Information on EC 4.3.1.1 - aspartate ammonia-lyase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
4.3.1.1
-
RECOMMENDED NAME
GeneOntology No.
aspartate ammonia-lyase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-aspartate = fumarate + NH3
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
addition
-
reverse reaction
beta-elimination
enzyme directly forms fumarate by beta-elimination of ammonia
C-N bond cleavage
Deamination
elimination
-
-
of NH3, C-N bond cleavage
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Alanine, aspartate and glutamate metabolism
-
-
L-glutamate degradation II
-
-
Metabolic pathways
-
-
glutamate and glutamine metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
L-aspartate ammonia-lyase (fumarate-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9027-30-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Bacterium cadaveris
Cj0087; zoonotic pathogen, a number of avian species are reservoirs for this organism
UniProt
Manually annotated by BRENDA team
KUC-1
-
-
Manually annotated by BRENDA team
KUC-1
-
-
Manually annotated by BRENDA team
strain J2, plasmid carrying the L-aspartase gene
-
-
Manually annotated by BRENDA team
Frog
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain HI-23459
-
-
Manually annotated by BRENDA team
CNRZ 313
-
-
Manually annotated by BRENDA team
CNRZ 313
-
-
Manually annotated by BRENDA team
ssp. freudenreichii; ssp. shermanii
-
-
Manually annotated by BRENDA team
NCDO 566, ATCC 9614, MNS, DRI, KFA
-
-
Manually annotated by BRENDA team
shark
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
AspA increases acid survival by producing ammonia. Addition of aspartate increases acid survival of the wild type but not the AspA knockout mutant
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-malate
?
show the reaction diagram
-
L-malic acid
-
-
-
fumarate + hydroxylamine
?
show the reaction diagram
fumarate + hydroxylamine
L-aspartate
show the reaction diagram
fumarate + NH3
L-aspartate
show the reaction diagram
fumarate + NH4Cl
?
show the reaction diagram
-
substrates for reverse reaction
-
-
-
fumaric acid + NH3
L-aspartic acid
show the reaction diagram
hydrazine + fumarate
2-hydrazinosuccinic acid
show the reaction diagram
-
reverse reaction, 100% conversion after 1 day at pH 7
-
-
r
hydroxylamine + fumarate
N-hydroxyaspartic acid
show the reaction diagram
-
reverse reaction, 100% conversion after 20 min at pH 7
-
-
r
L-asparagine
?
show the reaction diagram
-
L-Asn
-
-
-
L-aspartate
fumarate + NH3
show the reaction diagram
L-aspartate-di-t-butylester
?
show the reaction diagram
-
very low activity
-
-
-
L-aspartatephenylmethyl ester
?
show the reaction diagram
-
very low activity
-
-
-
L-aspartic acid alpha-amide
(2E)-4-amino-4-oxobut-2-enoate + NH3
show the reaction diagram
-
catalyzed by mutant enzyme K327N, no activity with wild-type enzyme
-
-
?
L-benzyl-aspartate
?
