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EC Tree
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
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ammonia-lyase, aspartate
-
-
-
-
aspartate ammonia lyase
-
-
aspartate:ammonia lyase
reverse reaction
L-aspartate ammonia lyase
-
L-aspartate ammonia-lyase
ASPA
-
aspartase
-
-
-
-
aspartase
-
Val in in position 363
aspartase
-
Val in in position 363
aspartate ammonia-lyase
-
-
aspartate ammonia-lyase
-
-
aspartate ammonia-lyase
-
-
aspB
-
L-aspartate ammonia-lyase
-
L-aspartate ammonia-lyase
-
-
L-aspartate ammonia-lyase
-
-
L-aspartate ammonia-lyase
-
-
-
L-aspartate ammonia-lyase
-
-
maspase 1
-
insertion of a 15-peptide random peptide into the three domains of L-aspartase to enhance their mobility. After directed screening, the three isoforms of monomeric, dimeric and tetrameric enzyme (named maspase 1, maspase 2 and maspase 3) with the activity of L-aspartase are obtained
maspase 1
-
insertion of a 15-peptide random peptide into the three domains of L-aspartase to enhance their mobility. After directed screening, the three isoforms of monomeric, dimeric and tetrameric enzyme (named maspase 1, maspase 2 and maspase 3) with the activity of L-aspartase are obtained
-
maspase 2
-
insertion of a 15-peptide random peptide into the three domains of L-aspartase to enhance their mobility. After directed screening, the three isoforms of monomeric, dimeric and tetrameric enzyme (named maspase 1, maspase 2 and maspase 3) with the activity of L-aspartase are obtained
maspase 2
-
insertion of a 15-peptide random peptide into the three domains of L-aspartase to enhance their mobility. After directed screening, the three isoforms of monomeric, dimeric and tetrameric enzyme (named maspase 1, maspase 2 and maspase 3) with the activity of L-aspartase are obtained
-
maspase 3
-
insertion of a 15-peptide random peptide into the three domains of L-aspartase to enhance their mobility. After directed screening, the three isoforms of monomeric, dimeric and tetrameric enzyme (named maspase 1, maspase 2 and maspase 3) with the activity of L-aspartase are obtained
maspase 3
-
insertion of a 15-peptide random peptide into the three domains of L-aspartase to enhance their mobility. After directed screening, the three isoforms of monomeric, dimeric and tetrameric enzyme (named maspase 1, maspase 2 and maspase 3) with the activity of L-aspartase are obtained
-
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L-aspartate = fumarate + NH3
L-aspartate = fumarate + NH3
Escherichia coli
-
-
-
L-aspartate = fumarate + NH3
Bacillus sp. (in: Bacteria)
-
-
-
L-aspartate = fumarate + NH3
Hafnia alvei
-
-
-
L-aspartate = fumarate + NH3
-
-
-
-
L-aspartate = fumarate + NH3
Bacillus sp. (in: Bacteria) YM55-1
-
-
-
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elimination
-
-
of NH3, C-N bond cleavage
-
addition
-
reverse reaction
beta-elimination
enzyme directly forms fumarate by beta-elimination of ammonia
Deamination
-
-
C-N bond cleavage
-
-
C-N bond cleavage
oxidative and non-oxidative catabolic mechanism exists
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
L-aspartate ammonia-lyase (fumarate-forming)
-
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(S)-malate
?
-
L-malic acid
-
-
?
fumarate + hydroxylamine
?
fumarate + hydroxylamine
L-aspartate
fumarate + NH3
L-aspartate
fumarate + NH4Cl
?
-
substrates for reverse reaction
-
-
?
fumaric acid + NH3
L-aspartic acid
hydrazine + fumarate
2-hydrazinosuccinic acid
-
reverse reaction, 100% conversion after 1 day at pH 7
-
-
r
hydroxylamine + fumarate
N-hydroxyaspartic acid
-
reverse reaction, 100% conversion after 20 min at pH 7
-
-
r
L-asparagine
?
-
L-Asn
-
-
?
L-aspartate
fumarate + NH3
L-aspartate-di-t-butylester
?
-
very low activity
-
-
?
L-aspartatephenylmethyl ester
?
-
very low activity
-
-
?
L-aspartic acid alpha-amide
(2E)-4-amino-4-oxobut-2-enoate + NH3
catalyzed by mutant enzyme K327N, no activity with wild-type enzyme
-
-
?
L-benzyl-aspartate
?
-
-
-
-
?
L-phenylalanine
cinnamic acid + NH3
-
-
-
r
methoxylamine + fumarate
N-methoxyaspartic acid
-
reverse reaction, 100% conversion after 6 days at pH 8 and after 12 days at pH 7
-
-
r
methylamine + fumarate
N-methylaspartic acid
-
reverse reaction, 100% conversion after 7 day at pH 8
-
-
r
additional information
?
-
fumarate + hydroxylamine
?
Bacterium cadaveris
-
-
-
-
?
fumarate + hydroxylamine
?
-
-
-
-
?
fumarate + hydroxylamine
?
-
substrates for reverse reaction
-
-
?
fumarate + hydroxylamine
?
-
fumarate
-
-
?
fumarate + hydroxylamine
L-aspartate
-
at 64% the rate of NH3
-
?
fumarate + hydroxylamine
L-aspartate
-
at 64% the rate of NH3
-
?
fumarate + NH3
L-aspartate
-
-
-
?
fumarate + NH3
L-aspartate
-
-
-
?
fumarate + NH3
L-aspartate
-
-
-
?
fumarate + NH3
L-aspartate
-
-
-
?
fumarate + NH3
L-aspartate
-
-
-
r
fumarate + NH3
L-aspartate
important enzyme in production of L-aspartate
-
-
r
fumarate + NH3
L-aspartate
-
-
-
r
fumarate + NH3
L-aspartate
important enzyme in production of L-aspartate
-
-
r
fumarate + NH3
L-aspartate
-
-
-
?
fumarate + NH3
L-aspartate
-
-
-
r
fumaric acid + NH3
L-aspartic acid
-
-
-
-
?
fumaric acid + NH3
L-aspartic acid
-
-
-
-
?
L-aspartate
fumarate + NH3
-
r
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
-
-
?
L-aspartate
fumarate + NH3
-
-
-
?
L-aspartate
fumarate + NH3
-
r
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
-
-
?
L-aspartate
fumarate + NH3
-
r
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
-
-
?
L-aspartate
fumarate + NH3
-
-
-
-
r
L-aspartate
fumarate + NH3
-
key role in nitrogen metabolism by catalyzing the reversible elimination of NH3 from l-aspartate
-
-
r
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
Bacterium cadaveris
-
natural substrate
-
?
L-aspartate
fumarate + NH3
Bacterium cadaveris
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
-
-
?
L-aspartate
fumarate + NH3
-
-
-
r
L-aspartate
fumarate + NH3
-
-
-
r
L-aspartate
fumarate + NH3
-
-
-
?
