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Information on EC 2.6.1.85 - aminodeoxychorismate synthase
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EC Tree
2.6.1.85 aminodeoxychorismate synthaseIUBMB Comments
The enzyme is composed of two parts, a glutaminase (PabA in Escherichia coli) and an aminotransferase (PabB). In the absence of PabA and glutamine (but in the presence of Mg2+), PabB can convert ammonia and chorismate into 4-amino-4-deoxychorismate. PabA converts glutamine into glutamate only in the presence of stoichiometric amounts of PabB. In many organisms, including plants, the genes encoding the two proteins have fused to encode a single bifunctional protein. This enzyme is coupled with EC 4.1.3.38, aminodeoxychorismate lyase, to form 4-aminobenzoate. cf. EC 2.6.1.123, 4-amino-4-deoxychorismate synthase (2-amino-4-deoxychorismate-forming).
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Word Map
- 2.6.1.85
- folate
- p-aminobenzoate
- anthranilate
- isochorismate
-
chorismate-utilizing
-
para-aminobenzoic
-
amidotransferase
- shikimate
-
macrolactone
-
biofortification
- enterobactin
- candicidin
- biotechnology
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
aminodeoxychorismate synthase, pabab, 4-amino-4-deoxychorismate synthase, adc synthase, pvadcs, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
4-amino-4-deoxychorismate synthase
ADC synthase
ADCS
aminodeoxychorismate synthase
chorismate:L-glutamine amido-ligase
-
-
incorrect
-
EC 6.3.5.8
-
-
formerly
-
PabB
PvADCS
4-amino-4-deoxychorismate synthase
-
-
-
-
ADC synthase
-
-
-
-
aminodeoxychorismate synthase
-
heterodimeric complex, subunit PabB catalyces the amination of chorismate, subunit PabA is an amidotransferase that supplies ammonia from glutamine hydrolysis, subunit PabA is not identfied in Stenotrophomonas maltophilia
PabB
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
chorismate + NH3 = 4-amino-4-deoxychorismate + H2O
(1b)
-
-
-
L-glutamine + H2O = L-glutamate + NH3
(1a)
-
-
-
chorismate + L-glutamine = 4-amino-4-deoxychorismate + L-glutamate
the enzyme is composed of two parts, PabA and PabB
-
chorismate + L-glutamine = 4-amino-4-deoxychorismate + L-glutamate
association of PabA and PabB is greatly enhanced by 5 mM glutamine and greatly reduced at cold temperatures
-
chorismate + L-glutamine = 4-amino-4-deoxychorismate + L-glutamate
in the absence of PabA and glutamine, PabB converts ammonia and chorismate into 4-amino-4-deoxychorismate (in the presence of Mg2+)
-
chorismate + L-glutamine = 4-amino-4-deoxychorismate + L-glutamate
non linear production of PABA in the ADC synthase-ADC lyase-coupled reaction system, at different glutamine and chorismate concentrations, with limiting PabB
-
chorismate + L-glutamine = 4-amino-4-deoxychorismate + L-glutamate
mechanism includes nucleophile addition to C2 of chorismate in an SN2'' process
-
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
-
chorismate + L-glutamine = 4-amino-4-deoxychorismate + L-glutamate
overall reaction
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amino group transfer
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
chorismate:L-glutamine aminotransferase
The enzyme is composed of two parts, a glutaminase (PabA in Escherichia coli) and an aminotransferase (PabB). In the absence of PabA and glutamine (but in the presence of Mg2+), PabB can convert ammonia and chorismate into 4-amino-4-deoxychorismate. PabA converts glutamine into glutamate only in the presence of stoichiometric amounts of PabB. In many organisms, including plants, the genes encoding the two proteins have fused to encode a single bifunctional protein. This enzyme is coupled with EC 4.1.3.38, aminodeoxychorismate lyase, to form 4-aminobenzoate. cf. EC 2.6.1.123, 4-amino-4-deoxychorismate synthase (2-amino-4-deoxychorismate-forming).
