2-Amino-4-deoxychorismate dehydrogenase
(Redirected from 2-amino-4-deoxychorismate dehydrogenase)
2-Amino-4-deoxychorismate dehydrogenase (EC 1.3.99.24, 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
| 2-amino-4-deoxychorismate dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.3.99.24 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
- (2S)-2-amino-4-deoxychorismate + FMN 3-(1-carboxyvinyloxy)anthranilate + FMNH2
This enzyme participates in the formation of the benzoxazolinate moiety of the enediyne antitumour antibiotic C-1027].
References
edit- ^ 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. doi:10.1021/ja00139a032.
External links
edit- 2-amino-4-deoxychorismate+dehydrogenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
