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4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
D-alanine + pyridoxal 5'-phosphate
pyridoxamine 5'-phosphate + pyruvate
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L-alanine and other D- and L-amino acids tested are inert as substrates of transamination
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additional information
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4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
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last step of the 4-aminobenzoate branch
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4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
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4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
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4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
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4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
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4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
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4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
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4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
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re-face specificity
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4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
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4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
the enzyme catalyzes the beta-elimination of pyruvate and the aromatization of the ADC ring to yield 4-aminobenzoate. Substrate synthesis from chorismate and ammonia by chorismate aminase in a coupled assay, the substrate is unstable
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4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
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4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
molecular modeling of the catalytic intermediate, overview
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4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
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4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
simulation and validation of the substrate-binding model, overview
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4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
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last step of the 4-aminobenzoate branch
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4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
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4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
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4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
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additional information
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The enzyme shows some transaminase activity towards different D-amino acids (D-Asp, D-Ala and D-Glu, in particular) using 2-oxoacids such as oxaloacetate or pyruvate as amino group acceptors. This activity corresponds to EC 2.6.1.21.
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additional information
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The enzyme shows some transaminase activity towards different D-amino acids (D-Asp, D-Ala and D-Glu, in particular) using 2-oxoacids such as oxaloacetate or pyruvate as amino group acceptors. This activity corresponds to EC 2.6.1.21.
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4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
D-alanine + pyridoxal 5'-phosphate
pyridoxamine 5'-phosphate + pyruvate
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L-alanine and other D- and L-amino acids tested are inert as substrates of transamination
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r
4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
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last step of the 4-aminobenzoate branch
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4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
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4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
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4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
Q8IKP7
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4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
Q9HZN6
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4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
Q03266
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4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
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last step of the 4-aminobenzoate branch
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small yellow prisms crystals in the unliganded form obtained using the sparse-matrix method along with the hanging-drop vapor-difussion method
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purified recombinant detagged enzyme, hanging drop vapour diffusion method, mixing of 0.001 ml of 33 mg/mL prrotein in 100 mM HEPES, pH 7.5, 500 mM NaCl, 0.1 mM pyridoxal 5'-phosphate, and 10 mM 4-aminobenzoate, with 0001 ml of reservoir solution containing 10% w/v PEG 400, 1.8 M ammonium sulfate and 100 mM MES, pH 6.5, 20°C, 1 week, X-ray diffraction structure dtermination and analysis at 1.75 A resolution
