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show all sequences of 1.14.19.B5

Tandem action of the O2- and FADH2-dependent halogenases KtzQ and KtzR produce 6,7-dichlorotryptophan for kutzneride assembly

Heemstra, J.R. Jr.; Walsh, C.T.; J. Am. Chem. Soc. 130, 14024-14025 (2008)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
-
Kutzneria sp. 744
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.114
-
7-chloro-L-tryptophan
pH 7.0, 22°C
Kutzneria sp. 744
0.808
-
L-tryptophan
pH 7.0, 22°C
Kutzneria sp. 744
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
7-chloro-L-tryptophan + FADH2 + Cl- + O2 + H+
Kutzneria sp. 744
the enzyme is involved in the biosynthesis of 6,7-dichloro-L-tryptophan, a component of kutznerides (antifungal nonribosomal hexadepsipeptides)
6,7-dichloro-L-tryptophan + FAD + 2 H2O
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Kutzneria sp. 744
A8CF74
-
-
Purification (Commentary)
Commentary
Organism
-
Kutzneria sp. 744
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
7-chloro-L-tryptophan + FADH2 + Cl- + O2 + H+
-
727660
Kutzneria sp. 744
6,7-dichloro-L-tryptophan + FAD + 2 H2O
-
-
-
?
7-chloro-L-tryptophan + FADH2 + Cl- + O2 + H+
the enzyme is involved in the biosynthesis of 6,7-dichloro-L-tryptophan, a component of kutznerides (antifungal nonribosomal hexadepsipeptides)
727660
Kutzneria sp. 744
6,7-dichloro-L-tryptophan + FAD + 2 H2O
-
-
-
?
L-tryptophan + FADH2 + Cl- + O2 + H+
kcat/Km for the halogenation of L-tryptophan is less than 1% compared to the value for the halogenation 7-chloro-L-tryptophan
727660
Kutzneria sp. 744
6-chloro-L-tryptophan + FAD + 2 H2O
-
-
-
?
additional information
KtzR is not active for introduction of chloride to piperazic acid or gamma,delta-dehydropiperazic acid
727660
Kutzneria sp. 744
?
-
-
-
-
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
22
-
assay at
Kutzneria sp. 744
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.0013
-
L-tryptophan
pH 7.0, 22°C
Kutzneria sp. 744
0.023
-
7-chloro-L-tryptophan
pH 7.0, 22°C
Kutzneria sp. 744
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Kutzneria sp. 744
Cloned(Commentary) (protein specific)
Commentary
Organism
-
Kutzneria sp. 744
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.114
-
7-chloro-L-tryptophan
pH 7.0, 22°C
Kutzneria sp. 744
0.808
-
L-tryptophan
pH 7.0, 22°C
Kutzneria sp. 744
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
7-chloro-L-tryptophan + FADH2 + Cl- + O2 + H+
Kutzneria sp. 744
the enzyme is involved in the biosynthesis of 6,7-dichloro-L-tryptophan, a component of kutznerides (antifungal nonribosomal hexadepsipeptides)
6,7-dichloro-L-tryptophan + FAD + 2 H2O
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
-
Kutzneria sp. 744
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
7-chloro-L-tryptophan + FADH2 + Cl- + O2 + H+
-
727660
Kutzneria sp. 744
6,7-dichloro-L-tryptophan + FAD + 2 H2O
-
-
-
?
7-chloro-L-tryptophan + FADH2 + Cl- + O2 + H+
the enzyme is involved in the biosynthesis of 6,7-dichloro-L-tryptophan, a component of kutznerides (antifungal nonribosomal hexadepsipeptides)
727660
Kutzneria sp. 744
6,7-dichloro-L-tryptophan + FAD + 2 H2O
-
-
-
?
L-tryptophan + FADH2 + Cl- + O2 + H+
kcat/Km for the halogenation of L-tryptophan is less than 1% compared to the value for the halogenation 7-chloro-L-tryptophan
727660
Kutzneria sp. 744
6-chloro-L-tryptophan + FAD + 2 H2O
-
-
-
?
additional information
KtzR is not active for introduction of chloride to piperazic acid or gamma,delta-dehydropiperazic acid
727660
Kutzneria sp. 744
?
-
-
-
-
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
22
-
assay at
Kutzneria sp. 744
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.0013
-
L-tryptophan
pH 7.0, 22°C
Kutzneria sp. 744
0.023
-
7-chloro-L-tryptophan
pH 7.0, 22°C
Kutzneria sp. 744
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Kutzneria sp. 744
General Information
General Information
Commentary
Organism
physiological function
the enzyme is involved in the biosynthesis of 6,7-dichloro-L-tryptophan, a component of kutznerides (antifungal nonribosomal hexadepsipeptides)
Kutzneria sp. 744
General Information (protein specific)
General Information
Commentary
Organism
physiological function
the enzyme is involved in the biosynthesis of 6,7-dichloro-L-tryptophan, a component of kutznerides (antifungal nonribosomal hexadepsipeptides)
Kutzneria sp. 744
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.0016
-
L-tryptophan
pH 7.0, 22°C
Kutzneria sp. 744
0.2
-
7-chloro-L-tryptophan
pH 7.0, 22°C
Kutzneria sp. 744
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.0016
-
L-tryptophan
pH 7.0, 22°C
Kutzneria sp. 744
0.2
-
7-chloro-L-tryptophan
pH 7.0, 22°C
Kutzneria sp. 744
Other publictions for EC 1.14.19.B5
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)
727660
Heemstra
Tandem action of the O2- and F ...
Kutzneria sp. 744
J. Am. Chem. Soc.
130
14024-14025
2008
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