KEGG   ENZYME: 1.23.5.1
Entry
EC 1.23.5.1                 Enzyme                                 

Name
violaxanthin de-epoxidase;
VDE
Class
Oxidoreductases;
Reducing C-O-C group as acceptor;
With a quinone or similar compound as acceptor
Sysname
violaxanthin:ascorbate oxidoreductase
Reaction(IUBMB)
violaxanthin + 2 L-ascorbate = zeaxanthin + 2 L-dehydroascorbate + 2 H2O (overall reaction) [RN:R10055];
(1a) violaxanthin + L-ascorbate = antheraxanthin + L-dehydroascorbate + H2O [RN:R07178];
(1b) antheraxanthin + L-ascorbate = zeaxanthin + L-dehydroascorbate + H2O [RN:R07179]
Reaction(KEGG)
Substrate
violaxanthin [CPD:C08614];
L-ascorbate [CPD:C00072];
antheraxanthin [CPD:C08579]
Product
zeaxanthin [CPD:C06098];
L-dehydroascorbate [CPD:C05422];
H2O [CPD:C00001];
antheraxanthin [CPD:C08579]
Comment
Along with EC 1.14.15.21, zeaxanthin epoxidase, this enzyme forms part of the xanthophyll (or violaxanthin) cycle for controlling the concentration of zeaxanthin in chloroplasts. It is activated by a low pH of the thylakoid lumen (produced by high light intensity). Zeaxanthin induces the dissipation of excitation energy in the chlorophyll of the light-harvesting protein complex of photosystem II. In higher plants the enzyme reacts with all-trans-diepoxides, such as violaxanthin, and all-trans-monoepoxides, but in the alga Mantoniella squamata, only the diepoxides are good substrates.
History
EC 1.23.5.1 created 2005 as EC 1.10.99.3, transfered 2015 to EC 1.23.5.1
Pathway
ec00906  Carotenoid biosynthesis
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
Orthology
K09839  violaxanthin de-epoxidase
Genes
AJM: 119048578
EAF: 111708017 111717370 111717442
MYI: 110443578
PMAX: 117326486
LAK: 106154330
AQU: 109580811
ATH: AT1G08550(NPQ1)
ALY: 9325766
CRB: 17899434
CSAT: 104739447 104743187 104755037 104766742 104778627
BRP: 103871599
BOE: 106295314
RSZ: 108838113
THJ: 104805797
CPAP: 110814926
CIT: 102577994(VDE)
PVY: 116120711
TCC: 18599962
GRA: 105804540
GAB: 108470789
DZI: 111277831
EGR: 104432572
VRA: 106754170
VAR: 108343747
VUN: 114186755
CCAJ: 109798128
APRC: 113860823
CAM: 101494261
LJA: Lj1g3v5021040.1(Lj1g3v5021040.1)
ADU: 107491984
AIP: 107645737
LANG: 109329534
FVE: 101303237
RCN: 112194871
PPER: 18774598
PMUM: 103318745
PAVI: 110745041
PDUL: 117632799
MDM: 103414012
PXB: 103968091
ZJU: 107434703
MNT: 21389890
CSV: 101216870(VDE)
CMO: 103485865
BHJ: 120080031
MCHA: 111014204
CMAX: 111465513
CMOS: 111443955
CPEP: 111798056
RCU: 8260952
JCU: 105650425
HBR: 110642716
MESC: 110622852
POP: 7474648
PEU: 105132561
PALZ: 118036525
JRE: 108995788
QSU: 111995758
QLO: 115991765
TWL: 119996349
VVI: 100257865(VDE1)
VRI: 117912819
SLY: 543696(VDE)
SPEN: 107017754
SOT: 102588520
CANN: 107850430
NTA: 107763628(TVDE1) 107780507
NSY: 104218706
NTO: 104101769
NAU: 109212333
INI: 109192201
ITR: 115997377
