BRENDA - Enzyme Database show
show all sequences of 2.6.1.85

Expression and characterization of PhzE from P. aeruginosa PAO1: aminodeoxyisochorismate synthase involved in pyocyanin and phenazine-1-carboxylate production

Culbertson, J.E.; Toney, M.D.; Biochim. Biophys. Acta 1834, 240-246 (2013)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
1-hydroxyphenazine
inhibitory above 0.200 mM
Pseudomonas aeruginosa
additional information
enzyme is not regulated by feedback inhibition. Little or no inhibition up to 1 mM: glyphosate, pyridoxamine 5'-phosphate, pyridoxal 5'-phosphate, and 3-hydroxypyridine-4-carboxylic acid
Pseudomonas aeruginosa
phosphate
phosphate buffer competitively inhibits PhzE, about 20% inhibition with 100 mM potassium phosphate at pH 7.0
Pseudomonas aeruginosa
pyocyanin
inhibitory above 0.250 mM
Pseudomonas aeruginosa
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.02
-
chorismate
cosubstrate L-glutamine, pH 7.0, 25°C
Pseudomonas aeruginosa
0.216
-
chorismate
cosubstrate L-glutamine, pH 7.0, 25°C
Pseudomonas aeruginosa
11
-
L-glutamine
pH 7.0, 25°C
Pseudomonas aeruginosa
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Co2+
-
Pseudomonas aeruginosa
Mg2+
required, Km value 0.29 mM
Pseudomonas aeruginosa
Mn2+
-
Pseudomonas aeruginosa
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
71251
-
-
Pseudomonas aeruginosa
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas aeruginosa
Q7DC81
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
chorismate + L-glutamine
-
724464
Pseudomonas aeruginosa
L-glutamate + 4-amino-4-deoxychorismate
-
-
-
?
chorismate + NH3
-
724464
Pseudomonas aeruginosa
4-amino-4-deoxychorismate + H2O
-
-
-
?
additional information
isoform PhzE catalyzes the addition of ammonia to C2 of chorismate, as does anthranilate synthase, yet unlike anthranilate synthase it does not catalyze elimination of pyruvate from enzyme-bound aminodeoxyisochorismate. Reaction follows a random kinetic mechanism, enzyme PhzE can use NH4+ as an alternative nucleophile. PhzE shows no lyase activity
724464
Pseudomonas aeruginosa
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
?
x * 71274, calculated, x * 71251, MALDI-TOF, His-tagged recombinant protein
Pseudomonas aeruginosa
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
30
-
Pseudomonas aeruginosa
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
45
-
20% of maximum activtiy
Pseudomonas aeruginosa
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.16
-
chorismate
cosubstrate NH3, pH 7.0, 25°C
Pseudomonas aeruginosa
2.2
-
chorismate
cosubstrate L-glutamine, pH 7.0, 25°C
Pseudomonas aeruginosa
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Pseudomonas aeruginosa
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
1-hydroxyphenazine
inhibitory above 0.200 mM
Pseudomonas aeruginosa
additional information
enzyme is not regulated by feedback inhibition. Little or no inhibition up to 1 mM: glyphosate, pyridoxamine 5'-phosphate, pyridoxal 5'-phosphate, and 3-hydroxypyridine-4-carboxylic acid
Pseudomonas aeruginosa
phosphate
phosphate buffer competitively inhibits PhzE, about 20% inhibition with 100 mM potassium phosphate at pH 7.0
Pseudomonas aeruginosa
pyocyanin
inhibitory above 0.250 mM
Pseudomonas aeruginosa
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.02
-
chorismate
cosubstrate L-glutamine, pH 7.0, 25°C
Pseudomonas aeruginosa
0.216
-
chorismate
cosubstrate L-glutamine, pH 7.0, 25°C
Pseudomonas aeruginosa
11
-
L-glutamine
pH 7.0, 25°C
Pseudomonas aeruginosa
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Co2+
-
Pseudomonas aeruginosa
Mg2+
required, Km value 0.29 mM
Pseudomonas aeruginosa
Mn2+
-
Pseudomonas aeruginosa
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
71251
-
-
Pseudomonas aeruginosa
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
chorismate + L-glutamine
-
724464
Pseudomonas aeruginosa
L-glutamate + 4-amino-4-deoxychorismate
-
-
-
?
