefferies D, Hoogland E, Lester D, Whitehead C, Farquharson C1999 Jan 119990301
Phosphorylcholine Phosphatase: A Peculiar Enzyme of Pseudomonas aeruginosa.Domenech CE, Otero LH, Beassoni PR, Lisa AT201121915373
Probing the substrate specificities of human PHOSPHO1 and PHOSPHO2.Roberts SJ, Stewart AJ, Schmid R, Blindauer CA, Bond SR, Sadler PJ, Farquharson C2005 Aug 3116054448
Human PHOSPHO1 exhibits high specific phosphoethanolamine and phosphocholine phosphatase activities.Roberts SJ, Stewart AJ, Sadler PJ, Farquharson C2004 Aug 1515175005
Comparative modelling of human PHOSPHO1 reveals a new group of phosphatases within the haloacid dehalogenase superfamily.Stewart AJ, Schmid R, Blindauer CA, Paisey SJ, Farquharson C2003 Dec14983068