Information on EC 4.1.3.38 - aminodeoxychorismate lyase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
4.1.3.38
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RECOMMENDED NAME
GeneOntology No.
aminodeoxychorismate lyase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4-amino-4-deoxychorismate = 4-aminobenzoate + pyruvate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
beta-elimination
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
4-aminobenzoate biosynthesis
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Folate biosynthesis
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tetrahydrofolate metabolism
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SYSTEMATIC NAME
IUBMB Comments
4-amino-4-deoxychorismate pyruvate-lyase (4-aminobenzoate-forming)
A pyridoxal-phosphate protein. Forms part of the folate biosynthesis pathway. Acts on 4-amino-4-deoxychorismate, the product of EC 2.6.1.85, aminodeoxychorismate synthase, to form p-aminobenzoate.
CAS REGISTRY NUMBER
COMMENTARY hide
132264-33-6
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
plasmodial gene PF14_0557 encodes a functional ADCL; gene PF14_0557
UniProt
Manually annotated by BRENDA team
gene pabC
UniProt
Manually annotated by BRENDA team
Mill. cv. Micro-Tom
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Manually annotated by BRENDA team
putative 4-amino-4-deoxychorismate lyase; strain HB8
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
physiological function
the enzyme is active in folate biosynthesis and essential for the cell growth of the pathogen
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
show the reaction diagram
D-alanine + pyridoxal 5'-phosphate
pyridoxamine 5'-phosphate + pyruvate
show the reaction diagram
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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
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
show the reaction diagram
D-alanine + pyridoxal 5'-phosphate
pyridoxamine 5'-phosphate + pyruvate
show the reaction diagram
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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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-glutamate
D-Glu (in the absence of 2-oxoacids) inhibits the aminodeoxychorismate lyase activity of the enzyme
additional information
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no feedback inhibition by physiological concentrations of 4-aminobenzoate, its glucose ester, or folates
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
the absence of the enzyme in humans and its essentiality in various microbes suggests that inhibition of PabC offers the possibility of therapeutics targeting a range of microbial infections, potential of this protein for early stage drug discovery
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