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Information on EC 4.1.3.38 - aminodeoxychorismate lyase and Organism(s) Escherichia coli and UniProt Accession P28305

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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:
Escherichia coli
UNIPROT: P28305
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The taxonomic range for the selected organisms is: Escherichia coli
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
-
-
-
-
aminodeoxychorismate synthase
-
-
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
-
-
?
4-amino-4-deoxychorismate
4-aminobenzoate + pyruvate
show the reaction diagram
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 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
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
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
pyridoxal 5'-phosphate
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29700
2 * 29700, most likely dimeric, SDS-PAGE
50000
gel filtration
25000
-
2 * 25000, SDS-PAGE
29715
-
2 * 29715
50000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 29700, most likely dimeric, SDS-PAGE
dimer
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
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
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
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli MC1000 cells
expression in Escherichia coli JM109
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ye, Q.Z.; Liu, J.; Walsh, C.T.
p-Aminobenzoate synthesis in Escherichia coli: purification and characterization of PabB as aminodeoxychorismate synthase and enzyme X as aminodeoxychorismate lyase
Proc. Natl. Acad. Sci. USA
87
9391-9395
1990
Escherichia coli
Manually annotated by BRENDA team
Green, J.M.; Merkel, W.K.; Nichols, B.P.
Characterization and sequence of Escherichia coli pabC, the gene encoding aminodeoxychorismate lyase, a pyridoxal phosphate-containing enzyme
J. Bacteriol.
174
5317-5323
1992
Escherichia coli (P28305), Escherichia coli
Manually annotated by BRENDA team
Green, J.M.; Nichols, B.P.
p-Aminobenzoate biosynthesis in Escherichia coli. Purification of aminodeoxychorismate lyase and cloning of pabC
J. Biol. Chem.
266
12971-12975
1991
Escherichia coli
Manually annotated by BRENDA team
Viswanathan, V.K.; Green, J.M.; Nicholas, B.P.
Kinetic characterization of 4-amino 4-deoxychorismate synthase from Escherichia coli
J. Bacteriol.
177
5918-5923
1995
Escherichia coli
Manually annotated by BRENDA team
Nakai, T.; Mizutani, H.; Miyahara, I.; Hirotsu, K.; Takeda, S.; Jhee, K.H.; Yoshimura, T.; Esaki, N.
Three-dimensional structure of 4-amino-4-deoxychorismate lyase from Escherichia coli
J. Biochem.
128
29-38
2000
Escherichia coli
Manually annotated by BRENDA team
Jhee, K.H.; Yoshimura, T.; Miles, E.W.; Takeda, S.; Miyahara, I.; Hirotsu, K.; Soda, K.; Kawata, Y.; Esaki, N.
Stereochemistry of the transamination reaction catalyzed by aminodeoxychorismate lyase from Escherichia coli: close relationship between fold type and stereochemistry
J. Biochem.
128
679-686
2000
Escherichia coli
Manually annotated by BRENDA team
Nichols, B.P.; Green, J.M.
Cloning and sequencing of Escherichia coli ubiC and purification of chorismate lyase
J. Bacteriol.
174
5309-5316
1992
Escherichia coli
Manually annotated by BRENDA team
Culbertson, J.; Chung, D.; Ziebart, K.; Espiritu, E.; Toney, M.
Conversion of aminodeoxychorismate synthase into anthranilate synthase with Janus mutations Mechanism of pyruvate elimination catalyzed by chorismate enzymes
Biochemistry
54
2372-2384
2015
Escherichia coli
Manually annotated by BRENDA team