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Mandelonitrile lyase

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mandelonitrile lyase
Identifiers
EC no.4.1.2.10
CAS no.9024-43-5
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
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Model of mandelonitrile lyase based on PDB entry 1JU2

In enzymology, a mandelonitrile lyase (EC 4.1.2.10, (R)-HNL, (R)-oxynitrilase, (R)-hydroxynitrile lyase) is an enzyme that catalyzes the chemical reaction

mandelonitrile hydrogen cyanide + benzaldehyde

Hence, this enzyme has one substrate, mandelonitrile, and two products, hydrogen cyanide and benzaldehyde.

This enzyme belongs to the family of lyases, specifically the aldehyde-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is mandelonitrile benzaldehyde-lyase (hydrogen cyanide-forming). Other names in common use include hydroxynitrile lyase, (R)-oxynitrilase, oxynitrilase, D-oxynitrilase, D-alpha-hydroxynitrile lyase, and mandelonitrile benzaldehyde-lyase. This enzyme participates in cyanoamino acid metabolism. It has 2 cofactors: flavin, and flavoprotein.

Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1JU2.

References

  • BECKER W, BENTHIN U, ESCHENHOF E, PFEIL E (1963). "[On the knowledge of cyanhydrin synthesis. II. Purification and properties of hydroxynitrilase from bitter almonds (Prunus communis Stokes)]". Biochem. Z. 337: 156–66. PMID 13970146.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  • Becker W and Pfeil E (1964). "Die Darstellung kristallisierter Oxynitrilase aus bitteren Mandeln (Prunus comm. Stks)". Naturwissenschaften. 51 (8): 193. doi:10.1007/BF00600723.
  • Gross M, Jacobs GH, Poulton JE (1982). "A rapid and sensitive spectrophotometric assay for prunasin hydrolase activity employing purified mandelonitrile lyase". Anal. Biochem. 119 (1): 25–30. doi:10.1016/0003-2697(82)90660-1. PMID 6803611.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  • Xu LL, Singh BK, Conn EE (1986). "Purification and characterization of mandelonitrile lyase from Prunus lyonii". Arch. Biochem. Biophys. 250 (2): 322–8. doi:10.1016/0003-9861(86)90733-2. PMID 3777939.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  • Yemm RS, Poulton JE (1986). "Isolation and characterization of multiple forms of mandelonitrile lyase from mature black cherry (Prunus serotina Ehrh.) seeds". Arch. Biochem. Biophys. 247 (2): 440–5. doi:10.1016/0003-9861(86)90604-1. PMID 3717954.