The Enzyme Database

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EC 1.1.3.49     
Accepted name: (R)-mandelonitrile oxidase
Reaction: (R)-mandelonitrile + O2 = benzoyl cyanide + H2O2
Glossary: (R)-mandelonitrile = (R)-2-hydroxy-2-phenylacetonitrile
Other name(s): ChuaMOX (gene name)
Systematic name: (R)-mandelonitrile:oxygen oxidoreductase
Comments: Contains FAD. The enzyme, characterized from the millipede Chamberlinius hualienensis, is segregated from its substrate, which is contained in special sacs. The sacs are ruptured during defensive behavior, allowing the enzyme and substrate to mix in special reaction chambers leading to production of the defensive chemical benzoyl cyanide.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ishida, Y., Kuwahara, Y., Dadashipour, M., Ina, A., Yamaguchi, T., Morita, M., Ichiki, Y. and Asano, Y. A sacrificial millipede altruistically protects its swarm using a drone blood enzyme, mandelonitrile oxidase. Sci. Rep. 6:26998 (2016). [DOI] [PMID: 27265180]
[EC 1.1.3.49 created 2016]
 
 
EC 1.14.14.44     
Accepted name: phenylacetaldehyde oxime monooxygenase
Reaction: (E)-phenylacetaldehyde oxime + [reduced NADPH—hemoprotein reductase] + O2 = (R)-mandelonitrile + [oxidized NADPH—hemoprotein reductase] + 2 H2O (overall reaction)
(1a) (E)-phenylacetaldehyde oxime = (Z)-phenylacetaldehyde oxime
(1b) (Z)-phenylacetaldehyde oxime = phenylacetonitrile + H2O
(1c) phenylacetonitrile + [reduced NADPH—hemoprotein reductase] + O2 = (R)-mandelonitrile + [oxidized NADPH—hemoprotein reductase] + H2O
Glossary: (R)-mandelonitrile = (2R)-hydroxy(phenyl)acetonitrile
Other name(s): CYP71AN24 (gene name)
Systematic name: (E)-phenylacetaldehyde oxime,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase
Comments: This cytochrome P-450 (heme-thiolate) enzyme is involved in the biosynthesis of the cyanogenic glucosides (R)-prunasin and (R)-amygdalin. It catalyses three different activities - isomerization of the (E) isomer to the (Z) isomer, dehydration, and C-hydroxylation.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Yamaguchi, T., Yamamoto, K. and Asano, Y. Identification and characterization of CYP79D16 and CYP71AN24 catalyzing the first and second steps in L-phenylalanine-derived cyanogenic glycoside biosynthesis in the Japanese apricot, Prunus mume Sieb. et Zucc. Plant Mol. Biol. 86 (2014) 215–223. [DOI] [PMID: 25015725]
[EC 1.14.14.44 created 2017]
 
 
EC 1.14.14.77     
Accepted name: phenylacetonitrile α-monooxygenase
Reaction: phenylacetonitrile + [reduced NADPH—hemoprotein reductase] + O2 = (R)-mandelonitrile + [oxidized NADPH—hemoprotein reductase] + H2O
Other name(s): CYP3201B1 (gene name)
Systematic name: phenylacetonitrile,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase [(R)-mandelonitrile-forming]
Comments: The enzyme has been characterized from the cyanogenic millipede Chamberlinius hualienensis. Unlike plant enzymes that can catalyse this reaction (EC 1.14.14.44, phenylacetaldehyde oxime monooxygenase), this enzyme cannot act on phenylacetaldehyde oximes. It can accept (4-hydroxyphenyl)acetonitrile, (2-methylphenyl)acetonitrile, and (3-methylphenyl)acetonitrile as substrates at a lower rate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Yamaguchi, T., Kuwahara, Y. and Asano, Y. A novel cytochrome P450, CYP3201B1, is involved in (R)-mandelonitrile biosynthesis in a cyanogenic millipede. FEBS Open Bio 7 (2017) 335–347. [DOI] [PMID: 28286729]
[EC 1.14.14.77 created 2018]
 
