7-Chloro-L-tryptophan oxidase
| 7-chloro-L-tryptophan oxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.4.3.23 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
7-Chloro-L-tryptophan oxidase (EC 1.4.3.23, RebO) is an enzyme with systematic name 7-chloro-L-tryptophan:oxygen oxidoreductase.[1] This enzyme catalyses the following chemical reaction
7-chloro-L-tryptophan
O2
H2O2
O2
H2O2
propionate.svg.png)
2-iminio-3-(7-chloroindol-3-yl)propionate
The two substrates of this enzyme are 7-chloro-L-tryptophan and oxygen. Its products are 2-iminio-3-(7-chloroindol-3-yl)propionate and hydrogen peroxide. It contains a noncovalently bound flavin adenine dinucleotide. The rection is a step in the biosynthesis of rebeccamycin in the bacterium Lechevalieria aerocolonigenes.[2][3]
References
- ^ Nishizawa T, Aldrich CC, Sherman DH (March 2005). "Molecular analysis of the rebeccamycin L-amino acid oxidase from Lechevalieria aerocolonigenes ATCC 39243". Journal of Bacteriology. 187 (6): 2084–92. doi:10.1128/JB.187.6.2084-2092.2005. PMC 1064027. PMID 15743957.
- ^ Enzyme 1.4.3.23 at KEGG Pathway Database.
- ^ Howard-Jones AR, Walsh CT (December 2005). "Enzymatic genеration 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.
External links
- 7-chloro-L-tryptophan+oxidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)