Aliphatic (R)-hydroxynitrile lyase
Aliphatic (R)-hydroxynitrile lyase (EC 4.1.2.46, (R)-HNL, (R)-oxynitrilase, (R)-hydroxynitrile lyase, LuHNL) is an enzyme with systematic name (2R)-2-hydroxy-2-methylbutanenitrile butan-2-one-lyase (cyanide forming).[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction
- (2R)-2-hydroxy-2-methylbutanenitrile
cyanide + butan-2-one
The enzyme contains Zn2+.
References
- ↑ Trummler, K., Roos, J., Schwaneberg, U., Effenberger, F., Förster, S., Pfizenmaier, K. and Wajant, H. (1998). "Expression of the Zn2+-containing hydroxynitrile lyase from flax (Linum usitatissimum) in Pichia pastoris— utilization of the recombinant enzyme for enzymatic analysis and site-directed mutagenesis". Plant Sci. 139: 19–27. doi:10.1016/s0168-9452(98)00173-3.
- ↑ Trummler, K. and Wajant, H. (1997). "Molecular cloning of acetone cyanohydrin lyase from flax (Linum usitatissimum). Definition of a novel class of hydroxynitrile lyases". J. Biol. Chem. 272 (8): 4770–4774. doi:10.1074/jbc.272.8.4770. PMID 9030531.
- ↑ Albrecht, J., Jansen, I.and Kula, M.R. (1993). "Improved purification of an (R)-oxynitrilase from Linum usitatissimum (flax) and investigation of the substrate range". Biotechnol. Appl. Biochem. 17: 191–203.
- ↑ Xu, L.-L., Singh, B.K. and Conn, E.E. (1988). "Purification and characterization of acetone cyanohydrin lyase from Linum usitatissimum". Arch. Biochem. Biophys. 263: 256–263. doi:10.1016/0003-9861(88)90634-0. PMID 3377504.
- ↑ Cabirol, F.L., Tan, P.L., Tay, B., Cheng, S., Hanefeld, U. and Sheldon, R.A. (2008). "Linum usitatissimum hydroxynitrile lyase cross-linked enzyme aggregates: a recyclable enantioselective catalyst". Adv. Synth. Catal. 350: 2329–2338. doi:10.1002/adsc.200800309.
- ↑ Breithaupt, H., Pohl, M., Bönigk, W., Heim, P., Schimz, K.-L. and Kula, M.-R. (1999). "Cloning and expression of (R)-hydroxynitrile lyase from Linum usitatissimum (flax)". J. Mol. Catal. B 6: 315–332. doi:10.1016/s1381-1177(98)00109-x.
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