L-aspartate
fumarate + NH3
-
-
-
-
?
L-aspartate
fumarate + NH3
-
-
-
r
L-aspartate
fumarate + NH3
-
-
-
-
r
L-aspartate
fumarate + NH3
-
-
-
r
L-aspartate
fumarate + NH3
-
r
-
?
L-aspartate
fumarate + NH3
-
r
-
?
L-aspartate
fumarate + NH3
-
r
-
?
L-aspartate
fumarate + NH3
-
r
-
?
L-aspartate
fumarate + NH3
-
r
-
?
L-aspartate
fumarate + NH3
-
r
-
?
L-aspartate
fumarate + NH3
-
r
-
?
L-aspartate
fumarate + NH3
-
r
-
?
L-aspartate
fumarate + NH3
-
r
-
?
L-aspartate
fumarate + NH3
-
r
-
?
L-aspartate
fumarate + NH3
-
r
-
?
L-aspartate
fumarate + NH3
-
r
-
?
L-aspartate
fumarate + NH3
-
r
-
?
L-aspartate
fumarate + NH3
-
r
-
?
L-aspartate
fumarate + NH3
-
r
-
?
L-aspartate
fumarate + NH3
-
r
-
?
L-aspartate
fumarate + NH3
r
-
?
L-aspartate
fumarate + NH3
-
absolutely specific
-
?
L-aspartate
fumarate + NH3
-
absolutely specific
-
?
L-aspartate
fumarate + NH3
-
absolutely specific
-
?
L-aspartate
fumarate + NH3
-
absolutely specific
-
?
L-aspartate
fumarate + NH3
-
absolutely specific
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
natural substrate
-
?
L-aspartate
fumarate + NH3
highly selective towards L-aspartate
-
-
r
L-aspartate
fumarate + NH3
-
-
-
-
?
L-aspartate
fumarate + NH3
-
-
-
r
L-aspartate
fumarate + NH3
Frog
-
r
-
?
L-aspartate
fumarate + NH3
Frog
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
r
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
-
-
r
L-aspartate
fumarate + NH3
-
-
-
r
L-aspartate
fumarate + NH3
-
-
-
-
r
L-aspartate
fumarate + NH3
-
r
-
?
L-aspartate
fumarate + NH3
-
r
-
?
L-aspartate
fumarate + NH3
-
r
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
r
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
r
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
r
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
-
-
r
L-aspartate
fumarate + NH3
-
r
-
?
L-aspartate
fumarate + NH3
-
r
-
?
L-aspartate
fumarate + NH3
-
r
-
?
L-aspartate
fumarate + NH3
-
r
-
?
L-aspartate
fumarate + NH3
-
r
-
?
L-aspartate
fumarate + NH3
-
r
-
?
L-aspartate
fumarate + NH3
-
r
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
r
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
shark
-
r
-
?
L-aspartate
fumarate + NH3
shark
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
-
-
-
?
L-aspartate
fumarate + NH3
-
-
-
-
?
L-aspartate
fumarate + NH3
-
-
fumarate is a component of the tricarboxylic acid (TCA) cycle
-
?
L-aspartate
fumarate + NH3
-
r
-
?
L-aspartate
fumarate + NH3
-
natural substrate
-
?
L-aspartate
fumarate + NH3
-
-
-
-
?
L-aspartate
fumarate + NH3
-
-
fumarate is a component of the tricarboxylic acid (TCA) cycle
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
important role in the bacterial nitrogen metabolism
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
important role in the bacterial nitrogen metabolism
-
-
?
additional information
?
-
-
AspA is one of the most specific enzymes known, no other substrates can replace L-aspartic acid in the deamination reaction
-
-
?
additional information
?
-
-
AspB efficiently processes small substituted amines, but displays very low (methoxylamine and methamine) or no (ethylamine, glycine, and formamide) activity with larger amine nucleophiles
-
-
?
additional information
?
-
aspartate enhances oxygen-limited strain growth via fumarate respiration in an aspA-dependent manner
-
-
?
additional information
?
-
-
aspartate enhances oxygen-limited strain growth via fumarate respiration in an aspA-dependent manner
-
-
?
additional information
?
-
both wild-type and AspA mutant Campylobacter jejuni strains show similar fumarate-dependent growth
-
-
?
additional information
?
-
-
both wild-type and AspA mutant Campylobacter jejuni strains show similar fumarate-dependent growth
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
no activity with D-aspartic acid or crotonic acid, overview substrate specificity
-
?
additional information
?
-
-
L-aspartate ammonia-lyase and fumarate hydratase share extensive sequence homology
-
-
?
additional information
?
-
-
L-aspartate ammonia-lyase and fumarate hydratase share extensive sequence homology
-
-
?
additional information
?
-
-
enzyme synthesis is subject to catabolite repression by glucose and is suppressed under aerobic conditions
-
-
?
additional information
?
-
-
enzyme is essential for the catabolism of the glutamate
-
-
?
additional information
?
-
-
aspartase, fumarase and argininosuccinase are structurally-related enzymes
-
-
?
additional information
?
-
-
plasminogen binding protein
-
-
?
additional information
?
-
-
plasminogen binding protein
-
-
?
additional information
?
-
-
one of the enzymes of the aspartate metabolism in lactic acid bacteria
-
-
?
additional information
?
-
-
one of the enzymes of the aspartate metabolism in lactic acid bacteria
-
-
?
additional information
?
-
-
key enzyme involved in the metabolism of aspartate
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
L-aspartate ammonia-lyase and fumarate hydratase share extensive sequence homology
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
fumarate + NH3
L-aspartate
L-aspartate
fumarate + NH3
additional information
?
-
fumarate + NH3
L-aspartate
important enzyme in production of L-aspartate
-
-
r
fumarate + NH3
L-aspartate
important enzyme in production of L-aspartate
-
-
r
L-aspartate
fumarate + NH3
-
key role in nitrogen metabolism by catalyzing the reversible elimination of NH3 from l-aspartate
-
-
r
L-aspartate
fumarate + NH3
-
-
-
?
L-aspartate
fumarate + NH3
-
-
-
-
r
L-aspartate
fumarate + NH3
-
-
-
-
?
L-aspartate
fumarate + NH3
-
-
-
-
?
L-aspartate
fumarate + NH3
-
-
fumarate is a component of the tricarboxylic acid (TCA) cycle
-
?
L-aspartate
fumarate + NH3
-
-
-
-
?
L-aspartate
fumarate + NH3
-
-
fumarate is a component of the tricarboxylic acid (TCA) cycle
-
?
additional information
?
-
-
important role in the bacterial nitrogen metabolism
-
-
?
additional information
?
-
-
important role in the bacterial nitrogen metabolism
-
-
?
additional information
?
-
-
AspA is one of the most specific enzymes known, no other substrates can replace L-aspartic acid in the deamination reaction
-
-
?
additional information
?
-
aspartate enhances oxygen-limited strain growth via fumarate respiration in an aspA-dependent manner
-
-
?
additional information
?
