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chorismate + L-glutamine = 4-amino-4-deoxychorismate + L-glutamate
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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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
L-glutamate + 4-amino-4-deoxychorismate
chorismate + NH3
4-amino-4-deoxychorismate + ?
chorismate + NH3
4-amino-4-deoxychorismate + H2O
chorismate + NH4+
4-amino-4-deoxychorismate + H2O + H+
-
-
-
-
?
additional information
?
-
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
-
-
-
-
?
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 + L-glutamine
L-glutamate + 4-amino-4-deoxychorismate
-
-
-
?
chorismate + NH3
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
-
-
?
chorismate + NH3
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
-
-
?
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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(5R,6R)-4-ammonio-5-((1-carboxylatovinyl)oxy)-6-hydroxycyclohex-1-ene-1-carboxylate
-
transition-state analogue, competitive
1-hydroxyphenazine
inhibitory above 0.200 mM
2-fluorochorismate
-
irreversible, covalent modification of K274
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
pyocyanin
inhibitory above 0.250 mM
additional information
-
not inhibited by sulfathiazole
-
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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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
0.013
chorismate
-
wild-type, cosubstrate L-glutamine, pH 8.5, 25°C
0.02
chorismate
cosubstrate L-glutamine, pH 7.0, 25°C
0.058
chorismate
-
wild-type, cosubstrate NH4+, pH 8.5, 25°C
0.097
chorismate
-
mutant K274A, cosubstrate NH4+, pH 8.5, 25°C
0.117
chorismate
pH 8.0, 25°C
0.216
chorismate
cosubstrate L-glutamine, pH 7.0, 25°C
0.24
chorismate
-
PabB, pH 8.0, 25°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
2.4
L-glutamine
pH 8.0, 25°C
11
L-glutamine
pH 7.0, 25°C
145
NH4+
-
wild-type, pH 8.5, 25°C
169
NH4+
-
mutant K274A, pH 8.5, 25°C
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0.02
2-amino-2-deoxychorismate
-
PabB, second half of the reaction, pH 8.0, 25°C
0.000098 - 2.2
chorismate
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
0.000098
chorismate
-
mutant K274R, cosubstrate NH4+, pH 8.5, 25°C
0.00083
chorismate
-
mutant K274R, cosubstrate L-glutamine, pH 8.5, 25°C
0.002
chorismate
-
mutant K274A, cosubstrate L-glutamine, pH 8.5, 25°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
0.017
chorismate
pH 8.0, 25°C
0.026
chorismate
-
mutant K274A, cosubstrate NH4+, pH 8.5, 25°C
0.032
chorismate
-
wild-type, cosubstrate NH4+, pH 8.5, 25°C
0.16
chorismate
cosubstrate NH3, pH 7.0, 25°C
0.53
chorismate
-
wild-type, cosubstrate L-glutamine, pH 8.5, 25°C
2.2
chorismate
cosubstrate L-glutamine, pH 7.0, 25°C
0.013
L-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
0.67
L-glutamine
-
wild type 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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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
-
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
-
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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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
-
265fold reduction of kcat-value
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
K274R
-
640fold reduction of kcat-value
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
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
-
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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Ye, Q.Z.; Liu, J.; Walsh, C.T.
p-Aminobenzoate synthesis in Escherichia coli: purification and characterization of PabB as aminodeoxychorismate synthase and enzyme X as aminodeoxychorismate lyase
Proc. Natl. Acad. Sci. USA
87
9391-9395
1990
Escherichia coli
brenda
Viswanathan, V.K.; Green, J.M.; Nicholas, B.P.
Kinetic characterization of 4-amino 4-deoxychorismate synthase from Escherichia coli
J. Bacteriol.
177
5918-5923
1995
Escherichia coli
brenda
Rayl, E.A.; Green, J.M.; Nichols, B.P.
Escherichia coli aminodeoxychorismate synthase: analysis of pabB mutations affecting catalysis and subunit association
Biochim. Biophys. Acta
1295
81-88
1996
Escherichia coli
brenda
Parsons, J.F.; Jensen, P.Y.; Pachikara, A.S.; Howard, A.J.; Eisenstein, E.; Ladner, J.E.
