Dichlorochromopyrrolate synthase
| Dichlorochromopyrrolate synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.21.3.9 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Dichlorochromopyrrolate synthase (EC 1.21.3.9, RebD, dichlorochromopyrrolic acid synthase) is an enzyme with systematic name 2-imino-3-(7-chloroindol-3-yl)propanoate ammonia-lyase (dichlorochromopyrrolate-forming).[1][2] This enzyme catalyses the following chemical reaction
4
propionate.svg.png)
2-iminio-3-(7-chloroindol-3-yl)propionate
O2
2 H2O
2
-1H-pyrrole-2%252C5-dicarboxylic_acid.svg.png)
dichlorochromopyrrolic acid
+ 2 NH3
This enzyme catalyses a step in the biosynthesis of rebeccamycin.[3]
References
- ↑ Nishizawa T, Grüschow S, Jayamaha DH, Nishizawa-Harada C, Sherman DH (January 2006). "Enzymatic assembly of the bis-indole core of rebeccamycin". Journal of the American Chemical Society. 128 (3): 724–5. Bibcode:2006JAChS.128..724N. doi:10.1021/ja056749x. PMID 16417354.
- ↑ Howard-Jones AR, Walsh CT (December 2005). "Enzymatic generation of the chromopyrrolic acid scaffold of rebeccamycin by the tandem action of RebO and RebD". Biochemistry. 44 (48): 15652–63. CiteSeerX 10.1.1.537.5773. doi:10.1021/bi051706e. PMID 16313168.
{{cite journal}}: Cite uses deprecated parameter|citeseerx=(help) - ↑ Pommerehne, Kathrin; Walisko, Jana; Ebersbach, Anna; Krull, Rainer (2019). "The antitumor antibiotic rebeccamycin—challenges and advanced approaches in production processes". Applied Microbiology and Biotechnology. 103 (9): 3627–3636. doi:10.1007/s00253-019-09741-y. PMID 30888461.
External links
- Chromopyrrolate+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
Category: