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Information on EC 4.3.1.1 - aspartate ammonia-lyase and Organism(s) Campylobacter jejuni and UniProt Accession Q0PC50

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EC Tree
     4 Lyases
         4.3 Carbon-nitrogen lyases
             4.3.1 Ammonia-lyases
                4.3.1.1 aspartate ammonia-lyase
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This record set is specific for:
Campylobacter jejuni
UNIPROT: Q0PC50 not found.
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The taxonomic range for the selected organisms is: Campylobacter jejuni
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
aspartase, l-aspartase, aspartate ammonia-lyase, aspartate ammonia lyase, l-aspartate ammonia-lyase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aspartate:ammonia lyase
reverse reaction
ammonia-lyase, aspartate
-
-
-
-
aspartase
-
-
-
-
fumaric aminase
-
-
-
-
L-aspartase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
beta-elimination
enzyme directly forms fumarate by beta-elimination of ammonia
C-N bond cleavage
oxidative and non-oxidative catabolic mechanism exists
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
L-aspartate ammonia-lyase (fumarate-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9027-30-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-aspartate
fumarate + NH3
show the reaction diagram
-
-
-
?
additional information
?
-
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
L-aspartate
fumarate + NH3
show the reaction diagram
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
aspartase activity is stimulated about 2fold by inclusion of 6 mM magnesium chloride in the assay
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KCl
aspartase activity is severely inhibited by potassium chloride
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10 - 38.2
L-aspartate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.23
strain 81-176 aspA mutant
119.7
at pH 7.0, recombinant produced and purified AspA enzyme
191
at pH 8.0, recombinant produced and purified AspA enzyme
2.06
wild-type aspartase activity, spectrophotometric assay in cell-free extracts from cells grown to early stationary phase in BHI-FCS medium
93.7
at pH 6.5, recombinant produced and purified AspA enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Cj0087; zoonotic pathogen, a number of avian species are reservoirs for this organism
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
strain NCTC 11168
Manually annotated by BRENDA team
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
over 24 h of microaerobic batch growth, the AspA specific enzyme activity increases 10fold and the relative abundance of the protein increases over 13fold. After transferring initially microaerobic cultures to oxygenlimiting conditions in the absence of an added electron acceptor, there is an immediate cessation of growth but an approximately 3fold rise in AspA specific activity up to 24 h correlated with a smaller increase in the abundance of the protein.
694233
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
After overexpression of the aspA gene in Escherichia coli BL21, the gene product is purified to homogeneity by ion-exchange and hydrophobic interaction chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
An aspartase mutant 81-176 unable to utilize any amino acid except serine (defective in microaerobic growth on multiple amino acids) and an aspA sdaA double-mutant (also lacking serine dehydratase) is cloned. The aspA gene is cloned into the pET101 expression vector and overexpressed in Escherichia coli BL21
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Morris, G.A.; Ikumapayi, U.N.; Antonio, M.; Howie, S.R.; Adegbola, R.A.
A novel Campylobacter jejuni sequence type from a culture-negative patient in the Gambia
Mol. Microbiol.
69
77-93
2008
Campylobacter jejuni (Q0PC50), Campylobacter jejuni
Manually annotated by BRENDA team