Enzyme

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EC Tree
     3. Hydrolases
        3.1 Acting on ester bonds
            3.1.3 Phosphoric-monoester hydrolases
ID:3.1.3.22
Description:Mannitol-1-phosphatase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 3.1.3.22
BRENDA Enzyme Link: BRENDA 3.1.3.22
KEGG Enzyme Link: KEGG3.1.3.22
BioCyc Enzyme Link: BioCyc 3.1.3.22
ExPASy Enzyme Link: ExPASy3.1.3.22
EC2PDB Enzyme Link: EC2PDB 3.1.3.22
ExplorEnz Enzyme Link: ExplorEnz 3.1.3.22
PRIAM enzyme-specific profiles Link: PRIAM 3.1.3.22
IntEnz Enzyme Link: IntEnz 3.1.3.22
MEDLINE Enzyme Link: MEDLINE 3.1.3.22
MSA:

3.1.3.22;

Phylogenetic Tree:

3.1.3.22;

Uniprot:
M-CSA:
RHEA:19537 D-mannitol 1-phosphate + H2O = D-mannitol + 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
Molecular cloning and functional expression of mannitol-1-phosphatase from the apicomplexan parasite Eimeria tenella.Liberator P, Anderson J, Feiglin M, Sardana M, Griffin P, Schmatz D, Myers RW1998 Feb 139461622
Enzymatic studies on mannitol formation by Piricularia oryzae.YAMADA H, OKAMOTO K, KODAMA K, NOGUCHI F, TANAKA S1961 May13787089
A pathway for photosynthetic carbon flow to mannitol in celery leaves : activity and localization of key enzymes.Rumpho ME, Edwards GE, Loescher WH1983 Dec16663332