show the reaction diagram
-
-
-
-
-
methoxylamine + fumarate
N-methoxyaspartic acid
show the reaction diagram
-
reverse reaction, 100% conversion after 6 days at pH 8 and after 12 days at pH 7
-
-
r
methylamine + fumarate
N-methylaspartic acid
show the reaction diagram
-
reverse reaction, 100% conversion after 7 day at pH 8
-
-
r
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
Co2+
-
activates at pH 7.0
K+
-
activates
Li+
-
activates
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(1-aminopropyl)-phosphonate
-
-
(3-aminopropyl)-phosphonate
-
-
(aminomethyl)-phosphonate
-
-
2,3-diphosphoglycerate
-
-
2-hydroxy-3-nitropropionate
-
-
2-mercaptoethanol
-
inactivation above 10 mM
3-nitropropanoate
-
-
3-nitropropionate
5,5'-dithiobis(2-nitrobenzoate)
ammonium
-
-
aspartate beta-semialdehyde
Ba2+
-
2 mM, 98% inhibition
beta-aspartylhydrazine
-
-
Ca2+
-
10 mM, 18% loss of activity
CTP
-
allosteric inhibition, moderate decrease in activity
cytidine
-
allosteric inhibition, moderate decrease in activity
D-2-methylmalate
-
-
D-Aspartate
-
competitive
D-malate
diethyldicarbonate
-
reactivated by hydroxylamine
Diethylpyrocarbonate
-
inactivation, reactivation with NH2OH, aspartate, fumarate and chloride protect
dimethyl sulfoxide
-
nonspecific
DL-2-amino-3-phosphonopropionate
-
-
DL-2-amino-4-phosphonobutyrate
DL-2-bromosuccinate
-
-
DL-2amino-3-phosphonopropanoate
-
-
ethanol
-
moderate, nonspecific
fumarate
fumaric acid aldehyde
-
-
-
fumaric acid aldehyde ethyl ester
-
-
guanidine hydrochloride
-
at concentrations lower than 1 M, activity is gradually decreased suggesting the existence of the native tetrameric form with denaturation intermediates such as dimeric and monomeric forms of the enzyme. At higher concentrations above 1 M, the enzyme completely lost the activity, suggesting that the enzyme structure is completely denatured
Hg2+
-
2 mM, 98% inhibition
HgCl2
-
1 mM, 89.5% inhibition
hydroxylamine
-
competitive
iodoacetamide
-
-
iodoacetate
-
1 mM, 94% inhibition
K+
-
2 mM, 98% inhibition
L-2-chlorosuccinate
-
-
L-malate
-
-
Mercaptosuccinate
-
-
methanol
-
moderate, nonspecific
Methylsuccinate
-
-
MgCl2
-
inhibitor at high concentrations (above 10 mM)
N-acetyl-L-aspartate
-
-
N-ethylmaleimide
NaCN
-
1 mM, 42% inhibition
Ni2+
-
2 mM, 98% inhibition
o-phospho-D-serine
O-phospho-L-serine
-
competitive
p-chloromercuribenzoate
-
0.1 mM, 100% inhibition
p-hydroxymercuribenzoate
Phosphoglycolate
-
-
Semicarbazide hydrochloride
-
1 mM, 30% inhibition
succinate
Zn2+
-
0.0005 mM, 40% loss of activity
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Acetic anhydride
-
activation up to 7.5fold, allosteric
acid anhydride
-
activates
-
adenosine
-
activation to 120-130%, allosteric
alpha-methyl-DL-aspartate
AMP
-
allosteric activation, restores original activity of trypsin-treated enzyme
D-Aspartate
-
-
Dimethylsulfoxide
-
activates
glycerol
-
activates
GTP
-
allosteric activation, restores original activity of trypsin-treated enzyme
guanosine
-
activation to 120-130%, allosteric
L-aspartate
-
activates the fumarate-amination reaction
N-hydroxysuccinimide acetate
-
activates
-
o-phospho-D-serine
-
-
Propylene glycol
-
activates
subtilisin BPN'
-
activates
-
Trypsin
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.58 - 2.5
aspartate
0.2 - 244
fumarate
1.54 - 308
hydrazine
2.78 - 151
hydroxylamine
0.54 - 163
L-aspartate
2.1 - 28.3
L-aspartic acid
1450
L-aspartic acid alpha-amide
-
pH 7.0, 30°C
1.61 - 85
NH3
20
NH4+
-
-
additional information
L-aspartate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
90
fumarate
Bacillus sp. YM55-1
-
reverse reaction
92 - 94
hydrazine
31 - 99
hydroxylamine
0.1 - 190
L-aspartate
59 - 89
NH3
additional information
L-aspartate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000016 - 2.7
L-aspartate
97
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.1
2,3-diphosphoglycerate
-
-
0.83
3-nitropropanoate
-
-
0.01 - 2
3-nitropropionate
1.19 - 2.2
ammonium
0.4 - 68
D-malate
0.66
DL-2amino-3-phosphonopropanoate
-
-
0.165 - 2.83
fumarate
0.2
o-phospho-D-serine
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.008
-
strain Angola
0.02
-
strain A16
0.028
-
pestoides D
0.039
-
pestoides F
0.042
-
pestoides B
0.044
-
pYV- (lacking low-calcium response plasmid into pseudogenes), 4 mM Ca2+, 250 mmol Tris/HCl buffer, 5.0 mmol MgCl2
