Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Unversucht, S.; Hollmann, F.; Schmid, A.; van Pee, K.
    FADH2-dependence of tryptophan 7-halogenase (2005), Adv. Synth. Catal., 347, 1163-1167.
No PubMed abstract available

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.19.9 formate complete loss of activity above 200 mM Pseudomonas fluorescens

Organism

EC Number Organism UniProt Comment Textmining
1.14.19.9 Pseudomonas fluorescens
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.14.19.9 tryptophan + FADH2 + chloride + O2 + H+ = 7-chloro-L-tryptophan + FAD + 2 H2O monooxygenase-like mechanism proposed. First, FADH2 is produced by a flavin reductase using NADH. FADH2 binds to flavin-free enzyme and reacts to enzyme-bound 4alpha-flavin hydroperoxide which attacks L-tryptophan. Activated tryptophan is attacked by chloride as a nucleophile, the resulting halohydrin is dehydrated to the end product 7-chlorotryptophan Pseudomonas fluorescens
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.19.9 L-tryptophan + FADH2 + Cl- + O2 + H+ regioselective reaction Pseudomonas fluorescens 7-chloro-L-tryptophan + FAD + H2O
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.14.19.9 0.0018
-
 (25R)-3beta-hydroxycholest-5-en-27-oate pH 7.2, 30°C, in vitro two-component system of enzyme and flavin reductase to provide FADH2 Pseudomonas fluorescens

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.19.9 FADH2 required, purified enzyme does not contain flavin. FADH2 may be provided by a flavin reductase or by regeneration via the organometallic complex (pentamethylcyclopentadienyl)rhodium-bipyridine Pseudomonas fluorescens