2-Amino-4-deoxychorismate dehydrogenase
| 2-amino-4-deoxychorismate dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.3.8.16 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
2-Amino-4-deoxychorismate dehydrogenase (EC 1.3.8.16, ADIC dehydrogenase, 2-amino-2-deoxyisochorismate dehydrogenase, SgcG) is an enzyme with systematic name (2S)-2-amino-4-deoxychorismate:FMN oxidoreductase.[1][2] This enzyme catalyses the following chemical reaction
(1)
+ FMN
(2)
+ FMNH2
It converts 2-amino-2-deoxyisochorismic acid (1) into 3-(1-carboxyvinyloxy)anthranilic acid (2) by oxidation using flavin mononucleotide (FMN) as its cofactor.[3]
This reaction is part of the biosynthesis of the benzoxazolinate moiety of the enediyne antitumour antibiotic C-1027 from Streptomyces globisporus. The intermediate acid (1) is produced from chorismic acid by the enzyme 2-amino-4-deoxychorismate synthase:[1]
References
- ^ a b Van Lanen SG, Lin S, Shen B (January 2008). "Biosynthesis of the enediyne antitumor antibiotic C-1027 involves a new branching point in chorismate metabolism". Proceedings of the National Academy of Sciences of the United States of America. 105 (2): 494–9. Bibcode:2008PNAS..105..494V. doi:10.1073/pnas.0708750105. PMC 2206564. PMID 18182490.
- ^ Yu L, Mah S, Otani T, Dedon P (1995). "The benzoxazolinate of C-1027 confers intercalative DNA binding". J. Am. Chem. Soc. 117 (34): 8877–8878. Bibcode:1995JAChS.117.8877Y. doi:10.1021/ja00139a032.
- ^ Enzyme 1.3.99.24 at KEGG Pathway Database.
External links
- 2-amino-4-deoxychorismate+dehydrogenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)