| EC |
1.14.15.41 |
| Accepted name: |
L-tryptophan 4-nitrase |
| Reaction: |
L-tryptophan + nitric oxide + O2 + reduced ferredoxin + H+ = 4-nitro-L-tryptophan + H2O + oxidized ferredoxin |
| Other name(s): |
txtE (gene name); 4-nitro-L-tryptophane synthase |
| Systematic name: |
L-tryptophan,nitric oxide, reduced ferredoxin:oxygen oxidoreductase (4-nitro-L-tryptophan-forming) |
| Comments: |
A cytochrome P-450 (heme-thiolate) enzyme characterized from the bacterium Streptomyces turgidiscabies. The enzyme participates in biosynthesis of thaxtomins, cyclic dipeptides formed from the condensation of 4-nitro-L-tryptophan and L-phenylalanine that have phytotoxic properties. The enzyme requires ferredoxin as its electron donor and catalyses a reaction in which nitric oxide is oxidized to a nitro group and inserted into L-tryptophan at the 4 position (not necessarily in this order). |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Barry, S.M., Kers, J.A., Johnson, E.G., Song, L., Aston, P.R., Patel, B., Krasnoff, S.B., Crane, B.R., Gibson, D.M., Loria, R. and Challis, G.L. Cytochrome P450-catalyzed L-tryptophan nitration in thaxtomin phytotoxin biosynthesis. Nat. Chem. Biol. 8 (2012) 814–816. [DOI] [PMID: 22941045] |
|
| [EC 1.14.15.41 created 2024] |
| |
|
| |
|
Printable version