purified recombinant selenomethionine-labeled enzyme and of purified recombinant wild-type enzyme in complex with cofactor pyridoxal 5'-phosphate, hanging drop vapor diffusion method, mixing of 0.001 ml of 10 mg/ml protein in 100 mM NaCl, 20 mM Tris-Cl, pH 8.0, with an equal volume of reservoir solution containing 20% w/v PEG monomethyl ether 5000, 0.1 M Bis-Tris, pH 6.2, 1-2 days to 1 week, 16°C, X-ray diffraction structure determination and analysis at 1.90-2.20 A resolution
sitting drop vapor diffusion method, using 0.1 M HEPES buffer pH 8.0 containing 1.3 M Li2SO4 and 2% (v/v) PEG 200
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DEAE-Sephacel, phenyl-Sepharose column, Superose 6 gel filtration column, Mono Q, Superose 12 column, yield 400-800fold
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fractionation with ammonium sulfate pH 7.5, DEAE-Sephacel column, butyl-Sepharose 4B column, Gigapite column
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fractionation with ammonium sulfate, DEAE-Toyopearl column, butyl-Toyopearl column and Mono Q column
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nickel affinity column chromatography; nickel affinity column chromatography
reactive yellow 3-agarose column, Mono Q HR 5/5 FPLC column, Superose 12HR 10/30 FPLC column, Mono Q HR 5/20 FPLC column, Aquapore RP-300 C8 HPLC column: 4100fold to near homogeneity
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recombinant His-tagged wild-type and selenomethionine-labeled enzymes from Escherichia coli strain BL21(DE3) and B834(DE3), respectively, by nickel affinity chromatography
recombinant His6-tagged enzyme from Escherichia coli by metal affinity chromatography
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) GOLD by nickel affinity chromatography, cleavage of the tag by TEV protease, and gel filtration
Resource ISO column chromatography, ammonium sulfate precipitation, Resource Q column chromatography, and Superdex 75 gel filtration
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cDNAs are shown to encode functional enzymes by complementation of an Escherichia coli pabC mutant, and by demonstrating that the partially purified recombinant proteins convert 4-amino-4-deoxychorismate to 4-aminobenzoate
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cDNAs are shown to encode functional enzymes by complementation of an Escherichia coli pabC mutant, and by demonstrating that the partially purified recombinant proteins convert 4-amino-4-deoxychorismate to 4-aminobenzoate. The full-length Arabidopsis ADC lyase polypeptide is translocated into isolated pea chloroplasts and, when fused to green fluorescent protein, directed the passenger protein to Arabidopsis chloroplasts in transient expression experiments
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expressed in Escherichia coli B834 (DE3) cells
expressed in Escherichia coli BL21(DE3) cells; expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli JM109
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expression in Escherichia coli MC1000 cells
gene pabC, expression of His6-tagged enzyme with TEV protease cleavage site in Escherichia coli strain BL21(DE3) GOLD
gene PF14_0557, functional overexpression as His6-tagged protein in Escherichia coli cells
recombinant expression of His-tagged wild-type and selenomethionine-labeled enzymes in Escherichia coli strain BL21(DE3) and B834(DE3), respectively
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K180A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
N360A
site-directed mutagenesis, inactive mutant
N360D
site-directed mutagenesis, inactive mutant
T30A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
additional information
a mutant with pabC-1 inactivated still retains about 20% of the wild type level of antibiotic FR-008 production, pabC-1/pabC-2 double mutation severely reduces antibiotic FR-008 production and renders the mutant p-aminobenzoic acid-auxotrophic; pabC-1/pabC-2 double mutation severely reduces antibiotic FR-008 production and renders the mutant p-aminobenzoic acid-auxotrophic
additional information
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a mutant with pabC-1 inactivated still retains about 20% of the wild type level of antibiotic FR-008 production, pabC-1/pabC-2 double mutation severely reduces antibiotic FR-008 production and renders the mutant p-aminobenzoic acid-auxotrophic; pabC-1/pabC-2 double mutation severely reduces antibiotic FR-008 production and renders the mutant p-aminobenzoic acid-auxotrophic
additional information
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a mutant with pabC-1 inactivated still retains about 20% of the wild type level of antibiotic FR-008 production, pabC-1/pabC-2 double mutation severely reduces antibiotic FR-008 production and renders the mutant p-aminobenzoic acid-auxotrophic; pabC-1/pabC-2 double mutation severely reduces antibiotic FR-008 production and renders the mutant p-aminobenzoic acid-auxotrophic
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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
Green, J.M.; Merkel, W.K.; Nichols, B.P.
Characterization and sequence of Escherichia coli pabC, the gene encoding aminodeoxychorismate lyase, a pyridoxal phosphate-containing enzyme
J. Bacteriol.
174
5317-5323
1992
Escherichia coli, Escherichia coli (P28305)
brenda
Green, J.M.; Nichols, B.P.
p-Aminobenzoate biosynthesis in Escherichia coli. Purification of aminodeoxychorismate lyase and cloning of pabC
J. Biol. Chem.
266
12971-12975
1991
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
Nakai, T.; Mizutani, H.; Miyahara, I.; Hirotsu, K.; Takeda, S.; Jhee, K.H.; Yoshimura, T.; Esaki, N.
