BRENDA - Enzyme Database show
show all sequences of 2.6.1.85

Identification of 4-amino-4-deoxychorismate synthase as the molecular target for the antimicrobial action of (6S)-6-fluoroshikimate

Bulloch, E.M.M.; Jones, M.A.; Parker, E.J.; Osborne, A.P.; Stephens, E.; Davies, G.M.; Coggins, J.R.; Abell, C.; J. Am. Chem. Soc. 126, 9912-9913 (2004)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
2-fluorochorismate
irreversible, covalent modification of K274
Escherichia coli
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
-
-
-
Reaction
Reaction
Commentary
Organism
chorismate + L-glutamine = 4-amino-4-deoxychorismate + L-glutamate
omega-amino group of K274 adds to chorismate at C2, leading to elimination of the C4 hydroxyl in an SN2'' displacement reaction. After attack of ammonia to intermediate, another SN2'' displacement expels K274 and forms aminodeoxychorismate
Escherichia coli
Subunits
Subunits
Commentary
Organism
dimer
heterodimer of chorismate aminating subunit and glutamine amidotransferase subunit. Mass of glutamine amidotransferase subunit is 50969 Da, as determined by electrospray mass spectrometry
Escherichia coli
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.13
-
2-fluorochorismate
-
Escherichia coli
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
2-fluorochorismate
irreversible, covalent modification of K274
Escherichia coli
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.13
-
2-fluorochorismate
-
Escherichia coli
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
heterodimer of chorismate aminating subunit and glutamine amidotransferase subunit. Mass of glutamine amidotransferase subunit is 50969 Da, as determined by electrospray mass spectrometry
Escherichia coli
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
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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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2
724464
Culbertson
Expression and characterizatio ...
Pseudomonas aeruginosa
Biochim. Biophys. Acta
1834
240-246
2013
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3
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1
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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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724111
Camara
The synthesis of pABA: Couplin ...
Arabidopsis thaliana
Arch. Biochem. Biophys.
505
83-90
2011
1
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1
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1
7
1
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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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5
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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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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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8
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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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644227
Ye
p-Aminobenzoate synthesis in E ...
Escherichia coli
Proc. Natl. Acad. Sci. USA
87
9391-9395
1990
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