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Information on EC 4.3.1.1 - aspartate ammonia-lyase and Organism(s) Pseudomonas aeruginosa

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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:
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
aspartase, l-aspartase, aspartate ammonia-lyase, aspartate ammonia lyase, l-aspartate ammonia-lyase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ammonia-lyase, aspartate
-
-
-
-
aspartase
-
-
-
-
fumaric aminase
-
-
-
-
L-aspartase
-
-
-
-
L-aspartate ammonia lyase
-
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
fumarate + NH3
L-aspartate
show the reaction diagram
-
-
-
r
L-aspartate
fumarate + NH3
show the reaction diagram
-
-
-
r
L-phenylalanine
cinnamic acid + NH3
show the reaction diagram
-
-
-
r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
the enzyme does not require metal ion for its activity. It is activated in the presence of metal ions. Mg2+ is the most effective
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2000
fumarate
pH 8.0, 35°C
0.346
L-aspartate
pH 8.0, 35°C
1.71
L-phenylalanine
pH 8.0, 35°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
13.64
fumarate
pH 8.0, 35°C
4.908
L-aspartate
pH 8.0, 35°C
8.002
L-phenylalanine
pH 8., 35°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.038
fumarate
pH 8.0, 35°C
14.18
L-aspartate
pH 8.0, 35°C
4.65
L-phenylalanine
pH 8.0, 35°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
31.21
substrate: L-aspartate, pH 8.0, 35°C
38.35
substrate: L-phenylalanine, pH 8.0, 35°C
5.42
substrate: fumarate, pH 8.0, 35°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
deamination reaction
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8
pH 5.0: about 80% of maximal activity, pH 8.0: maximal activity, pH 9.0: about 25% of maximal activity, deamination reaction
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
deamination reaction
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15 - 40
15°C: about 80% of maximal activity, 30°C: about 40% of maximal activity, 35: maximal activity, 40°C: about 90% of maximal activity, 50°C: about 30% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A072ZFI1_PSEAI
474
0
51070
TrEMBL
-
A0A8G4MTW2_PSEAI
474
0
51042
TrEMBL
-
A0A8G3YLE9_PSEAI
474
0
51054
TrEMBL
-
A0A8G3IQR8_PSEAI
474
0
51100
TrEMBL
-
A0A8G5R9D2_PSEAI
474
0
51082
TrEMBL
-
A0A8G7K903_PSEAI
474
0
51017
TrEMBL
-
A0A8G4GDK5_PSEAI
474
0
51100
TrEMBL
-
A0A8G6YET7_PSEAI
474
0
51100
TrEMBL
-
A0A2R3IPS3_PSEAI
474
0
51084
TrEMBL
-
A0A8G3D5Q2_PSEAI
474
0
51044
TrEMBL
-
A0A8G6N705_PSEAI
474
0
51052
TrEMBL
-
A0A485H477_PSEAI
583
0
63065
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
51000
recombinant His-tagged enzyme, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 51000, recombinant His-tagged enzyme, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
the enzyme retains 56% activity after 7 days of incubation
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli BL21
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
bioproduction of L-aspartic acid and cinnamic acid. From an initial concentration of 1000 mM of fumarate and 30 mM of L-phenylalanine, the enzyme converts 0.395 mM L-aspartic acid and 3.47 mM cinnamic acid, respectively
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Patel, A.T.; Akhani, R.C.; Patel, M.J.; Dedania, S.R.; Patel, D.H.
Bioproduction of L-aspartic acid and cinnamic Acid by L-aspartate ammonia lyase from Pseudomonas aeruginosa PAO1
Appl. Biochem. Biotechnol.
182
792-803
2017
Pseudomonas aeruginosa (Q9HTD7)
Manually annotated by BRENDA team