0.052
-
pestoides E
0.057
-
pestoides C
0.06
-
pYV+ (containing low-calcium response plasmid into pseudogenes), 4 mM Ca2+, 250 mmol Tris/HCl buffer, 5.0 mmol MgCl2
0.064
-
pestoides A
0.072
-
strain TX83-0489
0.075
-
pYV+ (containing low-calcium response plasmid into pseudogenes), 250 mmol Tris/HCl buffer, 5.0 mmol MgCl2
0.137
-
strain PB1
0.2
-
mutant L363V, 50 mM HEPES, 50 mM HEPES, 10 mM Mg acetate, 20 mM L-aspartate; mutant Y146D, 50 mM HEPES, 10 mM Mg acetate, 20 mM L-aspartate; recombinant enzyme, 50 mM HEPES, 10 mM Mg acetate, 20 mM L-aspartate
0.202
-
strain WA; strain Windblad
0.207
-
strain E705
0.23
strain 81-176 aspA mutant
2.06
wild-type aspartase activity, spectrophotometric assay in cell-free extracts from cells grown to early stationary phase in BHI-FCS medium
72
-
double mutant L363V/Y146D, 50 mM HEPES, 10 mM Mg acetate, 20 mM L-aspartate
80
-
50 mM HEPES, 10 mM Mg acetate, 20 mM L-aspartate
93.7
at pH 6.5, recombinant produced and purified AspA enzyme
119.7
at pH 7.0, recombinant produced and purified AspA enzyme
167
-
30°C
191
at pH 8.0, recombinant produced and purified AspA enzyme
236.8
-
-
301
-
pH 8.5, 30°C
700
-
30°C
800
-
55C, pH 8.0
2200
-
55C
2500
-
65C, pH 7.5
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
deamination of L-aspartic acid alpha-amide, mutant enzyme K327N
6.3
-
monomeric mutant enzyme maspase 1
6.8
-
dimeric mutant enzyme maspase 2
7.1
-
tetrameric mutant enzyme maspase 3
7.3
-
N-ethylmaleimide-modified enzyme, in the absence of MgCl2
7.7
-
in the absence of MgCl2
7.8
-
in the absence of MgCl2
7.9
-
acetylated enzyme
8.3
-
native enzyme in the absence of MgCl2
9
-
mutant C14
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8
-
mutant N217K/T233R/V367G
7 - 9
-
pH 7.0: about 40% of maximal activity, pH 9.0: about 90% of maximal activity, substrate: L-aspartate, wild-type enzyme
7.5 - 9
-
pH 7.5: about 70% of maximal activity, pH 9.0: about 85% of maximal activity, substrate: L-aspartic acid, mutant enzyme K327N
7.8 - 9.3
-
evolved enzyme
additional information
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
optimum temperature for reactivation
40
-
acetylated enzyme
65
-
at pH 7.5
additional information
-
temperature dependence of kinetic parameters
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 35
-
no reactivation between 0-10°C, linear increase at 10-25°C, with a level off between 25-35°C and completely stopped at 35°C
15 - 45
-
-
50
-
60 min, 80% residual activity
additional information
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50859
-
4 * 50859, calculation from sequence of amino acid
51218
-
4 * 51218, calculation from sequence of amino acid
51630
4 * 51630, deduced from gene sequence
52190
-
4 * 52190, calculation from sequence of amino acid
52224
-
4 * 52224, calculation from sequence of amino acid
52470
-
mass of monomer, determined by an ESI-qTOF mass spectrometer
52540
-
mass of monomer, determined by an ESI-qTOF mass spectrometer
56000
-
1 * 56000, mutant enzyme maspase 1, SDS-PAGE; 2 * 56000, mutant enzyme maspase 2, SDS-PAGE; 4 * 56000, mutant enzyme maspase 3, SDS-PAGE
56200
-
monomeric mutant enzyme maspase 1, gel filtration
109600
-
dimeric mutant enzyme maspase 2, gel filtration
173000
-
sedimentation equilibrium analysis
180000
Bacterium cadaveris
-
sucrose density gradient centrifugation
192000
-
gel filtration
193000
198000
-
pore gradient polyacrylamide
200000
213800
-
tetrameric mutant enzyme maspase 3, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
monomer
tetramer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
functional sites, mechanism
-
in an unliganded state and in complex with L-aspartate at 2.4 and 2.6 A resolution, respectively. AspB forces the bound substrate to adopt a high-energy, enediolate-like conformation that is stabilized, in part, by an extensive network of hydrogen bonds between residues Thr101, Ser140, Thr141, and Ser319 and the substrate's beta-carboxylate group. Substrate binding induces a large conformational change in the SS loop, residuesG317SSIMPGKVN326, from an open conformation to one that closes over the active site. In the closed conformation, the strictly conserved SS loop residue Ser318 is at a suitable position to act as a catalytic base, abstracting the Cbeta proton of the substrate in the first step of the reaction mechanism. The small C-terminal domain of AspB plays an important role in controlling the conformation of the SS loop
