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Information on EC 4.1.3.38 - aminodeoxychorismate lyase and Organism(s) Pseudomonas aeruginosa

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.3 Oxo-acid-lyases
                4.1.3.38 aminodeoxychorismate lyase
IUBMB Comments
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.
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This record set is specific for:
Pseudomonas aeruginosa
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The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
enzyme x, aminodeoxychorismate lyase, 4-amino-4-deoxychorismate lyase, adc lyase, pabc-2, pabc-1, ttha0621 protein, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4-amino-4-deoxychorismate lyase
ADC lyase
-
-
-
-
ADCL
-
-
-
-
enzyme X
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
beta-elimination
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
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
-
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
NATURAL SUBSTRATE
NATURAL 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
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
dependent on, the PLP methyl group makes van der Waals interactions with Gln147 and is positioned 3.2 A distant from the carbonyl oxygen of Val175, Ser237 interacts with the pyridoxal 5'-phosphate phosphate
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene pabC
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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
physiological function
the enzyme is active in folate biosynthesis and essential for the cell growth of the pathogen
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A3S3VYT0_PSEAI
271
0
29956
TrEMBL
-
A0A5E8W8X2_PSEAI
271
0
29886
TrEMBL
-
A0A485F1M6_PSEAI
271
0
30140
TrEMBL
-
A0A8G5UNJ9_PSEAI
271
0
29915
TrEMBL
-
A0A6A9JYU1_PSEAI
271
0
29797
TrEMBL
-
A0A8G4HPS2_PSEAI
271
0
29831
TrEMBL
-
A0A7M3A502_PSEAI
271
0
29869
TrEMBL
-
A0A8B5BEA2_PSEAI
271
0
29833
TrEMBL
-
A0A8B4ZQ99_PSEAI
271
0
29886
TrEMBL
-
A0A8G2KER5_PSEAI
271
0
29839
TrEMBL
-
A0A367MDS9_PSEAI
190
0
20725
TrEMBL
-
A0A3S0LX14_PSEAI
271
0
30006
TrEMBL
-
A0A8G4ZYP7_PSEAI
271
0
29826
TrEMBL
-
A0A8G4A651_PSEAI
271
0
29872
TrEMBL
-
A0A0D6H6T5_PSEAI
271
0
29856
TrEMBL
-
A0A080VS18_PSEAI
271
0
29855
TrEMBL
-
A0A8G4B6G8_PSEAI
271
0
29803
TrEMBL
-
A0A2R3IWF2_PSEAI
271
0
29996
TrEMBL
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
sequence comparisons, structure modeling of the catalytic intermediate and ligand-bound enzyme, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene pabC, expression of His6-tagged enzyme with TEV protease cleavage site in Escherichia coli strain BL21(DE3) GOLD
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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 (Q9HZN6), Pseudomonas aeruginosa
Manually annotated by BRENDA team