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Literature summary extracted from

  • Armenia, I.; Balzaretti, R.; Pirrone, C.; Allegretti, C.; DArrigo, P.; Valentino, M.; Gornati, R.; Bernardini, G.; Pollegioni, L.
    L-aspartate oxidase magnetic nanoparticles synthesis, characterization and L-aspartate bioconversion (2017), RSC Adv., 7, 21136-21143 .
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.4.3.16 expressed in Escherichia coli Sulfurisphaera tokodaii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.4.3.16 L-aspartate + O2 Sulfurisphaera tokodaii
-
 iminosuccinate + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.4.3.16 Sulfurisphaera tokodaii Q972D2
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.4.3.16
-
 Sulfurisphaera tokodaii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.3.16 L-aspartate + O2
-
 Sulfurisphaera tokodaii iminosuccinate + H2O2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.4.3.16 LASPO
-
 Sulfurisphaera tokodaii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.4.3.16 70
-
-
 Sulfurisphaera tokodaii

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.4.3.16 8 11 when compared to the free enzyme form, the immobilized enzyme shows a full stability at pH values 9.0-11.0 after 60 min of incubation, while for the free enzyme the stability strongly decreases at pH above 8.0 Sulfurisphaera tokodaii

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.3.16 FAD
-
 Sulfurisphaera tokodaii