Anthranilate adenylyltransferase
| anthranilate adenylyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.7.55 | ||||||||
| CAS no. | 70248-64-5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, an anthranilate adenylyltransferase (EC 2.7.7.55) is an enzyme that catalyzes the chemical reaction
- ATP + anthranilate diphosphate + N-adenylylanthranilate
Thus, the two substrates of this enzyme are ATP and anthranilate, whereas its two products are diphosphate and N-adenylylanthranilate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is ATP:anthranilate N-adenylyltransferase. This enzyme is also called anthranilic acid adenylyltransferase.
References[edit]
- Lerbs W, Luckner M (1985). "Cyclopeptine synthetase activity in surface cultures of Penicillium cyclopium". J. Basic Microbiol. 25 (6): 387–91. doi:10.1002/jobm.3620250611. PMID 2995633.