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CAS REGISTRY NUMBER
COMMENTARY
132264-37-0
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-amino-2-deoxychorismate + NH3
4-amino-4-deoxychorismate + NH3
-
PabB, second half of the reaction, starting with the intermediate
-
-
?
chorismate + L-asparagine
4-amino-4-deoxychorismate + L-aspartate
11% of the activity with L-glutamine
-
-
?
chorismate + L-glutamine
4-amino-4-deoxychorismate + L-glutamate
-
-
-
?
chorismate + L-glutamine
4-amino-4-deoxychorismate + L-glutamate
-
-
-
?
chorismate + L-glutamine
4-amino-4-deoxychorismate + L-glutamate
-
-
-
?
chorismate + L-glutamine
4-amino-4-deoxychorismate + L-glutamate
-
-
-
r
chorismate + L-glutamine
4-amino-4-deoxychorismate + L-glutamate
-
-
?
chorismate + L-glutamine
4-amino-4-deoxychorismate + L-glutamate
-
commited step in PABA biosynthesis
-
?
chorismate + L-glutamine
4-amino-4-deoxychorismate + L-glutamate
commited step in PABA biosynthesis
-
?
chorismate + L-glutamine
4-amino-4-deoxychorismate + L-glutamate
-
-
-
?
chorismate + L-glutamine
4-amino-4-deoxychorismate + L-glutamate
-
-
-
?
chorismate + L-glutamine
L-glutamate + 4-amino-4-deoxychorismate
-
-
-
-
?
chorismate + L-glutamine
L-glutamate + 4-amino-4-deoxychorismate
-
-
-
?
chorismate + NH3
4-amino-4-deoxychorismate + ?
-
PabB, intermediate 2-amino-2-deoxychorismate involved
-
-
?
chorismate + NH3
4-amino-4-deoxychorismate + H2O
30% of the activity with L-glutamine
-
-
?
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
-
-
?
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
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
chorismate + L-glutamine
4-amino-4-deoxychorismate + L-glutamate
-
-
-
?
chorismate + L-glutamine
4-amino-4-deoxychorismate + L-glutamate
-
-
-
r
chorismate + L-glutamine
4-amino-4-deoxychorismate + L-glutamate
-
commited step in PABA biosynthesis
-
?
chorismate + L-glutamine
4-amino-4-deoxychorismate + L-glutamate
commited step in PABA biosynthesis
-
?
chorismate + L-glutamine
4-amino-4-deoxychorismate + L-glutamate
-
-
-
?
chorismate + L-glutamine
4-amino-4-deoxychorismate + L-glutamate
-
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Mg2+
Mn2+
Co2+
divalent cation required, in decreasing activity: Mg2+, Mn2+, Co2+
Mg2+
divalent cation required, in decreasing activity: Mg2+, Mn2+, Co2+. Highest activity at 5 mM Mg2+
Mn2+
divalent cation required, in decreasing activity: Mg2+, Mn2+, Co2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(5R,6R)-4-ammonio-5-((1-carboxylatovinyl)oxy)-6-hydroxycyclohex-1-ene-1-carboxylate
-
transition-state analogue, competitive
NH3
-
inhibitor of the glutamine amidotransferase reaction (Ki = 5 mM, lowered to 0.27 mM if considered that NH3 and not NH4+ is the true inhibitor (pKa value of 9.24))
phosphate
phosphate buffer competitively inhibits PhzE, about 20% inhibition with 100 mM potassium phosphate at pH 7.0
additional information
-
not inhibited by ATP, AMP, dAMP, guanosine, GMP, dGMP, GTP, deoxyguanosine, dTMP, serine, glycine, tyrosine, methionine, p-hydroxybenzoate, PABA, sulfanilamide
-
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
-
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
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
195
NH3
-
NH3-dependent p-aminobenzoate production in the absence of glutamine (assay contains 4-amino-4-desoxychorismate lyase), pH 8.0, 37°C
0.0016
chorismate
-
apparent K0.5 of chorismate for the activation of glutamine amidotransferase (calculated from chorismate-dependent activation), pH 8.0, 37°C
0.0022
chorismate
-
p-aminobenzoate or pyruvate production in the presence of glutamine (assay contains 4-amino-4-desoxychorismate lyase), pH 8.0, 37°C
0.009
chorismate
-
NH3-dependent p-aminobenzoate production in the absence of glutamine (assay contains 4-amino-4-desoxychorismate lyase), pH 8.0, 37°C
0.045
L-glutamine
-
glutamate production in the presence of chorismate, pH 8.0, 37°C
0.05
L-glutamine
-
glutamate production in the absence of chorismate, pH 8.0, 37°C
0.064
L-glutamine
-