-
-
aspartate enhances oxygen-limited strain growth via fumarate respiration in an aspA-dependent manner
-
-
?
additional information
?
-
both wild-type and AspA mutant Campylobacter jejuni strains show similar fumarate-dependent growth
-
-
?
additional information
?
-
-
both wild-type and AspA mutant Campylobacter jejuni strains show similar fumarate-dependent growth
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
L-aspartate ammonia-lyase and fumarate hydratase share extensive sequence homology
-
-
?
additional information
?
-
-
L-aspartate ammonia-lyase and fumarate hydratase share extensive sequence homology
-
-
?
additional information
?
-
-
enzyme synthesis is subject to catabolite repression by glucose and is suppressed under aerobic conditions
-
-
?
additional information
?
-
-
enzyme is essential for the catabolism of the glutamate
-
-
?
additional information
?
-
-
aspartase, fumarase and argininosuccinase are structurally-related enzymes
-
-
?
additional information
?
-
-
plasminogen binding protein
-
-
?
additional information
?
-
-
plasminogen binding protein
-
-
?
additional information
?
-
-
one of the enzymes of the aspartate metabolism in lactic acid bacteria
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-
?
additional information
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one of the enzymes of the aspartate metabolism in lactic acid bacteria
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-
?
additional information
?
-
-
key enzyme involved in the metabolism of aspartate
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-
?
additional information
?
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-
-
-
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?
additional information
?
-
-
-
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?
additional information
?
-
-
L-aspartate ammonia-lyase and fumarate hydratase share extensive sequence homology
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-
?
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Co2+
-
activates at pH 7.0
Ca2+
-
activation at neutral pH
Ca2+
-
activates at pH 7.0
Cd2+
-
activates
Cd2+
-
activates at pH 7.0
Mg2+
-
enzyme is allosterically activated by its substrate and Mg2+ ions, which are required for activity at alkaline pH
Mg2+
aspartase activity is stimulated about 2fold by inclusion of 6 mM magnesium chloride in the assay
Mg2+
-
activation at neutral pH
Mg2+
-
activates at the alkine pH
Mg2+
-
maximal activity: 1.0 mM for native enzyme, 2.2 mM for monomeric mutant enzyme maspase 1, 1.8 mM for dimeric mutant enzyme maspase 2, 1.6 mM for tetrameric mutant enzyme maspase 3
Mg2+
-
absolutely required
Mg2+
-
activates at the alkine pH
Mg2+
-
Km-value for acetylated enzyme: 2.1 mM, for native enzyme: 1.05 mM
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
Mg2+
-
included in assay medium
Mg2+
-
included in assay medium
Mg2+
-
included in assay medium
Mn2+
-
activation at neutral pH
Mn2+
-
activates at the alkine pH
Mn2+
-
activates at pH 7.0
Mn2+
-
required at alkine pH
Zn2+
-
activates
Zn2+
-
activates at pH 7.0
Zn2+
-
most potent activating metal ion
additional information
-
no activation by Mg2+ at alkaline pH
additional information
-
-
additional information
-
-
additional information
-
absolute requirement for divalent metal ion at high pH value
additional information
-
absolute requirement for divalent metal ion at higher pH
additional information
-
-
additional information
-
-
additional information
-
no activation by Ca2+, minimal activation by Co2+, pH-dependent activation by divalent cations at high pH values
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(1-aminopropyl)-phosphonate
-
-
(3-aminopropyl)-phosphonate
-
-
(aminomethyl)-phosphonate
-
-
2,3-diphosphoglycerate
-
-
2-hydroxy-3-nitropropionate
-
-
2-mercaptoethanol
-
inactivation above 10 mM
5,5'-dithiobis(2-nitrobenzoate)
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-Aspartate
-
competitive
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-2amino-3-phosphonopropanoate
-
-
ethanol
-
moderate, nonspecific
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
HgCl2
-
1 mM, 89.5% inhibition
hydroxylamine
-
competitive
iodoacetate
-
1 mM, 94% inhibition
K+
-
2 mM, 98% inhibition
methanol
-
moderate, nonspecific
MgCl2
-
inhibitor at high concentrations (above 10 mM)
NaCN
-
1 mM, 42% inhibition
Ni2+
-
2 mM, 98% inhibition
O-phospho-L-serine
-
competitive
p-chloromercuribenzoate
-
0.1 mM, 100% inhibition
Semicarbazide hydrochloride
-
1 mM, 30% inhibition
Zn2+
-
0.0005 mM, 40% loss of activity
3-nitropropionate
-
competitive
3-nitropropionate
-
competitive
5,5'-dithiobis(2-nitrobenzoate)
-
complete
5,5'-dithiobis(2-nitrobenzoate)
-
-
aspartate beta-semialdehyde
-
i.e. aspartic beta-semialdehyde.Inactivates as an active-site directed agent
aspartate beta-semialdehyde
-
-
D-malate
-
competitive
DL-2-amino-4-phosphonobutyrate
-
-
DL-2-amino-4-phosphonobutyrate
-
competitive
EDTA
-
complete
fumarate
-
-
fumarate
-
50% inhibition at a concentration of 0.2 to 0.6 mM, pH 6.2, 50% inhibition at a concentration of 1.1 to 2.5 mM, pH 7.5
Hg2+
-
2 mM, 98% inhibition
KCl
aspartase activity is severely inhibited by potassium chloride
N-ethylmaleimide
-
1 mM, 100% inhibition
Na+
-
2 mM, 98% inhibition
o-phospho-D-serine
-
-
o-phospho-D-serine
-
competitive
p-hydroxymercuribenzoate
-
complete
p-hydroxymercuribenzoate
-
-
succinate
-
competitive
additional information
enzyme is upregulated by oxygen limitation
-
additional information
-
enzyme is upregulated by oxygen limitation
-
additional information
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-
-
additional information
-
-
-
additional information
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-
-
additional information
-
overview on inhibitors
-
additional information
-
-
-
additional information
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-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Dimethylsulfoxide
-
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
Propylene glycol
-
activates
subtilisin BPN'
-
activates
-
alpha-methyl-DL-aspartate
-
activates
alpha-methyl-DL-aspartate
-
activates wild-type enzyme, mutant C-terminal-truncated and acetylated enzyme
Trypsin
-
enzyme is activated several-fold by limited treatment
-
Trypsin
-
mechanism of activation
-
Trypsin
-
limited digestion at pH 7.4, 30°C, first 1.5 min
-
additional information
-
no allosteric effects
-
additional information
-
-
-
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aspartate ammonia-lyase deficiency
A missense mutation causes aspartase deficiency in Yersinia pestis.
aspartate ammonia-lyase deficiency
Consequences of aspartase deficiency in Yersinia pestis.
Carcinogenesis
TASP1 mutation in a female with craniofacial anomalies, anterior segment dysgenesis, congenital immunodeficiency and macrocytic anemia.
