EC Tree |
2. Transferases |
2.7 Transferring phosphorus-containing groups |
2.7.8 Transferases for other substituted phosphate groups |
ID: | 2.7.8.37 |
---|---|
Description: | Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase. |
Cath: | 3.40.50.11310; |
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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 2.7.8.37 |
BRENDA Enzyme Link: | BRENDA 2.7.8.37 |
KEGG Enzyme Link: | KEGG2.7.8.37 |
BioCyc Enzyme Link: | BioCyc 2.7.8.37 |
ExPASy Enzyme Link: | ExPASy2.7.8.37 |
EC2PDB Enzyme Link: | EC2PDB 2.7.8.37 |
ExplorEnz Enzyme Link: | ExplorEnz 2.7.8.37 |
PRIAM enzyme-specific profiles Link: | PRIAM 2.7.8.37 |
IntEnz Enzyme Link: | IntEnz 2.7.8.37 |
MEDLINE Enzyme Link: | MEDLINE 2.7.8.37 |
RHEA:34679 | ATP + methylphosphonate = adenine + alpha-D-ribose 1-methylphosphonate 5-triphosphate |
RULE(radius=1) | [*:1]-[CH;+0:2](-[*:3])-[n;H0;+0:4](:[*:5]):[*:6].[*:7]-[OH;+0:8]>>[*:1]-[CH;+0:2](-[*:3])-[O;H0;+0:8]-[*:7].[*:5]:[nH;+0:4]:[*:6] |
Reaction | ![]() |
Core-to-Core | |
Core-to-Core |
Title | Authors | Date | PubMed ID |
---|---|---|---|
Intermediates in the transformation of phosphonates to phosphate by bacteria. | Kamat SS, Williams HJ, Raushel FM | 2011 Nov 16 | 22089136 |