p-aminobenzoate or pyruvate production in the presence of glutamine (assay contains 4-amino-4-desoxychorismate lyase), pH 8.0, 37°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02
2-amino-2-deoxychorismate
-
PabB, second half of the reaction, pH 8.0, 25°C
0.12
NH3
-
NH3-dependent p-aminobenzoate production in the absence of glutamine (assay contains 4-amino-4-desoxychorismate lyase), pH 8.0, 37°C
0.007
chorismate
-
PabB, addition of Escherichia coli PabA enhances the reaction rate 20fold in the absence of glutamine, pH 8.0, 25°C
0.22
L-glutamine
-
p-aminobenzoate or pyruvate production in the presence of glutamine (assay contains 4-amino-4-desoxychorismate lyase), pH 8.0, 37°C
0.23
L-glutamine
-
glutamate production in the absence of chorismate, pH 8.0, 37°C
0.6
L-glutamine
-
mutant K213A/Q147K amidotransferase activity, pH 8.0, 25°C
0.79
L-glutamine
-
glutamate production in the presence of chorismate, pH 8.0, 37°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00061
NH3
-
NH3-dependent p-aminobenzoate production in the absence of glutamine (assay contains 4-amino-4-desoxychorismate lyase), pH 8.0, 37°C
13.3
chorismate
-
NH3-dependent p-aminobenzoate production in the absence of glutamine (assay contains 4-amino-4-desoxychorismate lyase), pH 8.0, 37°C
100
chorismate
-
p-aminobenzoate or pyruvate production in the presence of glutamine (assay contains 4-amino-4-desoxychorismate lyase), pH 8.0, 37°C
3.4
L-glutamine
-
p-aminobenzoate or pyruvate production in the presence of glutamine (assay contains 4-amino-4-desoxychorismate lyase), pH 8.0, 37°C
4.6
L-glutamine
-
glutamate production in the absence of chorismate, pH 8.0, 37°C
17.5
L-glutamine
-
glutamate production in the presence of chorismate, pH 8.0, 37°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0007 - 0.0056
(5R,6R)-4-ammonio-5-((1-carboxylatovinyl)oxy)-6-hydroxycyclohex-1-ene-1-carboxylate
5
NH3
-
inhibitor of the glutamine amidotransferase reaction (Ki lowered to 0.27 mM if considered that NH3 and not NH4+ is the true inhibitor (pKa value of 9.24)), pH 8.0, 37°C
0.0007
(5R,6R)-4-ammonio-5-((1-carboxylatovinyl)oxy)-6-hydroxycyclohex-1-ene-1-carboxylate
-
mutant K274A, pH 8.5, 25°C
0.0056
(5R,6R)-4-ammonio-5-((1-carboxylatovinyl)oxy)-6-hydroxycyclohex-1-ene-1-carboxylate
-
wild-type, pH 8.5, 25°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PabB heterologously overexpressed in Escherichia coli
SwissProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
evolution
common beans are excellent sources of dietary folates, but different varieties contain different amounts of these compounds. Dihydroneopterin aldolase (DHNA, EC 4.1.2.25) and aminodeoxychorismate synthase (ADCS) genes in the folate synthesis pathway, are characterized by PCR amplification, BAC clone sequencing, and whole genome sequencing. All DHNA and ADCS genes in the Mesoamerican cultivar OAC Rex are isolated and compared with those genes in the genome of Andean genotype G19833. Both genotypes have two functional DHNA genes and one pseudogene. There is only one ADCS gene (PvADCS) identified in the bean genome and it is identical in OAC Rex and G19833. PvADCS has the conserved motifs required for catalytic activity similar to other plant ADCS homologues. Genotype and geotype mapping
evolution
Phaseolus vulgaris BAT93
-
common beans are excellent sources of dietary folates, but different varieties contain different amounts of these compounds. Dihydroneopterin aldolase (DHNA, EC 4.1.2.25) and aminodeoxychorismate synthase (ADCS) genes in the folate synthesis pathway, are characterized by PCR amplification, BAC clone sequencing, and whole genome sequencing. All DHNA and ADCS genes in the Mesoamerican cultivar OAC Rex are isolated and compared with those genes in the genome of Andean genotype G19833. Both genotypes have two functional DHNA genes and one pseudogene. There is only one ADCS gene (PvADCS) identified in the bean genome and it is identical in OAC Rex and G19833. PvADCS has the conserved motifs required for catalytic activity similar to other plant ADCS homologues. Genotype and geotype mapping
