Literature summary for 1.14.19.9 extracted from

Yeh, E.; Blasiak, L.C.; Koglin, A.; Drennan, C.L.; Walsh, C.T.
Chlorination by a long-lived intermediate in the mechanism of flavin-dependent halogenases (2007), Biochemistry, 46, 1284-1292.

Search for more literature for 1.14.19.9

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Protein Variants

Protein Variants	Comment	Organism
K79A	inactive mutant with abolished FAD binding	Lentzea aerocolonigenes
K79M	inactive mutant with abolished FAD binding	Lentzea aerocolonigenes

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	kinetics analysis of apo-enzyme and ligand-bound enzyme	Lentzea aerocolonigenes

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
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	-	?

Organism

Organism	UniProt	Comment	Textmining
Lentzea aerocolonigenes	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
tryptophan + FADH2 + chloride + O2 + H+ = 7-chloro-L-tryptophan + FAD + 2 H2O	reaction mechanism	Lentzea aerocolonigenes	a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
0.17	-	4°C	Lentzea aerocolonigenes
0.29	-	25°C	Lentzea aerocolonigenes

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
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	-	?
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	-	?

Synonyms

Synonyms	Comment	Organism
flavin-dependent halogenase	-	Lentzea aerocolonigenes
RebH	-	Lentzea aerocolonigenes

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
25	-	assay at	Lentzea aerocolonigenes

Cofactor

Cofactor	Comment	Organism	Structure
FAD	dependent on, binding structure, overview	Lentzea aerocolonigenes

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Release 2023.1 (January 2023)