Infections
Deletion of the anaerobic regulator HlyX causes reduced colonization and persistence of Actinobacillus pleuropneumoniae in the porcine respiratory tract.
Leukemia
Bioassays to monitor Taspase1 function for the identification of pharmacogenetic inhibitors.
Leukemia
Cleaving for growth: threonine aspartase 1-a protease relevant for development and disease.
Neoplasms
Cleaving for growth: threonine aspartase 1-a protease relevant for development and disease.
Neoplasms
TASP1 mutation in a female with craniofacial anomalies, anterior segment dysgenesis, congenital immunodeficiency and macrocytic anemia.
Neoplasms
TASP1 Promotes Proliferation and Migration in Gastric Cancer via EMT and AKT/P-AKT Pathway.
Precursor Cell Lymphoblastic Leukemia-Lymphoma
[Effect of Huaier Aqueous Extract Combined with Routine Chemo-therapeutic Drugs on Human Acute Lymphoblastic Leukemia Cells Nalm-6 and Sup-B15].
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2.1 - 28.3
L-aspartic acid
1450
L-aspartic acid alpha-amide
pH 7.0, 30°C
1.71
L-phenylalanine
pH 8.0, 35°C
additional information
L-aspartate
2.5
aspartate
-
40°C, pH 7.85, native enzyme
0.58
aspartate
-
25°C, pH 7.0, in presence of Mg2+
1.73
aspartate
-
25°C, pH 7.0, in absence of Mg2+
1.97
aspartate
-
40°C, pH 7.85, acetylated enzyme
0.2
fumarate
-
25°C, pH 7.0, in presence of Mg2+
0.76
fumarate
-
25°C, pH 7.0, in absence of Mg2+
213
fumarate
co-substrate: NH3, pH 7.5, 37°, free-enzyme
213
fumarate
co-substrate: NH3, pH 7.5, 37°, LentiKats-immobilized enzyme
0.797
fumarate
-
0.1 mM, 100% inhibition
2000
fumarate
pH 8.0, 35°C
244
fumarate
co-substrate: NH3, pH 7.5, 37°, EupergitC-immobilized enzyme
244
fumarate
co-substrate: NH3, pH 7.5, 37°, MANA-agarose-immobilized enzyme
1.54
hydrazine
-
reverse reaction, 750 mM hydrazine, at pH 8, 22°C in 50 mM phosphate
308
hydrazine
-
reverse reaction, 20 mM fumarate, at pH 8, 22°C in 50 mM phosphate
5
hydroxylamine
-
substrate of the reverse reaction
151
hydroxylamine
-
reverse reaction, 20 mM fumarate, at pH 8, 22°C in 50 mM phosphate
2.78
hydroxylamine
-
reverse reaction, 400 mM hydroxylamine at pH 8, 22°C in 50 mM phosphate
0.6
L-aspartate
-
C140S/C273A mutant, pH 7.0
1.3
L-aspartate
-
C273S mutant, pH 7.0
1.3
L-aspartate
-
mutant Y146D1
1.3
L-aspartate
-
recmbinant enzyme
1.7
L-aspartate
-
T141A mutant protein
2.4
L-aspartate
-
in the presence of 3 mM MgCl2, pH 9.0
12.5
L-aspartate
-
N-ethylmaleimide-modified enzyme
20
L-aspartate
Bacterium cadaveris
-
phosphate buffer, pH 7.0
10
L-aspartate
pH 6.5, recombinant produced and purified AspA enzyme
0.54
L-aspartate
-
C273A mutant, pH 7.0
1.2
L-aspartate
-
native enzyme
1.2
L-aspartate
-
wild-type, pH 7.0
1.2
L-aspartate
-
wild type
1.2
L-aspartate
-
double mutant L363V/Y146D
1.5
L-aspartate
Bacterium cadaveris
-
Tris buffer, pH 7.0
1.5
L-aspartate
-
mutant L363V
2.5
L-aspartate
-
native enzyme
12
L-aspartate
-
K139I mutant, pH 7.0
1.09
L-aspartate
-
pH 7.0, 55°C
11
L-aspartate
mutant P322A, pH 8.5, 25°C
32
L-aspartate
-
55°C, pH 7.8
9.1
L-aspartate
-
100 mM Bis-Tris-propane hydrochloride buffer, pH 6.2
0.346
L-aspartate
pH 8.0, 35°C
2.6
L-aspartate
-
mutant N217K/T233R/V367G
2.6
L-aspartate
-
dimeric mutant enzyme maspase 2
15
L-aspartate
wild-type, pH 8.5, 25°C
15
L-aspartate
-
wild-type protein
15
L-aspartate
-
his-tagged protein, pH 8.5, 25°C, in 50 mM NaHPO4 buffer
12.8
L-aspartate
pH 7.0, recombinant produced and purified AspA enzyme
30
L-aspartate
Bacterium cadaveris
-
phosphate buffer, pH 6.8
1.23
L-aspartate
-
tetrameric mutant enzyme maspase 3
27
L-aspartate
-
H188A mutant protein
28
L-aspartate
mutant S319A, pH 8.5, 25°C
5.5
L-aspartate
-
monomeric mutant enzyme maspase 1
28.5
L-aspartate
-
30°C, pH 8.5
163
L-aspartate
-
T187S mutant protein
38.2
L-aspartate
pH 8.0, recombinant produced and purified AspA enzyme
2.1
L-aspartic acid
pH 8.5, 30°C, wild-type enzyme
28.3
L-aspartic acid
pH 8.5, 30°C, mutant enzyme K327N
1.61
NH3
-
reverse reaction, 200 mM NH3, at pH 8, 22°C in 50 mM phosphate
25.2
NH3
-
0.1 mM, 100% inhibition
85
NH3
-
reverse reaction, 20 mM fumarate, at pH 8, 22°C in 50 mM phosphate
additional information
L-aspartate
-
above 1 M, N142Q mutant protein
additional information
L-aspartate
-
above 1 M, N326A mutant protein
additional information
L-aspartate
-
above 1 M, N326Q mutant protein
additional information
L-aspartate
-
above 1 M, T101A mutant protein
additional information
L-aspartate
-
above 1 M, T101S mutant protein
additional information
L-aspartate
-
above 1 M, T187A mutant protein
additional information
L-aspartate
-
above 400 mM, S140A mutant protein
additional information
L-aspartate
-
above 400 mM, T141K mutant protein
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
enzyme processes L-aspartic acid, but not D-aspartic acid
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
8.002
L-phenylalanine
pH 8., 35°C
additional information
L-aspartate
90
fumarate
-
reverse reaction
13.64
fumarate
pH 8.0, 35°C
92
hydrazine
-
reverse reaction, 750 mM hydrazine, at pH 8, 22°C in 50 mM phosphate
94
hydrazine
-
reverse reaction, 20 mM fumarate, at pH 8, 22°C in 50 mM phosphate
31
hydroxylamine
-
reverse reaction, 400 mM hydroxylamine at pH 8, 22°C in 50 mM phosphate
99
hydroxylamine
-
reverse reaction, 20 mM fumarate, at pH 8, 22°C in 50 mM phosphate
0.3
L-aspartate
-
T141A mutant protein
0.1
L-aspartate
-
recombinant enzyme
0.7
L-aspartate
-
H188A mutant protein
21
L-aspartate
mutant P322A, pH 8.5, 25°C
17
L-aspartate
mutant S319A, pH 8.5, 25°C
190
L-aspartate
-
T187S mutant protein
40
L-aspartate
wild-type, pH 8.5, 25°C
40
L-aspartate
-
wild-type protein
40
L-aspartate
-
his-tagged protein, pH 8.5, 25°C, in 50 mM NaHPO4 buffer
0.12
L-aspartate
-
mutant L363V
0.13
L-aspartate
-
mutant Y146D
170
L-aspartate
-
tetrameric mutant enzyme maspase 3
180
L-aspartate
-
native enzyme
86
L-aspartate
-
double mutant L363V/Y146D
163
L-aspartate
-
monomeric mutant enzyme maspase 1
165
L-aspartate
-
dimeric mutant enzyme maspase 2
4.908
L-aspartate
pH 8.0, 35°C
89
NH3
-
reverse reaction, 20 mM fumarate, at pH 8, 22°C in 50 mM phosphate
59
NH3
-
reverse reaction, 200 mM NH3, at pH 8, 22°C in 50 mM phosphate
additional information
L-aspartate
-
above 0.016 1/sec, N326Q mutant protein
additional information
L-aspartate
-
above 0.027 1/sec, T141K mutant protein
additional information
L-aspartate
-
above 0.12 1/sec, N326A mutant protein
additional information
L-aspartate
-
above 0.38 1/sec, T101A mutant protein
additional information
L-aspartate
-
above 0.43 1/sec, T187A mutant protein
additional information
L-aspartate
-
above 0.88 1/sec, N142Q mutant protein
