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Literature summary for 1.14.19.9 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
Search for more literature for 1.14.19.9

Inhibitors

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

Organism

Organism UniProt Comment Textmining
Pseudomonas fluorescens
-
-
-

Reaction

Reaction Comment Organism Reaction ID
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)

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

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
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

Cofactor Comment Organism Structure
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