-
evolution
Phaseolus vulgaris Jalo EEP558
-
common beans are excellent sources of dietary folates, but different varieties contain different amounts of these compounds. Dihydroneopterin aldolase (DHNA, EC 4.1.2.25) and aminodeoxychorismate synthase (ADCS) genes in the folate synthesis pathway, are characterized by PCR amplification, BAC clone sequencing, and whole genome sequencing. All DHNA and ADCS genes in the Mesoamerican cultivar OAC Rex are isolated and compared with those genes in the genome of Andean genotype G19833. Both genotypes have two functional DHNA genes and one pseudogene. There is only one ADCS gene (PvADCS) identified in the bean genome and it is identical in OAC Rex and G19833. PvADCS has the conserved motifs required for catalytic activity similar to other plant ADCS homologues. Genotype and geotype mapping
-
metabolism
the enzyme is involved in the folate synthesis pathway
metabolism
Phaseolus vulgaris Jalo EEP558
-
the enzyme is involved in the folate synthesis pathway
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
heterodimer of chorismate aminating subunit and glutamine amidotransferase subunit. Mass of glutamine amidotransferase subunit is 50969 Da, as determined by electrospray mass spectrometry
monomer
?
x * 71274, calculated, x * 71251, MALDI-TOF, His-tagged recombinant protein
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K213A
-
subunit PabB, numbering used is based on the EntC protein from Escherichia coli, reduced activity
K213A/Q147K
-
subunit PabB, numbering used is based on the EntC protein from Escherichia coli, strongly reduced activity
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
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
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
additional information
additional information
a single-nucleotide polymorphism (SNP) for PvADCS is identified between the ADCS gene fragment sequences of BAT93 (JN392964) and Jalo EEP558 (JN392965)
additional information
a single-nucleotide polymorphism (SNP) for PvADCS is identified between the ADCS gene fragment sequences of BAT93 (JN392964) and Jalo EEP558 (JN392965)
additional information
Phaseolus vulgaris BAT93
-
a single-nucleotide polymorphism (SNP) for PvADCS is identified between the ADCS gene fragment sequences of BAT93 (JN392964) and Jalo EEP558 (JN392965)
-
additional information
Phaseolus vulgaris Jalo EEP558
-
a single-nucleotide polymorphism (SNP) for PvADCS is identified between the ADCS gene fragment sequences of BAT93 (JN392964) and Jalo EEP558 (JN392965)
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80º, 50 mM MOPS, 50 mM KCl, 0.1 mM EDTA, 2 mM DTT, 5 mM MgCl, pH 7.6
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
chromatography on Poros HQ50, HS20 cation exchange chromatography and chromatography on hydroxyapatite
immobilized metal ion affinity chromatography (Co2+), fusion tag removed
-
protamine sulfate precipitation, ammonium sulfate fractionation, chromatography on Sephacryl S-200, chromatography on DEAE-Sephacel and chromatography on dye-agarose
-
streptomycin sulfate precipitation, ammonium sulfate fractionation, chromatography on DEAE-cellulose
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene ADCS, a ADCS gene-specific marker is developed, mapped and compared to its physical location on chromosome 7, DNA and amino acid sequence determination and analysis, genotyping, sequence comparisons and phylogenetic analysis
gene ADCS, a ADCS gene-specific marker is developed, mapped, and compared to its physical location on chromosome 7, DNA and amino acid sequence determination and analysis, genotyping, sequence comparisons and phylogenetic analysis
His-tagged protein (first 43 amino acid residues deleted) expressed in Escherichia coli BL21-CodonPlus (DE3)-RIL
-
pabB, optimized for overexpression in Escherichia coli, His-tagged protein expressed in Escherichia coli BL21(DE3)
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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