additional information
L-aspartate
-
above 34 1/sec, T101S mutant protein
additional information
L-aspartate
-
above 40 1/sec, S140A mutant protein
additional information
L-aspartate
-
below 0.001 1/sec, H188A, H188R and H188K mutant protein
additional information
L-aspartate
-
below 0.001 1/sec, K324A mutant protein
additional information
L-aspartate
-
below 0.001 1/sec, K324D mutant protein
additional information
L-aspartate
-
below 0.001 1/sec, K324H mutant protein
additional information
L-aspartate
-
below 0.001 1/sec, K324R mutant protein
additional information
L-aspartate
-
below 0.001 1/sec, K324S mutant protein
additional information
L-aspartate
-
below 0.001 1/sec, K324V mutant protein
additional information
L-aspartate
-
below 0.001 1/sec, N142A mutant protein
additional information
L-aspartate
-
below 0.001 1/sec, S140G/T141G mutant protein
additional information
L-aspartate
-
below 0.001 1/sec, S140K mutant protein
additional information
L-aspartate
-
below 0.001 1/sec, S140K/T141K mutant protein
additional information
L-aspartate
-
below 0.001 1/sec, S140R mutant protein
additional information
L-aspartate
-
below 0.001 1/sec, T141R mutant protein
additional information
L-aspartate
-
below 0.001 1/sec, T141V mutant protein
additional information
additional information
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.038
fumarate
pH 8.0, 35°C
0.000016 - 14.18
L-aspartate
4.65
L-phenylalanine
pH 8.0, 35°C
0.61
L-aspartate
mutant S319A, pH 8.5, 25°C
1.2
L-aspartate
-
T187S mutant protein
0.00012
L-aspartate
-
N326A mutant protein
0.18
L-aspartate
-
T141A mutant protein
0.034
L-aspartate
-
T101S mutant protein
0.026
L-aspartate
-
H188A mutant protein
0.055
L-aspartate
mutant I320A, pH 8.5, 25°C
0.008
L-aspartate
mutant M321A, pH 8.5, 25°C
0.1
L-aspartate
-
S140A mutant protein
1.9
L-aspartate
mutant P322A, pH 8.5, 25°C
2.7
L-aspartate
-
wild-type protein
2.7
L-aspartate
wild-type, pH 8.5, 25°C
0.00038
L-aspartate
-
T101A mutant protein
0.00088
L-aspartate
-
N142Q mutant protein
0.000068
L-aspartate
-
T141K mutant protein
0.00043
L-aspartate
-
T187A mutant protein
0.000016
L-aspartate
-
N326Q mutant protein
14.18
L-aspartate
pH 8.0, 35°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1.1
2,3-diphosphoglycerate
-
-
0.83
3-nitropropanoate
-
-
0.01 - 2
3-nitropropionate
0.66
DL-2amino-3-phosphonopropanoate
-
-
0.2
o-phospho-D-serine
-
-
0.01
3-nitropropionate
-
H188A mutant protein
0.5
3-nitropropionate
-
T141A mutant protein
2
3-nitropropionate
-
wild-type protein
2.2
ammonium
-
25°C, pH 7.0, in presence of Mg2+
1.19
ammonium
-
25°C, pH 7.0, in absence of Mg2+
0.4
D-malate
-
H188A mutant protein
48
D-malate
-
T141A mutant protein
68
D-malate
-
wild-type protein
0.2 - 0.6
fumarate
-
-
1.1 - 0.6
fumarate
-
pH 7.5
0.165
fumarate
-
25°C, pH 7.0, in presence of Mg2+
2.83
fumarate
-
25°C, pH 7.0, in absence of Mg2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.044
-
pYV- (lacking low-calcium response plasmid into pseudogenes), 4 mM Ca2+, 250 mmol Tris/HCl buffer, 5.0 mmol MgCl2
0.06
-
pYV+ (containing low-calcium response plasmid into pseudogenes), 4 mM Ca2+, 250 mmol Tris/HCl buffer, 5.0 mmol MgCl2
0.075
-
pYV+ (containing low-calcium response plasmid into pseudogenes), 250 mmol Tris/HCl buffer, 5.0 mmol MgCl2
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
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
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
0.05
-
pestoides G
0.05
-
pYV- (lacking low-calcium response plasmid into pseudogenes), 250 mmol Tris/HCl buffer, 5.0 mmol MgCl2
0.2
-
mutant L363V, 50 mM HEPES, 50 mM HEPES, 10 mM Mg acetate, 20 mM L-aspartate
0.2
-
mutant Y146D, 50 mM HEPES, 10 mM Mg acetate, 20 mM L-aspartate
0.2
-
recombinant enzyme, 50 mM HEPES, 10 mM Mg acetate, 20 mM L-aspartate
0.202
-
strain WA
700
-
30°C
700
-
activity in Escherichia coli BLR (DE3) cells after cloning the enzyme in the pLATE31 plasmid, composition and highly efficient expression under the control of the T7 phage promoter, pH and temperature not specified in the publication
additional information
-
-
additional information
AspB is immobilized by covalent attachment on Eupergit (epoxy support) and MANAagarose (amino support), and entrapment in LentiKats (polyvinyl alcohol) with retained activities of 24, 85 and 63%, respectively
additional information
-
AspB is immobilized by covalent attachment on Eupergit (epoxy support) and MANAagarose (amino support), and entrapment in LentiKats (polyvinyl alcohol) with retained activities of 24, 85 and 63%, respectively
additional information
-
His6-tag at enzyme does not affect AspB activity
additional information
-
no activity with D-aspartic acid, L-cysteine, L-histidine, L-phenylalanine, L-glutamine, L-tyrosine, L-serine, L-alanine, L-valine, L-leucine, L-threonine, L-lysine, alpha-methyl-DL-aspartic acid, beta-methyl-DL-aspartic acid, L-glutamate, beta-alanine, beta-DL-aminobutyric acid, beta-asparagine, beta-phenylalanine and beta-leucine as substrates (25 mm substrate in 100 mm Na2HPO4 buffer, pH 9.0 at 37°C)
additional information
AspA has a role in the persistence of Campylobacter jejuni in the avian intestine
additional information
-
AspA has a role in the persistence of Campylobacter jejuni in the avian intestine
additional information
aspA mutant strain is totally deficient in aspartase enzyme activity, whereas in the wild-type enzyme, an extremely high specific activity is present in stationary-phase cell-free extracts (more than 2 mmol fumarate are produced per min per mg protein)
additional information
-
aspA mutant strain is totally deficient in aspartase enzyme activity, whereas in the wild-type enzyme, an extremely high specific activity is present in stationary-phase cell-free extracts (more than 2 mmol fumarate are produced per min per mg protein)
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
kinetic analyses
additional information
-
kinetic analyses
additional information
-
-
additional information
-
-
additional information
-
0.202 - 0.207 micromol/min/mg in cell-free extracts, value depends on the strain
additional information
-
activity below 0.001, pCD- (lacking low-calcium response plasmid into pseudogenes)
additional information
-
activity below 0.001, pCD- (lacking low-calcium response plasmid into pseudogenes), 4 mM Ca2+
additional information
-
activity below 0.001, pCD+ (containing low-calcium response plasmid into pseudogenes), 250 mmol Tris/HCl buffer, 5.0 mmol MgCl2
additional information
-
activity below 0.001, pCD+ (containing low-calcium response plasmid into pseudogenes), 4 mM Ca2+
