Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 4.1.3.38 - aminodeoxychorismate lyase and Organism(s) Saccharomyces cerevisiae and UniProt Accession Q03266

for references in articles please use BRENDA:EC4.1.3.38
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: Q03266
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
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
-
4-amino-4-deoxychorismate lyase
-
-
-
-
ADC lyase
-
-
-
-
ADCL
-
-
-
-
enzyme X
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4-amino-4-deoxychorismate = 4-aminobenzoate + pyruvate
show the reaction diagram
catalytic mechanism, overview
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, one molecule of cofactor is deeply buried in the cleft between domains I and II, pyridoxal 5'-phosphate adopts the re-face specificity facing the protein side and is covalently linked to the catalytic residue Lys251 by forming an internal aldimine bond, Schiff base linkage
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
4-amino-4-deoxychorismate lyases can be divided into two classes of dimeric and monomeric enzyme, respectively
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and selenomethionine-labeled enzymes from Escherichia coli strain BL21(DE3) and B834(DE3), respectively, by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of His-tagged wild-type and selenomethionine-labeled enzymes in Escherichia coli strain BL21(DE3) and B834(DE3), respectively
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team