BRENDA - Enzyme Database
show all sequences of 1.14.19.9

Purification and Partial Characterization of Tryptophan 7-Halogenase (PrnA) from Pseudomonas fluorescens

Keller, S.; Wage, T.; Hohaus, K.; Hölzer, M.; Eichhorn, E.; van Pee, K.H.; Angew. Chem. Int. Ed. Engl. 39, 2300-2302 (2000)

Data extracted from this reference:

Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-tryptophan + FADH2 + Cl- + O2 + H+
Pseudomonas fluorescens
the enzyme is involved in biosynthesis of pyrrolnitrin
7-chloro-L-tryptophan + FAD + H2O
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas fluorescens
-
-
-
Purification (Commentary)
Commentary
Organism
-
Pseudomonas fluorescens
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
PrnA activities are determined after addition of flavin reductase (SsuE). Without reductase, fractions after elution from the molecular sieve column do not show any activity
Pseudomonas fluorescens
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-tryptophan + FADH2 + Cl- + O2 + H+
the enzyme is involved in biosynthesis of pyrrolnitrin
690425
Pseudomonas fluorescens
7-chloro-L-tryptophan + FAD + H2O
-
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
FADH2
the enzyme is specific for FADH2
Pseudomonas fluorescens
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FADH2
the enzyme is specific for FADH2
Pseudomonas fluorescens
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 + H+
Pseudomonas fluorescens
the enzyme is involved in biosynthesis of pyrrolnitrin
7-chloro-L-tryptophan + FAD + H2O
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
-
Pseudomonas fluorescens
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
PrnA activities are determined after addition of flavin reductase (SsuE). Without reductase, fractions after elution from the molecular sieve column do not show any activity
Pseudomonas fluorescens
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 + H+
the enzyme is involved in biosynthesis of pyrrolnitrin
690425
Pseudomonas fluorescens
7-chloro-L-tryptophan + FAD + H2O
-
-
-
?
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
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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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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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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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695031
Bitto
The structure of flavin-depend ...
Lechevalieria aerocolonigenes
Proteins
70
289-293
2008
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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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745152
Heemstra
Tandem action of the O2- and ...
Kutzneria sp. 744
J. Am. Chem. Soc.
130
14024-14025
2008
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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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672189
Yeh
Flavin redox chemistry precede ...
Lechevalieria aerocolonigenes
Biochemistry
45
7904-7912
2006
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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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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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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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