additional information
-
full AspA activity occurs in pestoides isolates where valine (pestoides A, B, C and D) or serine (pestoides E, F, G and I) occupy position 363. Reduced activity occurs in strains Angola and A16, which contains phenylalanine at position 363. The kcat but not Km of purified AspA from strain Angola is significantly reduced.
additional information
-
full AspA activity occurs in pestoides isolates where valine (pestoides A, B, C and D) or serine (pestoides E, F, G and I) occupy position 363. Reduced activity occurs in strains Angola and A16, which contains phenylalanine at this position. The kcat but not Km of purified AspA from strain Angola is significantly reduced.
additional information
-
below 0.001 micromol/min/mg in cell-free extracts of epidemic strains (Leu in position 363) /0,02-0.008 micromol/min/mg in cell-free extracts of strain A16 and Angola (Phe in position 363), value depends on the strain /0,028-0.064 micromol/min/mg in cell-free extracts of strain Pestoides A-D (Val in position 363), value depends on the strain /0,039-0.052 micromol/min/mg in cell-free extracts of strain Pestoides D-G and Pestoides I (Ser in position 363), value depends on the strain
additional information
-
0.059 - 0.172 micromol/min/mg in cell-free extracts, value depends on the strain
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
8.3
-
native enzyme in the absence of MgCl2
7
-
trypsin-activated enzyme in the absence of MgCl2
7
-
in the absence of MgCl2
7
-
optimum for reactivation
7
-
AspA assay in cell preparations
7
-
AspA assay in cell preparations
7.5
assay at
7.5
-
native enzyme in the absence of MgCl2
8
-
8
-
enzyme renatured by L-aspartate induction
8
-
wild-type enzyme, mutant enzyme (random mutagenesis)
8
-
AspA assay in purified preparations
8
-
AspA assay in purified preparations
8.2
-
N-ethylmaleimide-modified enzyme, in the presence of MgCl2
8.2
-
mutant N217K/T233R/V367G
8.5
-
assay at 30C
8.5
-
mutant (site-directed) enzyme
8.5
deamination of L-aspartate, wild-type enzyme and mutant enzyme K327N
8.5
-
in the presence of 20 mM MgCl2
8.8
-
native enzyme in the presence of MgCl2
8.8
-
trypsin-activated enzyme and native enzyme in the presence of MgCl2
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
pH dependence of kinetic parameters
additional information
-
-
additional information
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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
-
-
additional information
-
-
additional information
-
-
additional information
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
25
-
optimum temperature for reactivation
additional information
-
temperature dependence of kinetic parameters
30
-
assay at
37
assay at
45
-
maximum activity
55
-
assay at
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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 - 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
50
-
60 min, 80% residual activity
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
-
brenda
-
-
-
brenda
Cj0087; zoonotic pathogen, a number of avian species are reservoirs for this organism
UniProt
brenda
KUC-1
-
-
brenda
KUC-1
-
-
brenda
plasmid carrying the L-aspartase gene
-
-
brenda
-
SwissProt
brenda
-
-
-
brenda
Frog
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
CNRZ 313
-
-
brenda
CNRZ 313
-
-
brenda
NCDO 566, ATCC 9614, MNS, DRI, KFA
-
-
brenda
-
SwissProt
brenda
-
-
-
brenda
shark
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
SwissProt
brenda
EMBL; YM55-1
SwissProt
brenda
YM55-1
-
-
brenda
-
-
-
brenda
-
SwissProt
brenda
EMBL; YM55-1
SwissProt
brenda
YM55-1
-
-
brenda
-
-
-
brenda
thermophilic
-
-
brenda
Bacterium cadaveris
-
-
-
brenda
Bacterium cadaveris
ATCC 9760
-
-
brenda
-
5997 , 5998 , 6000 , 6001 , 6002 , 6003 , 6004 , 6005 , 6006 , 6008 , 6009 , 6011 , 6014 , 6016 , 6018 , 6019 , 6021 , 6022 , 6026 -
-
brenda
-
SwissProt
brenda
-
-
-
brenda
-
SwissProt
brenda
-
-
-
brenda
-
SwissProt
brenda
AS 1.881 (wild-type)
-
-
brenda
C273S, C273A, C140S/C273A, K139I (mutants)
-
-
brenda
C9, C14 (mutants of strain W)
-
-
brenda
J2 (mutant of AS 1.881)
-
-
brenda
K12
-
-
brenda
K12 strain JRG 1849
-
-
brenda
plasmid carrying the L-aspartase gene
-
-
brenda
-
-
-
brenda
ATCC 9760
-
-
brenda
ssp. freudenreichii
-
-
brenda
ssp. shermanii
-
-
brenda
-
-
-
brenda
IFO 3081
-
-
brenda
-
-
-
brenda
strains Winblad, WA, E705
-
-
brenda
-
-
-
brenda
enzootic (pestoides) isolates A-D
-
-
brenda
enzootic (pestoides) isolates E, F, G and I
-
-
brenda
epidemic strains Camel, CO92, KIM10, Kuma, Pestoides J, UG05-0454 /enzootic strains A16, Angola, Pestoides A, Pestoides B, Pestoides C, Pestoides D, Pestoides E, Pestoides F, Pestoides G, Pestoides I
-
-
brenda
strains Angola and A16
-
-
brenda
-
-
-
brenda
strains 1, PB1, 7, TX83-0489
-
-
brenda
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strain NCTC 11168
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
strain KIM, possesses a base transversion (GC-TA) at position 146 of AspA, causing replacement of aspartate by tyrosine
brenda
-
-
brenda
-
strain PB1 of serogroup 1b
brenda
-
-
brenda
Frog
-
-
brenda
-
-
brenda
shark
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
metabolism
important enzyme in production of L-aspartate
metabolism
-
important enzyme in production of L-aspartate
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
109600
-
dimeric mutant enzyme maspase 2, gel filtration
173000
-
sedimentation equilibrium analysis
180000
Bacterium cadaveris
-
sucrose density gradient centrifugation
198000
-
pore gradient polyacrylamide
213800
-
tetrameric mutant enzyme maspase 3, gel filtration
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
56200
-
monomeric mutant enzyme maspase 1, gel filtration
193000
-
sedimentation equilibrium analysis
193000
structure of the enzyme
200000
-
gel filtration
48500
-
4 * 48500, SDS-PAGE
48500
-
4 * 48500, SDS-PAGE
50000
SDS-PAGE
50000
-
4 * 50000, SDS-PAGE
51000
recombinant His-tagged enzyme, SDS-PAGE
51000
-
4 * 51000, SDS-PAGE
51000
-
4 * 51000, SDS-PAGE
52000
-
SDS-PAGE
52000
-
4 * 52000, SDS-PAGE
52000
-
4 * 52000, overview
55000
-
-
55000
-
4 * 55000, SDS-PAGE
55000
-
4 * 55000, SDS-PAGE
56000
-
1 * 56000, mutant enzyme maspase 1, SDS-PAGE
56000
-
2 * 56000, mutant enzyme maspase 2, SDS-PAGE
56000
-
4 * 56000, mutant enzyme maspase 3, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
?
-
x * 52000, SDS-PAGE
?
-
x * 52000, SDS-PAGE
-
?
-
x * 52000, SDS-PAGE
-
?
x * 51000, recombinant His-tagged enzyme, SDS-PAGE
dimer
-
2 * 56000, mutant enzyme maspase 2, SDS-PAGE
dimer
-