 
EC 2.4.1.354     
Accepted name: (R)-mandelonitrile β-glucosyltransferase
Reaction: UDP-α-D-glucose + (R)-mandelonitrile = UDP + (R)-prunasin
Glossary: (R)-mandelonitrile = (2R)-hydroxy(phenyl)acetonitrile
(R)-prunasin = (2R)-(β-D-glucosyloxy)(phenyl)acetonitrile
Other name(s): UGT85A19 (gene name)
Systematic name: UDP-α-D-glucose:(R)-mandelonitrile β-D-glucosyltransferase (configuration-inverting)
Comments: The enzyme, characterized from Prunus dulcis (almond), is involved in the biosynthesis of the cyanogenic glycosides (R)-prunasin and (R)-amygdalin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Franks, T. K., Yadollahi, A., Wirthensohn, M. G., Guerin, J. R., Kaiser, B. N., Sedgley, M. and Ford, C. M. A seed coat cyanohydrin glucosyltransferase is associated with bitterness in almond (Prunus dulcis) kernels. Funct. Plant Biol. 35 (2008) 236–246.
[EC 2.4.1.354 created 2018]
 
 
EC 4.1.2.10     
Accepted name: (R)-mandelonitrile lyase
Reaction: (R)-mandelonitrile = cyanide + benzaldehyde
Other name(s): (R)-oxynitrilase; oxynitrilase; D-oxynitrilase; D-α-hydroxynitrile lyase; mandelonitrile benzaldehyde-lyase; PaHNL; AtHNL; PhaMDL; (R)-HNL; (R)-PeHNL; (R)-hydroxynitrile lyase; R-selective hydroxynitrile lyase; R-selective HNL; (R)-(+)-mandelonitrile lyase
Systematic name: (R)-mandelonitrile benzaldehyde-lyase (cyanide-forming)
Comments: A variety of enzymes from different sources and with different properties. Some are flavoproteins, others are not. Active towards a number of aromatic and aliphatic hydroxynitriles (cyanohydrins).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9024-43-5
References:
1.  Ueatrongchit, T., Kayo, A., Komeda, H., Asano, Y. and H-Kittikun, A. Purification and characterization of a novel (R)-hydroxynitrile lyase from Eriobotrya japonica (Loquat). Biosci. Biotechnol. Biochem. 72 (2008) 1513–1522. [DOI] [PMID: 18540101]
2.  Lin, G., Han, S. and Li, Z. Enzymic synthesis of (R)-cyanohydrins by three (R)-oxynitrilase sources in micro-aqueous organic medium. Tetrahedron 55 (1999) 3531–3540.
3.  de Gonzalo, G., Brieva, R. and Gotor, V. (R)-Oxynitrilase-catalyzed transformation of ω-hydroxyalkanals. J. Mol. Catal. B 19-20 (2002) 223–230.
4.  Ueatrongchit, T., Tamura, K., Ohmiya, T., H-Kittikun, A. and Asano, Y. Hydroxynitrile lyase from Passiflora edulis. Purification, characteristics and application in asymmetric synthesis of (R)-mandelonitrile. Enzyme Microb. Technol. 46 (2010) 456–465. [PMID: 25919621]
5.  Andexer, J., von Langermann, J., Mell, A., Bocola, M., Kragl, U., Eggert, T. and Pohl, M. An R-selective hydroxynitrile lyase from Arabidopsis thaliana with an α/β-hydrolase fold. Angew. Chem. Int. Ed. Engl. 46 (2007) 8679–8681. [DOI] [PMID: 17907254]
6.  Guterl, J.K., Andexer, J.N., Sehl, T., von Langermann, J., Frindi-Wosch, I., Rosenkranz, T., Fitter, J., Gruber, K., Kragl, U., Eggert, T. and Pohl, M. Uneven twins: comparison of two enantiocomplementary hydroxynitrile lyases with α/β-hydrolase fold. J. Biotechnol. 141 (2009) 166–173. [DOI] [PMID: 19433222]
[EC 4.1.2.10 created 1961, modified 1999, modified 2011]
 
 


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