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9
-
mutant enzyme by random mutagenesis
6023
5.5 - 9
-
-
6029
6 - 9
-
-
729405
7 - 8
-
wild-type enzyme
6023
7 - 9
-
mutant enzyme by site-directed mutagenesis
6023
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15 - 60
-
15C: 90% loss of maximal activity, 60C: 90% loss of activity
60
-
complete loss of activity after 5 min
75
-
5 min, stable
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
1 M guanidine hydrochloride, 80% residual activity
-
10% glycerol protects against heat inactivation
-
after incubation in the presence of guanidine hydrochloride at a concentration of 1.1 M 50% loss of activity after 60 min
-
after incubation in the presence of guanidine hydrochloride at a concentration of 1.1 M complete inactivation
-
enzyme is fairly stable in the presence of high concentrations of ammonium sulfate, potassium phosphate, and KCl
-
glycerol stabilizes
-
irreversible inactivation during prolonged centrifugation
Bacterium cadaveris
-
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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, pH 7.0, 2% 2-mercaptoethanol, several months, no loss of activity
-
-20°C, stable for 1 month
-
-20°C, stable for a few weeks
-
-20°C, stable for several months
-
-70°C stable over 3 months
-
-70°C, stable for 1 month without addition of salts or glycerol
-
2-mercaptoethanol and dithiothreitol protect enzyme against inactivation during storage
-
4C, in the presence of various salts thiol compounds, or glycerol stable for 2 weeks
-
4°C, loss of activity after 1 month independently of the presence of glycerol or MgCl2
-
enzyme activity can be maintained by freezing up to 6 months in the ammonium sulfate precipitate
-
the catalytic function of the purified enzyme which stored at -70°C until use remains stable for at least 1 month at 4°C without appreciable loss of enzymatic activity
-
additional information
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
by using a combination of diethylaminoethyl cellulose, Red A-agarose,and Sepharose 6B chromatography
-
immobilized metal ion affinity chromatography (Ni2+)
-
partially purified by heat precipitation and saturation with ammonium sulfate
-
recombinant enzyme containing a C-terminal His6 tag is purified by one-step affinity purification
-
recombinant enzyme expressed in Escherichia coli
transformed cells of Escherichia coli JRG1476 are used to prepare the aspA products: proteins are fractionated in buffer with a NaCl gradient on successive anion-exchange Sepharose XL high-capacity and Source 30Q high-resolution chromatography columns
-
transformed cells of Escherichia coli JRG1476 are used to prepare the aspA products: proteins are fractionated in purification buffer with a NaCl gradient on successive anion-exchange Sepharose XL high-capacity and Source 30Q high-resolution chromatography columns
-
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
AspB is expressed in Escherichia coli
-
cloned and overexpressed in Escherichia coli TOP10
-
expression in Escherichia coli
-
expression of His-tagged wild-type enzyme and His-tagged mutant enzyme K327N in Escherichia coli
-
functional and inactive aspA are cloned and expressed in AspA-deficient Escherichia coli
-
functional and inactive aspA of Yersinia pestis KIM is cloned and expressed in AspA-deficient Escherichia coli
-
His-tagged version expressed in Escherichia coli TOP10
-
overexpression in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
increased expression at acidic pH
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H134A
no loss of activity
H188A
-
mutation of His188 to Ala only changes the active site structure and slightly elongates the distance of Cbeta proton of substrate with Ser318, causing the enzyme to remain significant but reduced activity
I320A
-
SS-loop mutant, about 2% of wild-type activity
K183A
complete loss of activity
M321A
-
SS-loop mutant, less than 1% of wild-type activity
P322A
-
SS-loop mutant, about 70% of wild-type activity
S318A
-
SS-loop mutant, complete loss of activity
S319A
-
