Global InformationAminodeoxychorismate synthase information
| 4-amino-4-deoxychorismate synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Aminodeoxychorismate synthase | |||||||||
| Identifiers | |||||||||
| EC no. | 2.6.1.85 | ||||||||
| CAS no. | 132264-37-0 | ||||||||
| 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 aminodeoxychorismate synthase (EC 2.6.1.85) is an enzyme that catalyzes the chemical reaction
- chorismate + L-glutamine 4-amino-4-deoxychorismate + L-glutamate
Thus, the two substrates of this enzyme are chorismate and L-glutamine, whereas its two products are 4-amino-4-deoxychorismate and L-glutamate.[1][2][3][4]
It is part of a pathway for the biosynthesis of para-aminobenzoic acid (PABA); a precursor for the production of folates. Folates are family of cofactors that are essential for living organisms. Folate cofactors are used in several one-carbon transfer reactions required during the synthesis of essential metabolites, including methionine and thymidylate.[1]
Aminodeoxychorismate synthase (PabB), a 51 kDa protein in E. coli, is encoded by the gene pabB.[2] 4-amino-4-deoxychorismate, the product of PabB, can be converted to para-aminobenzoic acid by the enzyme 4-amino-4-deoxychorismate lyase (PabC).
- ^ a b SAHR, Tobias (May 15, 2006). "Folate synthesis in plants: purification, kinetic properties, and inhibition of aminodeoxychorismate synthase". Biochem. J. 396 (1): 157–62. doi:10.1042/BJ20051851. PMC 1449997. PMID 16466344.
- ^ a b Ye, Qi-Zhuang (August 23, 1990). "p-Aminobenzoate synthesis in Escherichia coli: Purification and characterization of PabB as aminodeoxychorosmate synthase and enzyme X as aminodeoxychorismate lyase". Proc Natl Acad Sci USA. 87 (23): 9391–5. Bibcode:1990PNAS...87.9391Y. doi:10.1073/pnas.87.23.9391. PMC 55171. PMID 2251281.
- ^ Parsons, James (November 21, 2001). "Structure of Escherichia coli Aminodeoxychorismate Synthase: Architectural Conservation and Diversity in Chorismate-Utilizing Enzymes". Biochemistry. 41 (7): 2198–2208. doi:10.1021/bi015791b. PMID 11841211.
- ^ Bera, Asim (December 21, 2013). "Structure of Aminodeoxychorismate Synthase from Stenotrophomonas maltophilia". Biochemistry. 51 (51): 10208–17. doi:10.1021/bi301243v. PMC 3532939. PMID 23230967.