BRENDA - Enzyme Database
show all sequences of 1.14.19.9

Chlorination by a long-lived intermediate in the mechanism of flavin-dependent halogenases

Yeh, E.; Blasiak, L.C.; Koglin, A.; Drennan, C.L.; Walsh, C.T.; Biochemistry 46, 1284-1292 (2007)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization
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
Lechevalieria aerocolonigenes
Engineering
Amino acid exchange
Commentary
Organism
K79A
inactive mutant with abolished FAD binding
Lechevalieria aerocolonigenes
K79M
inactive mutant with abolished FAD binding
Lechevalieria aerocolonigenes
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetics analysis of apo-enzyme and ligand-bound enzyme
Lechevalieria aerocolonigenes
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-tryptophan + FADH2 + Cl- + O2
Lechevalieria aerocolonigenes
formation of 7-chlorotryptophan as the initial step in the biosynthesis of antitumor agent rebeccamycin
7-chloro-L-tryptophan + FAD + H2O
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Lechevalieria aerocolonigenes
-
-
-
Reaction
Reaction
Commentary
Organism
tryptophan + FADH2 + chloride + O2 + H+ = 7-chloro-L-tryptophan + FAD + 2 H2O
reaction mechanism
Lechevalieria aerocolonigenes
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.17
-
4°C
Lechevalieria aerocolonigenes
0.29
-
25°C
Lechevalieria aerocolonigenes
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-tryptophan + FADH2 + Cl- + O2
formation of 7-chlorotryptophan as the initial step in the biosynthesis of antitumor agent rebeccamycin
685105
Lechevalieria 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
685105
Lechevalieria aerocolonigenes
7-chloro-L-tryptophan + FAD + H2O
-
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Lechevalieria aerocolonigenes
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
dependent on, binding structure, overview
Lechevalieria aerocolonigenes
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
dependent on, binding structure, overview
Lechevalieria aerocolonigenes
Crystallization (Commentary) (protein specific)
Crystallization
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
Lechevalieria aerocolonigenes
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
K79A
inactive mutant with abolished FAD binding
Lechevalieria aerocolonigenes
K79M
inactive mutant with abolished FAD binding
Lechevalieria aerocolonigenes
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetics analysis of apo-enzyme and ligand-bound enzyme
Lechevalieria aerocolonigenes
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-tryptophan + FADH2 + Cl- + O2
Lechevalieria aerocolonigenes
formation of 7-chlorotryptophan as the initial step in the biosynthesis of antitumor agent rebeccamycin
7-chloro-L-tryptophan + FAD + H2O
-
-
?
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.17
-
4°C
Lechevalieria aerocolonigenes
0.29
-
25°C
Lechevalieria aerocolonigenes
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-tryptophan + FADH2 + Cl- + O2
formation of 7-chlorotryptophan as the initial step in the biosynthesis of antitumor agent rebeccamycin
685105
Lechevalieria 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
685105
Lechevalieria aerocolonigenes
7-chloro-L-tryptophan + FAD + H2O
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Lechevalieria aerocolonigenes
Other publictions for EC 1.14.19.9
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
746470
Karabencheva-Christova
Mechanistic insights into the ...
Pseudomonas fluorescens
Sci. Rep.
7
17395
2017
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1
1
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744565
Fraebel
Recombinant flavin-dependent ...
Lechevalieria aerocolonigenes
Biotechnol. J.
11
1586-1594
2016
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744027
Frese
Enzymatic halogenation of try ...
Lechevalieria aerocolonigenes
Angew. Chem. Int. Ed. Engl.
54
298-301
2015
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1
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744712
Frese
-
Regioselective enzymatic halo ...
Lechevalieria aerocolonigenes
ChemCatChem
6
1270-1276
2014
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1
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7
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1
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7
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1
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1
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726682
Lang
Changing the regioselectivity ...
Pseudomonas fluorescens
Angew. Chem. Int. Ed. Engl.
50
2951-2953
2011
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1
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4
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4
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1
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4
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727668
Glenn
Reengineering a tryptophan hal ...
Lechevalieria aerocolonigenes
J. Am. Chem. Soc.
133
19346-19349
2011
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1
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695031
Bitto
The structure of flavin-depend ...
Lechevalieria aerocolonigenes
Proteins
70
289-293
2008
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1
1
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695061
Bitto
The structure of flavin-depend ...
Lechevalieria aerocolonigenes
Proteins Struct. Funct. Genet.
70
289-293
2008
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1
1
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745152
Heemstra
Tandem action of the O2- and ...
Kutzneria sp. 744
J. Am. Chem. Soc.
130
14024-14025
2008
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3
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1
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2
2
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685105
Yeh
Chlorination by a long-lived i ...
Lechevalieria aerocolonigenes
Biochemistry
46
1284-1292
2007
-
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1
2
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1
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1
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1
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1
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2
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2
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1
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1
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1
1
2
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1
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1
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2
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2
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1
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672189
Yeh
Flavin redox chemistry precede ...
Lechevalieria aerocolonigenes
Biochemistry
45
7904-7912
2006
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1
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1
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2
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1
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1
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1
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1
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2
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3
1
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690566
van Pee
Flavin-dependent halogenases i ...
Lechevalieria aerocolonigenes, Pseudomonas fluorescens
Appl. Microbiol. Biotechnol.
70
631-641
2006
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671187
Unversucht
-
FADH2-dependence of tryptophan ...
Pseudomonas fluorescens
Adv. Synth. Catal.
347
1163-1167
2005
-
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1
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1
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676785
Yeh
Robust in vitro activity of Re ...
Lechevalieria aerocolonigenes, Lechevalieria aerocolonigenes 39243
Proc. Natl. Acad. Sci. USA
102
3960-3965
2005
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1
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6
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1
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677119
Dong
Tryptophan 7-halogenase (PrnA) ...
Pseudomonas fluorescens
Science
309
2216-2219
2005
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671039
Dong
Crystallization and X-ray diff ...
Pseudomonas fluorescens
Acta Crystallogr. Sect. D
60
1438-1440
2004
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690305
Hölzer
-
Substrate specificity and regi ...
Pseudomonas fluorescens, Pseudomonas fluorescens BL915
Adv. Synth. Catal.
343
591-595
2001
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690425
Keller
Purification and Partial Chara ...
Pseudomonas fluorescens
Angew. Chem. Int. Ed. Engl.
39
2300-2302
2000
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692818
Kirner
Functions encoded by pyrrolnit ...
Pseudomonas fluorescens
J. Bacteriol.
180
1939-1943
1998
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690514
Hammer
Four genes from Pseudomonas fl ...
Pseudomonas fluorescens
Appl. Environ. Microbiol.
63
2147-2154
1997
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