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Literature summary extracted from

  • Seo, Y.M.; Mathew, S.; Bea, H.S.; Khang, Y.H.; Lee, S.H.; Kim, B.G.; Yun, H.
    Deracemization of unnatural amino acid: homoalanine using D-amino acid oxidase and omega-transaminase (2012), Org. Biomol. Chem., 10, 2482-2485.
    View publication on PubMed

Application

EC Number Application Comment Organism
2.6.1.18 biotechnology an alternative deracemization method for the efficient production of L-homoalanine using D-amino acid oxidase (vide infra) and omega-TA is proposed Vibrio fluvialis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.6.1.18 expressed in Escherichia coli Vibrio fluvialis

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.6.1.18 benzaldehyde
-
Vibrio fluvialis

Organism

EC Number Organism UniProt Comment Textmining
2.6.1.18 Vibrio fluvialis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.6.1.18 using an Ni-NTA affinity column Vibrio fluvialis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.6.1.18 2-oxobutyrate + benzylamine enzyme inhibition by benzaldehyde is the major hurdle in carrying out the omega-TA reaction efficiently. To overcome the product inhibition, a biphasic reaction system in which an organic solvent is employed to extract the inhibitory benzaldehyde from an aqueous system is used Vibrio fluvialis L-homoalanine + benzaldehyde
-
?

Synonyms

EC Number Synonyms Comment Organism
2.6.1.18 omega-TA
-
Vibrio fluvialis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.6.1.18 37
-
assay at Vibrio fluvialis

Cofactor

EC Number Cofactor Comment Organism Structure
2.6.1.18 pyridoxal 5'-phosphate
-
Vibrio fluvialis