KEGG   ENZYME: 4.1.2.10
Entry
EC 4.1.2.10                 Enzyme                                 

Name
(R)-mandelonitrile lyase;
(R)-oxynitrilase;
oxynitrilase;
D-oxynitrilase;
D-alpha-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
Class
Lyases;
Carbon-carbon lyases;
Aldehyde-lyases
Sysname
(R)-mandelonitrile benzaldehyde-lyase (cyanide-forming)
Reaction(IUBMB)
(R)-mandelonitrile = cyanide + benzaldehyde [RN:R01767]
Reaction(KEGG)
R01767;
(other) R01409 R02811
Substrate
(R)-mandelonitrile [CPD:C00561]
Product
cyanide [CPD:C00177];
benzaldehyde [CPD:C00261]
Comment
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).
History
EC 4.1.2.10 created 1961, modified 1999, modified 2011
Pathway
ec00460  Cyanoamino acid metabolism
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
Orthology
K08248  (R)-mandelonitrile lyase
K20802  (R)-mandelonitrile lyase
Genes
ATH: AT1G73050 AT5G10300(MES5)
ALY: 9324968
CRB: 17882602 17894548
CSAT: 104701992 104712914 104751159
EUS: EUTSA_v10014451mg EUTSA_v10018360mg
BRP: 103831793 103846819 103852822
BNA: 106354249 106372481 106378088 106379433 106381275 106404872
BOE: 106299217 106327722
RSZ: 108814498 108841961 108841964
THJ: 104798892 104812207
CIT: 102626291
PVY: 116104932
TCC: 18595196
GRA: 105767552
DZI: 111280688
EGR: 104423258
GMX: 100820069
GSJ: 114419167
VRA: 106773780
VAR: 108320669
VUN: 114165905
CCAJ: 109808261
APRC: 113857241
CAM: 101508164
LJA: Lj3g3v2040180.1(Lj3g3v2040180.1)
ADU: 107482361
AIP: 107635832
LANG: 109356592
JCU: 105643749
HBR: 110655857
POP: 7490862
QSU: 112001779
QLO: 115989370
VVI: 100254058
VRI: 117905746
SLY: 101250204
SPEN: 107014093
SOT: 102580581
CANN: 107865788
NSY: 104246964
NTO: 104107041
NAU: 109224695
SIND: 105157899
OEU: 111401494
EGT: 105954354
CSIN: 114311932
BVG: 104901404
SOE: 110785208
NNU: 104599090
MING: 122073004
NCOL: 116250416
OSA: 9266710
DOSA: Os06t0656000-00(Os06g0656000)
OBR: 102719124
BDI: 100822804
ATS: 109783110
SBI: 8069366
ZMA: 100382914
SITA: 101763110
PHAI: 112888364
PDA: 103715972
EGU: 105039402
MUS: 103977401
DCT: 110096808
 » show all
Reference
1  [PMID:18540101]
  Authors
Ueatrongchit T, Kayo A, Komeda H, Asano Y, H-Kittikun A
  Title
Purification and characterization of a novel (R)-hydroxynitrile lyase from Eriobotrya japonica (Loquat).
  Journal
Biosci Biotechnol Biochem 72:1513-22 (2008)
DOI:10.1271/bbb.80023
Reference
2
  Authors
Lin, G., Han, S. and Li, Z.
  Title
Enzymic synthesis of (R)-cyanohydrins by three (R)-oxynitrilase sources in micro-aqueous organic medium.
  Journal
Tetrahedron 55:3531-3540 (1999)
Reference
3
  Authors
de Gonzalo, G., Brieva, R. and Gotor, V.
  Title
(R)-Oxynitrilase-catalyzed transformation of omega-hydroxyalkanals.
  Journal
J Mol Catal B 19-20:223-230 (2002)
Reference
4  [PMID:25919621]
  Authors
Ueatrongchit T, Tamura K, Ohmiya T, H-Kittikun A, Asano Y
  Title
Hydroxynitrile lyase from Passiflora edulis: Purification, characteristics and application in asymmetric synthesis of (R)-mandelonitrile.
  Journal
Enzyme Microb Technol 46:456-65 (2010)
DOI:10.1016/j.enzmictec.2010.02.008
Reference
5  [PMID:17907254]
  Authors
Andexer J, von Langermann J, Mell A, Bocola M, Kragl U, Eggert T, Pohl M
  Title
An R-selective hydroxynitrile lyase from Arabidopsis thaliana with an alpha/beta-hydrolase fold.
  Journal
Angew Chem Int Ed Engl 46:8679-81 (2007)
DOI:10.1002/anie.200701455
  Sequence
[ath:AT5G10300]
Reference
6  [PMID:19433222]
  Authors
Guterl JK, Andexer JN, Sehl T, von Langermann J, Frindi-Wosch I, Rosenkranz T, Fitter J, Gruber K, Kragl U, Eggert T, Pohl M
  Title
Uneven twins: comparison of two enantiocomplementary hydroxynitrile lyases with alpha/beta-hydrolase fold.
  Journal
J Biotechnol 141:166-73 (2009)
DOI:10.1016/j.jbiotec.2009.03.010
  Sequence
[ath:AT5G10300]
Other DBs
ExplorEnz - The Enzyme Database: 4.1.2.10
IUBMB Enzyme Nomenclature: 4.1.2.10
ExPASy - ENZYME nomenclature database: 4.1.2.10
BRENDA, the Enzyme Database: 4.1.2.10
CAS: 9024-43-5

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