Structure of Escherichia coli Aminodeoxychorismate Synthase: architectural conservation and diversity in chorismate-utilizing enzymes
Biochemistry
41
2198-2208
2002
Escherichia coli (P05041), Escherichia coli
brenda
Chang, Z.; Sun, Y.; He, J.; Vining, L.C.
p-Aminobenzoic acid and chloramphenicol biosynthesis in Streptomyces venezuelae: gene sets for a key enzyme, 4-amino-4-deoxychorismate synthase
Microbiology
147
2113-2126
2001
Streptomyces venezuelae, Streptomyces venezuelae ISP5230
brenda
He, Z.; Stigers Lavoie, K.D.; Bartlett, P.A.; Toney, M.D.
Conservation of mechanism in three chorismate-utilizing enzymes
J. Am. Chem. Soc.
126
2378-2385
2004
Escherichia coli
brenda
Bulloch, E.M.M.; Jones, M.A.; Parker, E.J.; Osborne, A.P.; Stephens, E.; Davies, G.M.; Coggins, J.R.; Abell, C.
Identification of 4-amino-4-deoxychorismate synthase as the molecular target for the antimicrobial action of (6S)-6-fluoroshikimate
J. Am. Chem. Soc.
126
9912-9913
2004
Escherichia coli
brenda
Keller, S.; Schadt, H.S.; Ortel, I.; Suessmuth, R.D.
Action of atrop-abyssomicin C as an inhibitor of 4-amino-4-deoxychorismate synthase PabB
Angew. Chem. Int. Ed. Engl.
46
8284-8286
2007
Bacillus subtilis (P28820)
brenda
Ziebart, K.T.; Toney, M.D.
Nucleophile specificity in anthranilate synthase, aminodeoxychorismate synthase, isochorismate synthase, and salicylate synthase
Biochemistry
49
2851-2859
2010
Escherichia coli
brenda
Camara, D.; Richefeu-Contesto, C.; Gambonnet, B.; Dumas, R.; Rebeille, F.
The synthesis of pABA: Coupling between the glutamine amidotransferase and aminodeoxychorismate synthase domains of the bifunctional aminodeoxychorismate synthase from Arabidopsis thaliana
Arch. Biochem. Biophys.
505
83-90
2011
Arabidopsis thaliana
brenda
Bera, A.K.; Atanasova, V.; Dhanda, A.; Ladner, J.E.; Parsons, J.F.
Structure of aminodeoxychorismate synthase from Stenotrophomonas maltophilia
Biochemistry
51
10208-10217
2012
Stenotrophomonas maltophilia
brenda
Culbertson, J.E.; Toney, M.D.
Expression and characterization of PhzE from P. aeruginosa PAO1: aminodeoxyisochorismate synthase involved in pyocyanin and phenazine-1-carboxylate production
Biochim. Biophys. Acta
1834
240-246
2013
Pseudomonas aeruginosa (Q7DC81), Pseudomonas aeruginosa
brenda
Culbertson, J.E.; Chung, D.h.; Ziebart, K.T.; Espiritu, E.; Toney, M.D.
Conversion of aminodeoxychorismate synthase into anthranilate synthase with Janus mutations: mechanism of pyruvate elimination catalyzed by chorismate enzymes
Biochemistry
54
2372-2384
2015
Escherichia coli (P00903), Escherichia coli
brenda
Deng, L.X.; Shen, Y.M.; Song, S.Y.
Cloning, expression, and characterization of para-aminobenzoic acid (PABA) synthase from Agaricus bisporus 02, a thermotolerant mushroom strain
J. Microbiol. Biotechnol.
25
66-73
2015
Agaricus bisporus (A0A060IGN1), Agaricus bisporus
brenda
Xie, W.; Perry, G.; Martin, C.J.; Shim, Y.-S.; Navabi, A.; Pauls, K.P.
Molecular characterization of dihydroneopterin aldolase and aminodeoxychorismate synthase in common bean - genes coding for enzymes in the folate synthesis pathway
Genome
60
588-600
2017
Phaseolus vulgaris (G1JT92), Phaseolus vulgaris (G1JT93), Phaseolus vulgaris BAT93 (G1JT92), Phaseolus vulgaris Jalo EEP558 (G1JT93)
brenda