SS-loop mutant, about 30% of wild-type activity
H188A
-
responsible for binding the amino group of the substrate
H188K
-
responsible for binding the amino group of the substrate
H188Q
-
responsible for binding the amino group of the substrate
H188R
-
responsible for binding the amino group of the substrate
K324A
-
responsible for binding the C1 carboxylate group of substrate
K324D
-
responsible for binding the C1 carboxylate group of substrate
K324H
-
responsible for binding the C1 carboxylate group of substrate
K324R
-
responsible for binding the C1 carboxylate group of substrate
K324S
-
responsible for binding the C1 carboxylate group of substrate
K324V
-
responsible for binding the C1 carboxylate group of substrate
N142A
-
responsible for binding the amino group of the substrate
N142Q
-
responsible for binding the amino group of the substrate
N326A
-
responsible for binding the C1 carboxylate group of substrate
N326Q
-
responsible for binding the C1 carboxylate group of substrate
S140A
-
implicated in binding the C4 carboxylate group of substrate
S140G/T141G
-
implicated in binding the C4 carboxylate group of substrate
S140K
-
implicated in binding the C4 carboxylate group of substrate
S140K/T141K
-
implicated in binding the C4 carboxylate group of substrate
S140R
-
implicated in binding the C4 carboxylate group of substrate
T101A
-
responsible for binding the amino group of the substrate
T101S
-
responsible for binding the amino group of the substrate
T141A
-
implicated in binding the C4 carboxylate group of substrate
T141K
-
implicated in binding the C4 carboxylate group of substrate
T141R
-
implicated in binding the C4 carboxylate group of substrate
T141V
-
implicated in binding the C4 carboxylate group of substrate
T187A
-
responsible for binding the C1 carboxylate group of substrate
T187S
-
responsible for binding the C1 carboxylate group of substrate
C141S/C274A
-
elimination of sensitivity to inactivation
K126R
-
replacement of Lys126 with Arg increases the activity of the enzyme
K140I
-
Km value 10fold higher than wild type, comparable increase in Ki for competitive inhibitors
K327N
-
mutant enzyme catalyzes the deamination of L-aspartic acid alpha-amide, 13.5fold increase in Km-value for L-aspartate compared to wild-type value
K55R
-
completeley inactive and insoluble protein, reactivation by an artificial chaperone system including beta-cyclodextrin and cetyltrimethylammonium bromide
L363V
-
single mutant
Y146D
-
single mutant
Y146D/L363V
-
double mutant
V363L
-
mutation in primary structure causing dramatic differences in catalytic activity do not promote significant changes in secondary structure
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
100% activity recovery is observed when the enzyme is renatured by dilution at concentrations below 1 M guanidine hydrochloride, the renaturation yield at concentrations above 1 M is 40%. The dissociation process from native tetramer to dimer is reversible but the dissociation process from dimer to monomer is not reversible.
-
denaturation by addition of high concentrations of guanidine-HCl leads to reversible dissociation and reassembly of the tetrameric structure
hydroxylamine reactivates diethyldicarbonate treated enzyme
-
reactivation of trypsin activated and native enzyme by dilution after inactivation by 4 M guanidine-HCl
-
regains its activity and quaternary structure upon dilution
-
renaturation by dialysis against 50 mM Tris-HCl buffer ,pH 8.0, at 4C for 2 days
-
renaturation by different inducers
-
reversible denaturation is influenced by various environmental factors
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
scaled-down method for determination of aspartase activity in a 96-well microtitre plate
biotechnology
food industry
-
propionic acid bacteria isolates originating from cheese show a wide range of aspartase activity. Aspartase activity is strain-dependent and each strain must be tested separately in order to be able to choose the most suitable starter culture for cheese production.70% of the 100 isolates tested, show very low levels of aspartate activity
industry
-
aspartate synthesis
medicine
-
involvement of enzyme in blood clotting and activation of plasminogen, overview
synthesis
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