The enzyme has been shown to react preferentially with short-chain ketones such as cyclohexanone, primary amine groups attached to secondary alkyl groups, or D- and L-amino acids. It also reduces aldehydes to primary amines. Cosubstrate preference depends on the substrate.
Determining a novel NAD+-dependent amine dehydrogenase with a broad substrate range from Streptomyces virginiae IFO 12827: purification and characterization.
Journal
Journal of Molecular Catalysis B: Enzymatic 10:281-290 (2000)
Reference
2
Authors
Mayol, O., David, S., Darii, E., Debard, A., Mariage, A., Pellouin, V., Petit, J.L., Salanoubat, M., de Berardinis, V., Zaparucha, A. and Vergne-Vaxelaire, C.
Title
Asymmetric reductive amination by a wild-type amine dehydrogenase from the thermophilic bacteria Petrotoga mobilis.
Journal
Catalysis Science & Technology 6:7421-7428 (2016)
Reference
3
Authors
Mayol, O., Bastard, K., Beloti, L., Frese, A., Turkenburg, J.P., Petit, J.L., Mariage, A., Debard, A., Pellouin, V., Perret, A., de Berardinis, V., Zaparucha, A., Grogan, G. and Vergne-Vaxelaire, C.
Title
A family of native amine dehydrogenases for the asymmetric reductive amination of ketones.
Journal
Nature Catalysis 2:324-333 (2019)
Reference
4
Authors
Lee, S., Jeon, H., Giri, P., Lee, U.J., Jung, H., Lim, S., Sarak, S., Khobragade, T.P., Kim, B.G. and Yun, H.
Title
The reductive amination of carbonyl compounds using native amine dehydrogenase from Laribacter hongkongensis.