2 * 56000, mutant enzyme maspase 2, SDS-PAGE
-
homotetramer
4 * 50000, SDS-PAGE
homotetramer
-
crystallographic data
homotetramer
-
crystallographic data
-
homotetramer
-
4 * 50000, SDS-PAGE
-
homotetramer
-
4 subunits of 478 amino acids
homotetramer
-
4 * 51000, SDS-PAGE
homotetramer
-
4 * 51000, SDS-PAGE
-
homotetramer
-
4 * 52000, overview
homotetramer
-
predicted and determined by dynamic light scattering (DLS), loss of activity in mutants reflects significant changes in subunit association.
monomer
-
1 * 56000, mutant enzyme maspase 1, SDS-PAGE
monomer
-
1 * 56000, mutant enzyme maspase 1, SDS-PAGE
-
tetramer
-
4 * 51000, SDS-PAGE
tetramer
4 * 51630, deduced from gene sequence
tetramer
-
4 * 51000, SDS-PAGE
-
tetramer
-
4 * 51630, deduced from gene sequence
-
tetramer
-
4 * 52224, calculation from sequence of amino acid
tetramer
-
4 * 48500, SDS-PAGE
tetramer
-
4 * 52190, calculation from sequence of amino acid
tetramer
-
subunit arrangement: D2 symmetry
tetramer
-
4 * 52000, SDS-PAGE
tetramer
-
4 * 56000, mutant enzyme maspase 3, SDS-PAGE
tetramer
-
4 * 56000, mutant enzyme maspase 3, SDS-PAGE
-
tetramer
-
4 * 55000, SDS-PAGE
tetramer
-
4 * 51218, calculation from sequence of amino acid
tetramer
-
4 * 55000, SDS-PAGE
-
tetramer
-
4 * 51218, calculation from sequence of amino acid
-
tetramer
-
4 * 55000, SDS-PAGE
tetramer
-
4 * 50000, SDS-PAGE
tetramer
-
4 * 48500, SDS-PAGE
tetramer
-
4 * 50859, calculation from sequence of amino acid
additional information
-
overview
additional information
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
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S319A
SS-loop mutant, about 30% of wild-type activity
K183A
complete loss of activity
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
S318A
SS-loop mutant, complete loss of activity
I320A
SS-loop mutant, about 2% of wild-type activity
M321A
SS-loop mutant, less than 1% of wild-type activity
P322A
SS-loop mutant, about 70% of wild-type activity
S319A
-
SS-loop mutant, about 30% of wild-type activity
-
K183A
-
complete loss of activity
-
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
-
S318A
-
SS-loop mutant, complete loss of activity
-
I320A
-
SS-loop mutant, about 2% of wild-type activity
-
M321A
-
SS-loop mutant, less than 1% of wild-type activity
-
P322A
-
SS-loop mutant, about 70% of wild-type activity
-
N142Q
-
responsible for binding the amino group of the substrate
H188A
-
responsible for binding the amino group of the substrate
N326A
-
responsible for binding the C1 carboxylate group of substrate
T141A
-
implicated in binding the C4 carboxylate group of substrate
T101S
-
responsible for binding the amino group of the substrate
T101A
-
responsible for binding the amino group of the substrate
S140A
-
implicated in binding the C4 carboxylate group of substrate
K324A
-
responsible for binding the C1 carboxylate group of substrate
N142A
-
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
H188K
-
responsible for binding the amino group of the substrate
S140R
-
implicated in binding the C4 carboxylate group of substrate
S140K
-
implicated in binding the C4 carboxylate group of substrate
T141V
-
implicated in binding the C4 carboxylate group of substrate
T141R
-
implicated in binding the C4 carboxylate group of substrate
T141K
-
implicated in binding the C4 carboxylate group of substrate
S140G/T141G
-
implicated in binding the C4 carboxylate group of substrate
S140K/T141K
-
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
K324S
-
responsible for binding the C1 carboxylate group of substrate
K324V
-
responsible for binding the C1 carboxylate group of substrate
K324H
-
responsible for binding the C1 carboxylate group of substrate
K324D
-
responsible for binding the C1 carboxylate group of substrate
K324R
-
responsible for binding the C1 carboxylate group of substrate
N326Q
-
responsible for binding the C1 carboxylate group of substrate
K126R
-
replacement of Lys126 with Arg increases the activity of the enzyme
K55R
-
completeley inactive and insoluble protein, reactivation by an artificial chaperone system including beta-cyclodextrin and cetyltrimethylammonium bromide
K140I
-
Km value 10fold higher than wild type, comparable increase in Ki for competitive inhibitors
C141S/C274A
-
elimination of sensitivity to inactivation
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
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
-
overview
additional information
-
design of enzyme variants by ligation of subdomains with a random hexapeptide loop, variant with highest activity is a monomer with high thermotolerance
additional information
-
mutant N217K/T233R/V367G through enzyme modification by direct evolution in order to enhance enzymic activity
additional information
-
construction of hybrid enzyme from alpha-aspartyl dipeptidase and L-aspartase. The hybrid enzyme can be used in synthesis of the precursor for aspartame
additional information
-
insertion of a 15-peptide random peptide into the three domains of L-aspartase to enhance their mobility. After directed screening, the three isoforms of monomeric, dimeric and tetrameric enzyme (named maspase 1, maspase 2 and maspase 3) with the activity of L-aspartase are obtained
additional information
-
insertion of a 15-peptide random peptide into the three domains of L-aspartase to enhance their mobility. After directed screening, the three isoforms of monomeric, dimeric and tetrameric enzyme (named maspase 1, maspase 2 and maspase 3) with the activity of L-aspartase are obtained
-
additional information
-
overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5 - 9
-
mutant enzyme by random mutagenesis
6023
7 - 8
-
wild-type enzyme
6023
7 - 9
-
mutant enzyme by site-directed mutagenesis
6023
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
15 - 60
-
15C: 90% loss of maximal activity, 60C: 90% loss of activity
35
the enzyme retains 56% activity after 7 days of incubation
60
-
complete loss of activity after 5 min
50
-
83% loss of activity (wild-type), 70% loss of activity (mutant enzyme) after 45 min
50
-
30 min, 17% residual activity, wild type enzyme
50
-
30 min, 80% residual activity, monomeric enzyme variant
50
-
30 min, native enzyme loses 83% of initial activity, monomeric mutant enzyme maspase 1 loses 23% of initial activity, dimeric mutant enzyme maspase 2 loses 48% of initial activity, tetrameric mutant enzyme maspase 3 loses 59% of initial activity
50
-
37% loss of activity after 5 min
55
-
20% loss of activity after 60 min
55
-
60 min, 80% residual activity
55
-
inactivated by heat-treatment
55
-
complete loss of activity after 60 min
55
-