chorismate + NH3
-
724464
Pseudomonas aeruginosa
4-amino-4-deoxychorismate + H2O
-
-
-
?
additional information
isoform PhzE catalyzes the addition of ammonia to C2 of chorismate, as does anthranilate synthase, yet unlike anthranilate synthase it does not catalyze elimination of pyruvate from enzyme-bound aminodeoxyisochorismate. Reaction follows a random kinetic mechanism, enzyme PhzE can use NH4+ as an alternative nucleophile. PhzE shows no lyase activity
724464
Pseudomonas aeruginosa
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 71274, calculated, x * 71251, MALDI-TOF, His-tagged recombinant protein
Pseudomonas aeruginosa
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
30
-
Pseudomonas aeruginosa
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
45
-
20% of maximum activtiy
Pseudomonas aeruginosa
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.16
-
chorismate
cosubstrate NH3, pH 7.0, 25°C
Pseudomonas aeruginosa
2.2
-
chorismate
cosubstrate L-glutamine, pH 7.0, 25°C
Pseudomonas aeruginosa
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Pseudomonas aeruginosa
Other publictions for EC 2.6.1.85
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)
737705
Culbertson
Conversion of aminodeoxychoris ...
Escherichia coli
Biochemistry
54
2372-2384
2015
-
1
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3
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738864
Deng
Cloning, expression, and chara ...
Agaricus bisporus
J. Microbiol. Biotechnol.
25
66-73
2015
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1
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1
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2
724464
Culbertson
Expression and characterizatio ...
Pseudomonas aeruginosa
Biochim. Biophys. Acta
1834
240-246
2013
-
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4
3
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3
1
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5
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3
1
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1
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1
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1
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3
1
1
1
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2
1
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724331
Bera
Structure of aminodeoxychorism ...
Stenotrophomonas maltophilia
Biochemistry
51
10208-10217
2012
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1
1
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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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724111
Camara
The synthesis of pABA: Couplin ...
Arabidopsis thaliana
Arch. Biochem. Biophys.
505
83-90
2011
1
-
1
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1
7
1
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3
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1
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1
4
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1
7
1
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1
4
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6
6
702371
Ziebart
Nucleophile specificity in ant ...
Escherichia coli
Biochemistry
49
2851-2859
2010
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684435
Keller
Action of atrop-abyssomicin C ...
Bacillus subtilis
Angew. Chem. Int. Ed. Engl.
46
8284-8286
2007
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661933
He
Conservation of mechanism in t ...
Escherichia coli
J. Am. Chem. Soc.
126
2378-2385
2004
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1
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2
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1
5
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3
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1
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6
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2
5
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2
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6
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661938
Bulloch
Identification of 4-amino-4-de ...
Escherichia coli
J. Am. Chem. Soc.
126
9912-9913
2004
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644249
Parsons
Structure of Escherichia coli ...
Escherichia coli
Biochemistry
41
2198-2208
2002
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1
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1
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2
1
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644250
Chang
p-Aminobenzoic acid and chlora ...
Streptomyces venezuelae, Streptomyces venezuelae ISP5230
Microbiology
147
2113-2126
2001
-
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1
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2
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8
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2
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644248
Rayl
Escherichia coli aminodeoxycho ...
Escherichia coli
Biochim. Biophys. Acta
1295
81-88
1996
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644230
Viswanathan
Kinetic characterization of 4- ...
Escherichia coli
J. Bacteriol.
177
5918-5923
1995
2
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1
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644227
Ye
p-Aminobenzoate synthesis in E ...
Escherichia coli
Proc. Natl. Acad. Sci. USA
87
9391-9395
1990
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