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
4.1.3.38
-
RECOMMENDED NAME
GeneOntology No.
aminodeoxychorismate lyase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4-amino-4-deoxychorismate = 4-aminobenzoate + pyruvate
show the reaction diagram
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
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
beta-elimination
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
4-aminobenzoate biosynthesis
-
candicidin biosynthesis
-
Folate biosynthesis
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4-amino-4-deoxychorismate lyase
-
-
-
-
4-amino-4-deoxychorismate lyase
-, B8Y8J0
-
4-amino-4-deoxychorismate lyase
-, B8Y8J0
-
-
4-amino-4-deoxychorismate lyase
Q5SKM2
-
ADC lyase
-
-
-
-
ADC lyase
-, B8Y8J0
-
ADC lyase
-, B8Y8J0
-
-
ADC lyase
Q5SKM2
-
ADCL
-
-
-
-
enzyme X
-
-
-
-
PabC-2
B8Y8J0
-
PabC-2
B8Y8J0
-
-
TTHA0621 protein
Q5SKM2
-
CAS REGISTRY NUMBER
COMMENTARY
132264-33-6
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
BN117 cells
-
-
Manually annotated by BRENDA team
SG-5 cells
-
-
Manually annotated by BRENDA team
Mill. cv. Micro-Tom
-
-
Manually annotated by BRENDA team
PabC-2; strain FR-008
UniProt
Manually annotated by BRENDA team
strain FR-008
-
-
Manually annotated by BRENDA team
PabC-2; strain FR-008
UniProt
Manually annotated by BRENDA team
strain FR-008
-
-
Manually annotated by BRENDA team
putative 4-amino-4-deoxychorismate lyase; strain HB8
UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
show the reaction diagram
-
-
-
?
4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
show the reaction diagram
-
-
-
?
4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
show the reaction diagram
-
-
-
?
4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
show the reaction diagram
-
-
-
?
4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
show the reaction diagram
-
-
-
?
4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
show the reaction diagram
B8Y8J0, -
-
-
-
?
4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
show the reaction diagram
P28305
-
-
?
4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
show the reaction diagram
Q5SKM2, -
-
-
-
?
4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
show the reaction diagram
-
re-face specificity
-
?
4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
show the reaction diagram
-
last step of the 4-aminobenzoate branch
-
-
?
4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
show the reaction diagram
B8Y8J0, -
-
-
-
?
D-alanine + pyridoxal 5'-phosphate
pyridoxamine 5'-phosphate + pyruvate
show the reaction diagram
-
L-alanine and other D- and L-amino acids tested are inert as substrates of transamination
-
r
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
show the reaction diagram
-
-
-
?
4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
show the reaction diagram
-
-
-
?
4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
show the reaction diagram
-
last step of the 4-aminobenzoate branch
-
-
?
D-alanine + pyridoxal 5'-phosphate
pyridoxamine 5'-phosphate + pyruvate
show the reaction diagram
-
L-alanine and other D- and L-amino acids tested are inert as substrates of transamination
-
r
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
tightly bound
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
Q5SKM2, -
dependent on
pyridoxal 5'-phosphate
B8Y8J0, -
;
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
no feedback inhibition by physiological concentrations of 4-aminobenzoate, its glucose ester, or folates
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
assay at
37
-
-
assay at
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
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
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
50000
-
-
gel filtration
50000
-
P28305
gel filtration
50000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
-
2 * 25000, SDS-PAGE
dimer
P28305
2 * 29700, most likely dimeric, SDS-PAGE
dimer
-
2 * 29715
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
small yellow prisms crystals in the unliganded form obtained using the sparse-matrix method along with the hanging-drop vapor-difussion method
-
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, -
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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
-
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, -
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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. 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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expression in Escherichia coli JM109
-
expression in Escherichia coli MC1000 cells
P28305
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, -
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
-