Three-dimensional structure of 4-amino-4-deoxychorismate lyase from Escherichia coli
J. Biochem.
128
29-38
2000
Escherichia coli
brenda
Jhee, K.H.; Yoshimura, T.; Miles, E.W.; Takeda, S.; Miyahara, I.; Hirotsu, K.; Soda, K.; Kawata, Y.; Esaki, N.
Stereochemistry of the transamination reaction catalyzed by aminodeoxychorismate lyase from Escherichia coli: close relationship between fold type and stereochemistry
J. Biochem.
128
679-686
2000
Escherichia coli
brenda
Nichols, B.P.; Green, J.M.
Cloning and sequencing of Escherichia coli ubiC and purification of chorismate lyase
J. Bacteriol.
174
5309-5316
1992
Escherichia coli
brenda
Basset, G.J.; Ravanel, S.; Quinlivan, E.P.; White, R.; Giovannoni, J.J.; Rebeille, F.; Nichols, B.P.; Shinozaki, K.; Seki, M.; Gregory, J.F., 3rd; Hanson, A.D.
Folate synthesis in plants: the last step of the p-aminobenzoate branch is catalyzed by a plastidial aminodeoxychorismate lyase
Plant J.
40
453-461
2004
Arabidopsis thaliana, Solanum lycopersicum
brenda
Padmanabhan, B.; Bessho, Y.; Ebihara, A.; Antonyuk, S.V.; Ellis, M.J.; Strange, R.W.; Kuramitsu, S.; Watanabe, N.; Hasnain, S.S.; Yokoyama, S.
Structure of putative 4-amino-4-deoxychorismate lyase from Thermus thermophilus HB8
Acta Crystallogr. Sect. F
65
1234-1239
2009
Thermus thermophilus (Q5SKM2)
brenda
Zhang, Y.; Bai, L.; Deng, Z.
Functional characterization of the first two actinomycete 4-amino-4-deoxychorismate lyase genes
Microbiology
155
2450-2459
2009
Streptomyces sp. (B8Y8J0), Streptomyces sp., Streptomyces sp. FR-008 (B8Y8J0), Streptomyces sp. FR-008
brenda
Magnani, G.; Lomazzi, M.; Peracchi, A.
Completing the folate biosynthesis pathway in Plasmodium falciparum: p-aminobenzoate is produced by a highly divergent promiscuous aminodeoxychorismate lyase
Biochem. J.
455
149-155
2013
Plasmodium falciparum, Plasmodium falciparum (Q8IKP7)
brenda
Dai, Y.N.; Chi, C.B.; Zhou, K.; Cheng, W.; Jiang, Y.L.; Ren, Y.M.; Ruan, K.; Chen, Y.; Zhou, C.Z.
Structure and catalytic mechanism of yeast 4-amino-4-deoxychorismate lyase
J. Biol. Chem.
288
22985-22992
2013
Saccharomyces cerevisiae (Q03266), Saccharomyces cerevisiae
brenda
ORourke, P.E.; Eadsforth, T.C.; Fyfe, P.K.; Shepherd, S.M.; Hunter, W.N.
Pseudomonas aeruginosa 4-amino-4-deoxychorismate lyase: spatial conservation of an active site tyrosine and classification of two types of enzyme
PLoS ONE
6
e24158
2011
Pseudomonas aeruginosa, Pseudomonas aeruginosa (Q9HZN6)
brenda
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Enzyme Nomenclature
COMMENTARY
4.1.3.38-RECOMMENDED NAME
A pyridoxal-phosphate protein; A pyridoxal-phosphate protein.; a pyridoxal-phosphate protein. Forms part of the folate biosynthesis pathway. Acts on 4-amino-4-deoxychorismate, the product of EC 6.3.5.8, aminodeoxychorismate synthase, to form p-aminobenzoate---4-amino-4-deoxychorismate = 4-aminobenzoate + pyruvate
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