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show all sequences of 2.6.1.86

Conversion of aminodeoxychorismate synthase into anthranilate synthase with Janus mutations: mechanism of pyruvate elimination catalyzed by chorismate enzymes

Culbertson, J.E.; Chung, D.h.; Ziebart, K.T.; Espiritu, E.; Toney, M.D.; Biochemistry 54, 2372-2384 (2015)

Data extracted from this reference:

Application
Application
Commentary
Organism
biotechnology
conversion of aminodeoxychorismate synthase into anthranilate synthase employing a bioinformatics method for predicting mutations required to functionally interconvert homologous enzymes. Complementation of an anthranilate synthase-deficient strain of Escherichia coli grown on minimal medium leads to several aminodeoxychorismate synthase mutants that allow growth in 6 days compared to 2 days for wild-type anthranilate synthase. The purified mutant enzymes catalyze the conversion of chorismate to anthranilate at rates that are about 50% of the rate of wild-type aminodeoxychorismate synthase-catalyzed conversion of chorismate to aminodeoxychorismate. The residues mutated do not contact the substrate
Escherichia coli
Engineering
Amino acid exchange
Commentary
Organism
K274A/L277R/D299E/N303H/I306L/F334Y/C391G
mutant displaying anthranilate synthase activity, the kcat/Kchoris value for anthranilate formation is 25% of the wild-type aminodeoxychorismate synthase value for 4-amino-4-deoxychorismate production
Escherichia coli
N213V/L214P/K274A/L277R/D299E/N303H/F334Y/P363N/I367L/C391G/G425A
mutant displaying anthranilate synthase activity, is able to produce both 2-amino-2-deoxyisochorismate and anthranilate
Escherichia coli
N213V/L214P/R259S/K274A/L277R/N303H/F334Y/S366T/C391G/G254A
mutant displaying anthranilate synthase activity, is able to produce both 2-amino-2-deoxyisochorismate and anthranilate
Escherichia coli
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
P00903
-
-
Application (protein specific)
Application
Commentary
Organism
biotechnology
conversion of aminodeoxychorismate synthase into anthranilate synthase employing a bioinformatics method for predicting mutations required to functionally interconvert homologous enzymes. Complementation of an anthranilate synthase-deficient strain of Escherichia coli grown on minimal medium leads to several aminodeoxychorismate synthase mutants that allow growth in 6 days compared to 2 days for wild-type anthranilate synthase. The purified mutant enzymes catalyze the conversion of chorismate to anthranilate at rates that are about 50% of the rate of wild-type aminodeoxychorismate synthase-catalyzed conversion of chorismate to aminodeoxychorismate. The residues mutated do not contact the substrate
Escherichia coli
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
K274A/L277R/D299E/N303H/I306L/F334Y/C391G
mutant displaying anthranilate synthase activity, the kcat/Kchoris value for anthranilate formation is 25% of the wild-type aminodeoxychorismate synthase value for 4-amino-4-deoxychorismate production
Escherichia coli
N213V/L214P/K274A/L277R/D299E/N303H/F334Y/P363N/I367L/C391G/G425A
mutant displaying anthranilate synthase activity, is able to produce both 2-amino-2-deoxyisochorismate and anthranilate
Escherichia coli
N213V/L214P/R259S/K274A/L277R/N303H/F334Y/S366T/C391G/G254A
mutant displaying anthranilate synthase activity, is able to produce both 2-amino-2-deoxyisochorismate and anthranilate
Escherichia coli
Other publictions for EC 2.6.1.86
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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Burkholderia lata, Burkholderia lata 383
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2011
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682589
Van Lanen
Biosynthesis of the enediyne a ...
Streptomyces globisporus
Proc. Natl. Acad. Sci. USA
105
494-499
2008
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680341
McDonald
Phenazine biosynthesis in Pseu ...
Pseudomonas fluorescens
J. Am. Chem. Soc.
123
9459-9460
2001
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33303
Morollo
Characterization of composite ...
Salmonella enterica subsp. enterica serovar Typhimurium
Proc. Natl. Acad. Sci. USA
90
9983-9987
1993
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