KEGG   ENZYME: 4.1.2.47Help
Entry
EC 4.1.2.47                 Enzyme                                 

Name
(S)-hydroxynitrile lyase;
(S)-cyanohydrin producing hydroxynitrile lyase;
(S)-oxynitrilase;
(S)-HbHNL;
(S)-MeHNL;
hydroxynitrile lyase;
oxynitrilase;
HbHNL;
MeHNL;
(S)-selective hydroxynitrile lyase;
(S)-cyanohydrin carbonyl-lyase (cyanide forming)
Class
Lyases;
Carbon-carbon lyases;
Aldehyde-lyases
BRITE hierarchy
Sysname
(S)-cyanohydrin lyase (cyanide forming)
Reaction(IUBMB)
(1) an aliphatic (S)-hydroxynitrile = cyanide + an aliphatic aldehyde or ketone;
(2) an aromatic (S)-hydroxynitrile = cyanide + an aromatic aldehyde [RN:R09359]
Reaction(KEGG)
R09359;
(other) R01409 R02811
Show
Substrate
aliphatic (S)-hydroxynitrile;
aromatic (S)-hydroxynitrile
Product
cyanide [CPD:C01326];
aliphatic aldehyde;
aliphatic ketone;
aromatic aldehyde [CPD:C00193]
Comment
Hydroxynitrile lyases catalyses the the cleavage of hydroxynitriles into cyanide and the corresponding aldehyde or ketone. In nature the liberation of cyanide serves as a defense mechanism against herbivores and microbial attack in plants. In vitro the enzymes from Manihot esculenta and Hevea brasiliensis accept a broad range of aliphatic and aromatic carbonyl compounds as substrates and catalyse the formation of (S)-hydroxynitriles [1,10].
History
EC 4.1.2.47 created 2011
Pathway
ec00460  Cyanoamino acid metabolism
ec01110  Biosynthesis of secondary metabolites
Orthology
K13033  (S)-hydroxynitrile lyase
Reference
1
  Authors
Forster, S., Roos, J., Effenberger, F., Wajant, H. and Sprauer, A.
  Title
The first recombinant hydroxynitrile lyase and its application in the synthesis of (S)-cyanohydrins.
  Journal
Angew Chem Int Ed 35:437-439 (1996)
Reference
2  [PMID:12616635]
  Authors
Buhler H, Effenberger F, Forster S, Roos J, Wajant H
  Title
Substrate specificity of mutants of the hydroxynitrile lyase from Manihot esculenta.
  Journal
Chembiochem 4:211-6 (2003)
DOI:10.1002/cbic.200390033
Reference
3  [PMID:18540112]
  Authors
Semba H, Dobashi Y, Matsui T
  Title
Expression of hydroxynitrile lyase from Manihot esculenta in yeast and its application in (S)-mandelonitrile production using an immobilized enzyme reactor.
  Journal
Biosci Biotechnol Biochem 72:1457-63 (2008)
Reference
4  [PMID:19006143]
  Authors
Avi M, Wiedner RM, Griengl H, Schwab H
  Title
Improvement of a stereoselective biocatalytic synthesis by substrate and enzyme engineering: 2-hydroxy-(4'-oxocyclohexyl)acetonitrile as the model.
  Journal
Chemistry 14:11415-22 (2008)
DOI:10.1002/chem.200800609
Reference
5  [PMID:18204865]
  Authors
von Langermann J, Guterl JK, Pohl M, Wajant H, Kragl U
  Title
Hydroxynitrile lyase catalyzed cyanohydrin synthesis at high pH-values.
  Journal
Bioprocess Biosyst Eng 31:155-61 (2008)
DOI:10.1007/s00449-008-0198-4
Reference
6  [PMID:18524775]
  Authors
Schmidt A, Gruber K, Kratky C, Lamzin VS
  Title
Atomic resolution crystal structures and quantum chemistry meet to reveal subtleties of hydroxynitrile lyase catalysis.
  Journal
J Biol Chem 283:21827-36 (2008)
DOI:10.1074/jbc.M801056200
Reference
7  [PMID:17250917]
  Authors
Gartler G, Kratky C, Gruber K
  Title
Structural determinants of the enantioselectivity of the hydroxynitrile lyase from Hevea brasiliensis.
  Journal
J Biotechnol 129:87-97 (2007)
DOI:10.1016/j.jbiotec.2006.12.009
Reference
8  [PMID:15299689]
  Authors
Wagner UG, Schall M, Hasslacher M, Hayn M, Griengl H, Schwab H, Kratky C
  Title
Crystallization and preliminary X-ray diffraction studies of a hydroxynitrile lyase from Hevea brasiliensis.
  Journal
Acta Crystallogr D Biol Crystallogr 52:591-3 (1996)
DOI:10.1107/S0907444995016830
Reference
9
  Authors
Schmidt, M., Herve, S., Klempier, N. and Griengl, H.
  Title
Preparation of optically active cyanohydrins using the (S)-hydroxynitrile lyase from Hevea brasiliensis.
  Journal
Tetrahedron 52:7833-7840 (1996)
Reference
10
  Authors
Klempier, N. and Griengl, H.
  Title
Aliphatic (S)-cyanohydrins by enzyme catalyzed synthesis.
  Journal
Tetrahedron Lett 34:4769-4772 (1993)
Other DBs
ExplorEnz - The Enzyme Database: 4.1.2.47
IUBMB Enzyme Nomenclature: 4.1.2.47
ExPASy - ENZYME nomenclature database: 4.1.2.47
BRENDA, the Enzyme Database: 4.1.2.47

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