Biology:7-Chloro-L-tryptophan oxidase
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Short description: Class of enzymes
| 7-chloro-L-tryptophan oxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 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][2] This enzyme catalyses the following chemical reaction
- 7-chloro-L-tryptophan + O2 [math]\displaystyle{ \rightleftharpoons }[/math] 2-imino-3-(7-chloroindol-3-yl)propanoate + H2O2
This enzyme contains a noncovalently bound FAD.
References
- ↑ "Molecular analysis of the rebeccamycin L-amino acid oxidase from Lechevalieria aerocolonigenes ATCC 39243". Journal of Bacteriology 187 (6): 2084–92. March 2005. doi:10.1128/JB.187.6.2084-2092.2005. PMID 15743957.
- ↑ "Enzymatic genеration of the chromopyrrolic acid scaffold of rebeccamycin by the tandem action of RebO and RebD". Biochemistry 44 (48): 15652–63. December 2005. doi:10.1021/bi051706e. PMID 16313168.
External links
- 7-chloro-L-tryptophan+oxidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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