EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.14.19.9 | apo-enzyme or enzyme bound to FAD or L-tryptophan, X-ray diffraction structure determination and analysis at 2.08-2.3 A resolution | Lentzea aerocolonigenes |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.14.19.9 | K79A | inactive mutant with abolished FAD binding | Lentzea aerocolonigenes |
1.14.19.9 | K79M | inactive mutant with abolished FAD binding | Lentzea aerocolonigenes |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.14.19.9 | additional information | - |
additional information | kinetics analysis of apo-enzyme and ligand-bound enzyme | Lentzea aerocolonigenes |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.19.9 | L-tryptophan + FADH2 + Cl- + O2 | Lentzea aerocolonigenes | formation of 7-chlorotryptophan as the initial step in the biosynthesis of antitumor agent rebeccamycin | 7-chloro-L-tryptophan + FAD + H2O | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.19.9 | Lentzea aerocolonigenes | - |
- |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.14.19.9 | tryptophan + FADH2 + chloride + O2 + H+ = 7-chloro-L-tryptophan + FAD + 2 H2O | reaction mechanism | Lentzea aerocolonigenes |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
1.14.19.9 | 0.17 | - |
4°C | Lentzea aerocolonigenes |
1.14.19.9 | 0.29 | - |
25°C | Lentzea aerocolonigenes |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.19.9 | L-tryptophan + FADH2 + Cl- + O2 | formation of 7-chlorotryptophan as the initial step in the biosynthesis of antitumor agent rebeccamycin | Lentzea aerocolonigenes | 7-chloro-L-tryptophan + FAD + H2O | - |
? | |
1.14.19.9 | L-tryptophan + FADH2 + Cl- + O2 | reaction of FADH2, Cl-, and O2 in the active site, involving active site Lys79, generates the powerful oxidant HOCl, which was presumed to carry out the chlorination reaction, formation of a long-living chlorinating intermediate, which remains on the enzyme after removal of FAD and transfers chlorine to tryptophan with kinetically competent rates, substrate binding structure, overview | Lentzea aerocolonigenes | 7-chloro-L-tryptophan + FAD + H2O | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.14.19.9 | flavin-dependent halogenase | - |
Lentzea aerocolonigenes |
1.14.19.9 | RebH | - |
Lentzea aerocolonigenes |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.14.19.9 | 25 | - |
assay at | Lentzea aerocolonigenes |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.14.19.9 | FAD | dependent on, binding structure, overview | Lentzea aerocolonigenes |