Enzyme

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EC Tree
     3. Hydrolases
        3.6 Acting on acid anhydrides
            3.6.1 In phosphorus-containing anhydrides
ID:3.6.1.2
Description:Trimetaphosphatase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 3.6.1.2
BRENDA Enzyme Link: BRENDA 3.6.1.2
KEGG Enzyme Link: KEGG3.6.1.2
BioCyc Enzyme Link: BioCyc 3.6.1.2
ExPASy Enzyme Link: ExPASy3.6.1.2
EC2PDB Enzyme Link: EC2PDB 3.6.1.2
ExplorEnz Enzyme Link: ExplorEnz 3.6.1.2
PRIAM enzyme-specific profiles Link: PRIAM 3.6.1.2
IntEnz Enzyme Link: IntEnz 3.6.1.2
MEDLINE Enzyme Link: MEDLINE 3.6.1.2
MSA:

3.6.1.2;

Phylogenetic Tree:

3.6.1.2;

Uniprot:
M-CSA:
RHEA:11088 H2O + trimetaphosphate = 2 H(+) + triphosphate
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
Tripolyphosphate and trimetaphosphate in yeast extracts.KORNBERG SR1956 Jan13278311
Heat of hydrolysis of trimetaphosphate.MEYERHOF O, SHATAS R, KAPLAN A1953 Sep-Oct13115420