85% loss of activity after 5 min
additional information
-
moderate thermophile
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
irreversible inactivation during prolonged centrifugation
Bacterium cadaveris
-
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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
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-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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
-
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although Corynebacterium glutamicum posses the aspartate ammonia-lyase gene (aspA), aspartate aminotransferase (AAT) is necessary to cell growth and L-lysine production, because the activity of Corynebacterium glutamicum aspartate ammonia-lyase (AAL) is too low to maintain the cell growth. Escherichia coli aspartate ammonia-lyase helps to restore the cell growth of aspB-deleted strain and also leads to the accumulation of L-lysine, L-glutamate, pyruvate and 2-oxoglutarate
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
-
cloning in the pLATE31 plasmid composition and highly efficient expression under the control of the T7 phage promoter in Escherichia coli BLR (DE3) cell. The use of the expression system allows an increase in aspartase activity in cells by 100times as compared to the initial strain. The maximal specific activity of cells reached 0.700 mM/mg/min
-
expression in Escherichia coli
-
expression in Escherichia coli BL21
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
-
-
-
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increased expression at acidic pH
-
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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.
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denaturation by addition of high concentrations of guanidine-HCl leads to reversible dissociation and reassembly of the tetrameric structure
hydroxylamine reactivates diethyldicarbonate treated enzyme
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reactivation of trypsin activated and native enzyme by dilution after inactivation by 4 M guanidine-HCl
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regains its activity and quaternary structure upon dilution
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renaturation by dialysis against 50 mM Tris-HCl buffer ,pH 8.0, at 4C for 2 days
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renaturation by different inducers
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reversible denaturation is influenced by various environmental factors
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denaturation by addition of high concentrations of guanidine-HCl leads to reversible dissociation and reassembly of the tetrameric structure
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denaturation by addition of high concentrations of guanidine-HCl leads to reversible dissociation and reassembly of the tetrameric structure
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analysis
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scaled-down method for determination of aspartase activity in a 96-well microtitre plate
food industry
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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
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aspartate synthesis
medicine
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involvement of enzyme in blood clotting and activation of plasminogen, overview
biotechnology
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overview on commercial applications
biotechnology
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enhancement of recombinant protein production in Escherichia coli by coproduction of aspartase. The excretion of acetate by the aerobic growth of Escherichia coli on glucose is a manifestation of imbalanced flux between glycolysis and the tricarboxylic acid (TCA) cycle. This may restrict the production of recombinant proteins in E. coli, due to the limited amounts of precursor metabolites produced in TCA cycle. To approach this issue, an extra supply of intermediate metabolites in TCA cycle is made by conversion of aspartate to fumarate, a reaction mediated by the activity of L-aspartate ammonia-lyase
biotechnology
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putative and attractive enzyme for the enantioselective synthesis of N-substituted aspartic acids
biotechnology
a complete biocatalytic process to synthesize high concentrations of L-aspartate catalyzed by aspartase from Bacillus sp. YM55-1 (AspB) is established using an immobilized enzyme in three different supports. MANA-agarose derivative could be selected as the most suitable biocatalyst for the synthesis of Asp due to the simplicity of the method and performance
biotechnology
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a complete biocatalytic process to synthesize high concentrations of L-aspartate catalyzed by aspartase from Bacillus sp. YM55-1 (AspB) is established using an immobilized enzyme in three different supports. MANA-agarose derivative could be selected as the most suitable biocatalyst for the synthesis of Asp due to the simplicity of the method and performance
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synthesis
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industrial production of L-aspartic acid using polyurethane-immobilized cells containing aspartase
synthesis
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enzyme or whole cells are used for the industrial production of L-aspartate, which together with L-phenylalanine is the basis of the sweetener aspartame
synthesis
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production of L-aspartic acid, which is used as a precursor for the synthesis of the low calorie synthetic sweetener aspartame
synthesis
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production of L-aspartic acid, which is used as an intermediate for aspartame, an artificial sweetener. It is also used as acidulant in pharmaceuticals and foods
synthesis
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construction of hybrid enzyme from alpha-aspartyl dipeptidase and L-aspartase. The hybrid enzyme can be used in synthesis of the precursor for aspartame. Synthesizing aspartate from fumarate and NH4+, and then taking advantage of the catalytic action of alpha-aspartyl dipeptidase, the precursor of aspartame is produced
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
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