4.3.1.1: aspartate ammonia-lyase
This is an abbreviated version!
For detailed information about aspartate ammonia-lyase, go to the full flat file.
Reaction
Synonyms
ammonia-lyase, aspartate, ASPA, aspartase, aspartate ammonia lyase, aspartate ammonia-lyase, aspartate:ammonia lyase, aspB, Cj0087, fumaric aminase, L-aspartase, L-aspartate ammonia lyase, L-aspartate ammonia-lyase, maspase 1, maspase 2, maspase 3
ECTree
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Application on EC 4.3.1.1 - aspartate ammonia-lyase
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APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
analysis
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scaled-down method for determination of aspartase activity in a 96-well microtitre plate
biotechnology
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
medicine
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involvement of enzyme in blood clotting and activation of plasminogen, overview
synthesis
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
Bacillus sp. (in: Bacteria) YM55-1
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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
