EC Tree |
3. Hydrolases |
3.6 Acting on acid anhydrides |
3.6.1 In phosphorus-containing anhydrides |
ID: | 3.6.1.2 |
---|---|
Description: | Trimetaphosphatase. |
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Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.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 |
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 |
Title | Authors | Date | PubMed ID |
---|---|---|---|
Tripolyphosphate and trimetaphosphate in yeast extracts. | KORNBERG SR | 1956 Jan | 13278311 |
Heat of hydrolysis of trimetaphosphate. | MEYERHOF O, SHATAS R, KAPLAN A | 1953 Sep-Oct | 13115420 |