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Literature summary extracted from

  • Cardenas-Fernandez, M.; Lopez, C.; Alvaro, G.; Lopez-Santin, J.
    Immobilized L-aspartate ammonia-lyase from Bacillus sp. YM55-1 as biocatalyst for highly concentrated L-aspartate synthesis (2012), Bioprocess Biosyst. Eng., 35, 1437-1444.
    View publication on PubMed

Application

EC Number Application Comment Organism
4.3.1.1 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 Bacillus sp. (in: Bacteria)

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.3.1.1 AspB is expressed in Escherichia coli Bacillus sp. (in: Bacteria)

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.3.1.1 213
-
 fumarate co-substrate: NH3, pH 7.5, 37°, free-enzyme Bacillus sp. (in: Bacteria)
4.3.1.1 213
-
 fumarate co-substrate: NH3, pH 7.5, 37°, LentiKats-immobilized enzyme Bacillus sp. (in: Bacteria)
4.3.1.1 244
-
 fumarate co-substrate: NH3, pH 7.5, 37°, EupergitC-immobilized enzyme Bacillus sp. (in: Bacteria)
4.3.1.1 244
-
 fumarate co-substrate: NH3, pH 7.5, 37°, MANA-agarose-immobilized enzyme Bacillus sp. (in: Bacteria)

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.3.1.1 50000
-
 SDS-PAGE Bacillus sp. (in: Bacteria)

Organism

EC Number Organism UniProt Comment Textmining
4.3.1.1 Bacillus sp. (in: Bacteria) Q9LCC6
-
-
4.3.1.1 Bacillus sp. (in: Bacteria) YM55-1 Q9LCC6
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.3.1.1 partially purified by heat precipitation and saturation with ammonium sulfate Bacillus sp. (in: Bacteria)

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.3.1.1 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 Bacillus sp. (in: Bacteria)

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.3.1.1 fumarate + NH3
-
 Bacillus sp. (in: Bacteria) L-aspartate
-
 ?
4.3.1.1 fumarate + NH3
-
 Bacillus sp. (in: Bacteria) YM55-1 L-aspartate
-
 ?

Subunits

EC Number Subunits Comment Organism
4.3.1.1 homotetramer 4 * 50000, SDS-PAGE Bacillus sp. (in: Bacteria)

Synonyms

EC Number Synonyms Comment Organism
4.3.1.1 aspB
-
 Bacillus sp. (in: Bacteria)
4.3.1.1 L-aspartate ammonia-lyase
-
 Bacillus sp. (in: Bacteria)

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.3.1.1 37
-
 assay at Bacillus sp. (in: Bacteria)

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.3.1.1 7.5
-
 assay at Bacillus sp. (in: Bacteria)

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
4.3.1.1 6 9
-
 Bacillus sp. (in: Bacteria)