Biology:Aliphatic (R)-hydroxynitrile lyase
From HandWiki
| Aliphatic (R)-hydroxynitrile lyase | |||||||||
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| Identifiers | |||||||||
| EC number | 4.1.2.46 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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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 [math]\displaystyle{ \rightleftharpoons }[/math] cyanide + butan-2-one
The enzyme contains Zn2+.
References
- ↑ Trummler, K.; Roos, J.; Schwaneberg, U.; Effenberger, F.; Förster, S.; Pfizenmaier, K.; 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.; 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.
- ↑ "Improved purification of an (R)-oxynitrilase from Linum usitatissimum (flax) and investigation of the substrate range". Biotechnol. Appl. Biochem. 17 (2): 191–203. 1993. PMID 8387315.
- ↑ Xu, L.-L.; Singh, B.K.; Conn, E.E. (1988). "Purification and characterization of acetone cyanohydrin lyase from Linum usitatissimum". Arch. Biochem. Biophys. 263 (2): 256–263. doi:10.1016/0003-9861(88)90634-0. PMID 3377504.
- ↑ Cabirol, F.L.; Tan, P.L.; Tay, B.; Cheng, S.; Hanefeld, U.; Sheldon, R.A. (2008). "Linum usitatissimum hydroxynitrile lyase cross-linked enzyme aggregates: a recyclable enantioselective catalyst". Adv. Synth. Catal. 350 (14–15): 2329–2338. doi:10.1002/adsc.200800309.
- ↑ Breithaupt, H.; Pohl, M.; Bönigk, W.; Heim, P.; Schimz, K.-L.; Kula, M.-R. (1999). "Cloning and expression of (R)-hydroxynitrile lyase from Linum usitatissimum (flax)". J. Mol. Catal. B 6 (3): 315–332. doi:10.1016/S1381-1177(98)00109-X.
External links
- Aliphatic+(R)-hydroxynitrile+lyase at the US National Library of Medicine Medical Subject Headings (MeSH)
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