SIND: 105161169
OEU: 111390352
EGT: 105955482
HAN: 110898842
LSV: 111889374
CCAV: 112512317
DCR: 108219423
CSIN: 114301681
BVG: 104890418
SOE: 110792983
NNU: 104590318
MING: 122077958
NCOL: 116250639
OSA: 4335625
DOSA: Os04t0379700-01(Os04g0379700)
OBR: 102708144
BDI: 100829969
ATS: 109771495
SBI: 8070802
ZMA: 100281366
SITA: 101754003
PHAI: 112899519
PDA: 103721734
EGU: 105038832
MUS: 103974860
DCT: 110102739
PEQ: 110038543
AOF: 109823913
ATR: 18425923
PPP: 112279974
MNG: MNEG_3176
CVR: CHLNCDRAFT_35609(VDE)
APRO: F751_1926
OLU: OSTLU_27727(VDE)
MIS: MICPUN_104842(VDE)
SMIN: v1.2.031718.t1(symbB.v1.2.031718.t1)
PTI: PHATRDRAFT_44635(VDE)
FCY: FRACYDRAFT_267113(VDE_1)
TPS: THAPSDRAFT_7677(DDE)
 » show all
Reference
1  [PMID:102251]
  Authors
Yamamoto HY, Higashi RM.
  Title
Violaxanthin de-epoxidase. Lipid composition and substrate specificity.
  Journal
Arch Biochem Biophys 190:514-22 (1978)
DOI:10.1016/0003-9861(78)90305-3
Reference
2  [PMID:8742341]
  Authors
Rockholm DC, Yamamoto HY
  Title
Violaxanthin de-epoxidase.
  Journal
Plant Physiol 110:697-703 (1996)
DOI:10.1104/pp.110.2.697
  Sequence
Reference
3  [PMID:9624110]
  Authors
Bugos RC, Hieber AD, Yamamoto HY
  Title
Xanthophyll cycle enzymes are members of the lipocalin family, the first identified from plants.
  Journal
J Biol Chem 273:15321-4 (1998)
DOI:10.1074/jbc.273.25.15321
  Sequence
[ath:AT1G08550] [ag:AAC50031]
Reference
4  [PMID:10635115]
  Authors
Kuwabara T, Hasegawa M, Kawano M, Takaichi S.
  Title
Characterization of violaxanthin de-epoxidase purified in the presence of Tween 20: effects of dithiothreitol and pepstatin A.
  Journal
Plant Cell Physiol 40:1119-26 (1999)
DOI:10.1093/oxfordjournals.pcp.a029496
Reference
5  [PMID:12230579]
  Authors
Latowski D, Kruk J, Burda K, Skrzynecka-Jaskier M, Kostecka-Gugala A, Strzalka K.
  Title
Kinetics of violaxanthin de-epoxidation by violaxanthin de-epoxidase, a xanthophyll cycle enzyme, is regulated by membrane fluidity in model lipid bilayers.
  Journal
Eur J Biochem 269:4656-65 (2002)
DOI:10.1046/j.1432-1033.2002.03166.x
Reference
6  [PMID:12748855]
  Authors
Goss R.
  Title
Substrate specificity of the violaxanthin de-epoxidase of the primitive green alga Mantoniella squamata (Prasinophyceae).
  Journal
Planta 217:801-12 (2003)
DOI:10.1007/s00425-003-1044-1
Reference
7  [PMID:15078086]
  Authors
Latowski D, Akerlund HE, Strzalka K
  Title
Violaxanthin de-epoxidase, the xanthophyll cycle enzyme, requires lipid inverted hexagonal structures for its activity.
  Journal
Biochemistry 43:4417-20 (2004)
DOI:10.1021/bi049652g
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 1.23.5.1
IUBMB Enzyme Nomenclature: 1.23.5.1
ExPASy - ENZYME nomenclature database: 1.23.5.1
BRENDA, the Enzyme Database: 1.23.5.1
CAS: 57534-73-3

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