Mandelonitrile lyase

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

\rightleftharpoons

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.
Becker W; 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. PMID 6803611. doi:10.1016/0003-2697(82)90660-1.
Xu LL, Singh BK, Conn EE (1986). "Purification and characterization of mandelonitrile lyase from Prunus lyonii". Arch. Biochem. Biophys. 250 (2): 322–8. PMID 3777939. doi:10.1016/0003-9861(86)90733-2.
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. PMID 3717954. doi:10.1016/0003-9861(86)90604-1.

Carbon-carbon lyases (EC 4.1)
4.1.1: Carboxy-lyases	Acetoacetate decarboxylase Adenosylmethionine decarboxylase Arginine decarboxylase Aromatic L-amino acid decarboxylase Glutamate decarboxylase Histidine decarboxylase Lysine decarboxylase Malonyl-CoA decarboxylase Ornithine decarboxylase Oxaloacetate decarboxylase Phosphoenolpyruvate carboxykinase Phosphoenolpyruvate carboxylase Phosphoribosylaminoimidazole carboxylase Pyrophosphomevalonate decarboxylase Pyruvate decarboxylase RuBisCO Uridine monophosphate synthetase/Orotidine 5'-phosphate decarboxylase Uroporphyrinogen III decarboxylase
4.1.2: Aldehyde-lyases	Fructose-bisphosphate aldolase Aldolase A Aldolase B Aldolase C 2-hydroxyphytanoyl-CoA lyase Threonine aldolase
4.1.3: Oxo-acid-lyases	Isocitrate lyase 3-hydroxy-3-methylglutaryl-CoA lyase
4.1.99: Other	Tryptophanase Photolyase CPD lyase Spore photoproduct lyase

Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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