Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
4-amino-4-deoxychorismate = 4-aminobenzoate + pyruvate
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
catalytic mechanism, overview
Q03266
evolution
Q03266
4-amino-4-deoxychorismate lyases can be divided into two classes of dimeric and monomeric enzyme, respectively
physiological function
Q9HZN6
the enzyme is active in folate biosynthesis and essential for the cell growth of the pathogen
evolution
Q9HZN6
structure comparisons with related enzymes, overview. PabC enzymes can be classified into two groups depending upon whether an active site and structurally conserved tyrosine is provided from the polypeptide that mainly forms an active site or from the partner subunit in the dimeric assembly
additional information
Q03266
the catalytic residue Lys251 covalently binds the cofactor pyridoxal 5'-phosphate
additional information
Q9HZN6
structure-activity relationship of PabC, ligand binding modeling and reaction mechanism, overview. No structure of PabC in complex with ligands is achieved, but a computational model of the catalytic intermediate docked into the enzyme active site is generated. A conserved tyrosine helps to create a hydrophobic wall on one side of the active site that provides important interactions to bind the catalytic intermediate, but it does not appear to participate in interactions with the C atom that undergoes an sp2 to sp3 conversion as pyruvate is produced. An active site threonine hydroxyl contributes a proton used in the reduction of the substrate methylene to pyruvate methyl in the final stage of the mechanism
4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
-
-
-
?
4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
-
-
-
?
4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
-
-
-
?
4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
-
-
-
?
4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
-
-
-
?
4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
B8Y8J0, -
-
-
-
?
4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
P28305
-
-
?
4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
Q5SKM2
-
-
-
?
4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
Q9HZN6
-
-
-
?
4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
-, Q8IKP7
-
-
-
?
4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
Q03266
-
-
-
?
4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
-
re-face specificity
-
?
4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
-
last step of the 4-aminobenzoate branch
-
-
?
4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
Q9HZN6
molecular modeling of the catalytic intermediate, overview
-
-
?
4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
Q03266
simulation and validation of the substrate-binding model, overview
-
-
?
4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
-, Q8IKP7
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
-
-
?
4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
B8Y8J0, -
-
-
-
?
D-alanine + pyridoxal 5'-phosphate
pyridoxamine 5'-phosphate + pyruvate
-
L-alanine and other D- and L-amino acids tested are inert as substrates of transamination
-
r
additional information
?
-
-, Q8IKP7
the enzyme also shows a pyridoxal 5'-phosphate-dependent transamination activity with D-asparate, EC 2.6.1.1, but PF14_0557 is unable to transaminate branched-chain amino acids L-leucine, L-isoleucine and L-valine. The enzyme also fails completely to carry out a transamination reaction between L-glutamate and 4-methyl 2-oxovalerate
-
-
-
4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
-
-
-
?
4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
-
-
-
?
4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
Q9HZN6
-
-
-
?
4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
-, Q8IKP7
-
-
-
?
4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
Q03266
-
-
-
?
4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
-
last step of the 4-aminobenzoate branch
-
-
?
D-alanine + pyridoxal 5'-phosphate
pyridoxamine 5'-phosphate + pyruvate
-
L-alanine and other D- and L-amino acids tested are inert as substrates of transamination
-
r
small yellow prisms crystals in the unliganded form obtained using the sparse-matrix method along with the hanging-drop vapor-difussion method
-
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
Q9HZN6
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 100mM NaCl, 20mM 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
Q03266
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
Q5SKM2
DEAE-Sephacel, phenyl-Sepharose column, Superose 6 gel filtration column, Mono Q, Superose 12 column, yield 400-800fold
-
fractionation with ammonium sulfate pH 7.5, DEAE-Sephacel column, butyl-Sepharose 4B column, Gigapite column
-
fractionation with ammonium sulfate, DEAE-Toyopearl column, butyl-Toyopearl column and Mono Q column
-
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
-
recombinant His6-tagged enzyme from Escherichia coli by metal affinity chromatography
-, Q8IKP7
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
Q9HZN6
recombinant His-tagged wild-type and selenomethionine-labeled enzymes from Escherichia coli strain BL21(DE3) and B834(DE3), respectively, by nickel affinity chromatography
Q03266
nickel affinity column chromatography; nickel affinity column chromatography
B8Y8J0, -
Resource ISO column chromatography, ammonium sulfate precipitation, Resource Q column chromatography, and Superdex 75 gel filtration
Q5SKM2
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
-
expression in Escherichia coli JM109
-
expression in Escherichia coli MC1000 cells
P28305
gene PF14_0557, functional overexpression as His6-tagged protein in Escherichia coli cells
-, Q8IKP7
gene pabC, expression of His6-tagged enzyme with TEV protease cleavage site in Escherichia coli strain BL21(DE3) GOLD
Q9HZN6
recombinant expression of His-tagged wild-type and selenomethionine-labeled enzymes in Escherichia coli strain BL21(DE3) and B834(DE3), respectively
Q03266
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
-
expressed in Escherichia coli BL21(DE3) cells; expressed in Escherichia coli BL21(DE3) cells
B8Y8J0, -
expressed in Escherichia coli B834 (DE3) cells
Q5SKM2
K180A
Q03266
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
N360A
Q03266
site-directed mutagenesis, inactive mutant
N360D
Q03266
site-directed mutagenesis, inactive mutant
T30A
Q03266
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
additional information
B8Y8J0, -
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
-
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
-
BRENDA home
login
history
all enzymes
BRENDA home
History
Enzyme Nomenclature
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
GENERAL INFORMATIONORGANISMUNIPROT ACCESSION NO.COMMENTARYLITERATUREevolutionQ032664-amino-4-deoxychorismate lyases can be divided into two classes of dimeric and monomeric enzyme, respectivelyphysiological functionQ9HZN6the enzyme is active in folate biosynthesis and essential for the cell growth of the pathogenevolutionQ9HZN6structure comparisons with related enzymes, overview. PabC enzymes can be classified into two groups depending upon whether an active site and structurally conserved tyrosine is provided from the polypeptide that mainly forms an active site or from the partner subunit in the dimeric assemblyadditional informationQ03266the catalytic residue Lys251 covalently binds the cofactor pyridoxal 5'-phosphateadditional informationQ9HZN6structure-activity relationship of PabC, ligand binding modeling and reaction mechanism, overview. No structure of PabC in complex with ligands is achieved, but a computational model of the catalytic intermediate docked into the enzyme active site is generated. A conserved tyrosine helps to create a hydrophobic wall on one side of the active site that provides important interactions to bind the catalytic intermediate, but it does not appear to participate in interactions with the C atom that undergoes an sp2 to sp3 conversion as pyruvate is produced. An active site threonine hydroxyl contributes a proton used in the reduction of the substrate methylene to pyruvate methyl in the final stage of the mechanismSUBSTRATEPRODUCTREACTION DIAGRAMORGANISMUNIPROT ACCESSION NO.COMMENTARY
Help
print
top
SBML Output
Soap
BRENDA on Facebook