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, transferred 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
AJM119048578
EAF111708017 111717370 111717442
HRF124127355
MYI110443578
PMAX117326486
LAK106154330
AQU109580811
ATHAT1G08550(NPQ1)
ALY9325766
CRB17899434
CSAT104739447 104743187 104755037 104766742 104778627
EUSEUTSA_v10007587mg
BRP103871599
BNA106346323 106415200
BOE106295314
RSZ108838113
THJ104805797
CPAP110814926
CIT102577994(VDE)
CICCICLE_v10019925mg
PVY116120711
MINC123209056
TCC18599962
GRA105804540
GHI107892463 107961898
GAB108470789
DZI111277831
EGR104432572
GMX100778118 100816085
GSJ114400542 114407765
PVUPHAVU_006G108200g
VRA106754170
VAR108343747
VUN114186755
CCAJ109798128
APRC113860823
MTR11429816
CAM101494261
LJALj1g3v5021040.1(Lj1g3v5021040.1)
ADU107491984
AIP107645737
AHF112695354 112758625
LANG109329534
FVE101303237
RCN112194871
PPER18774598
PMUM103318745
PAVI110745041
PDUL117632799
MDM103414012
PXB103968091
ZJU107434703
MNT21389890
CSV101216870(VDE)
CMO103485865
BHJ120080031
MCHA111014204
CMAX111465513
CMOS111443955
CPEP111798056
RCU8260952
JCU105650425
HBR110642716
MESC110622852
POP7474648
PEU105132561
PALZ118036525
JRE108995788
QSU111995758
QLO115991765
TWL119996349
VVI100257865(VDE1)
VRI117912819
SLY543696(VDE)
SPEN107017754
SOT102588520
SSTN125856526
CANN107850430
NTA107763628(TVDE1) 107780507
NSY104218706
NTO104101769
NAU109212333
INI109192201
ITR115997377
SIND105161169
OEU111390352
EGT105955482
SSPL121751030 121780456 121782995 121783809
HAN110898842
ECAD122581672
LSV111889374
CCAV112512317
DCR108219423
CSIN114301681
BVG104890418
SOE110792983
CQI110708773 110736759
NNU104590318
MING122077958
TSS122655509
PSOM113282971 113296739
NCOL116250639
OSA4335625
DOSAOs04t0379700-01(Os04g0379700)
OBR102708144
BDI100829969
ATS109771495
TDC119354938 119364074
TAES123053120 123189027 542859
TUA125537746
SBI8070802
ZMA100281366
SITA101754003
SVS117863445
PVIR120640699 120681920
PHAI112899519
PDA103721734
EGU105038832
MUS103974860
DCT110102739
PEQ110038543
AOF109823913
ATR18425923
SMOSELMODRAFT_121553 SELMODRAFT_182267
PPP112279974
MNGMNEG_3176
CSLCOCSUDRAFT_4775
CVRCHLNCDRAFT_35609(VDE)
APROF751_1926
OLUOSTLU_27727(VDE)
OTAOT_ostta16g00660
BPGBathy07g04400
MISMICPUN_104842(VDE)
MPPMICPUCDRAFT_60541(VDE)
SMINv1.2.031718.t1(symbB.v1.2.031718.t1)
PTIPHATRDRAFT_44635(VDE)
FCYFRACYDRAFT_267113(VDE_1)
TPSTHAPSDRAFT_7677(DDE)
NGDNGA_0074200 NGA_0270002(VDE)
AAFAURANDRAFT_2523
EHXEMIHUDRAFT_200654 EMIHUDRAFT_365129 EMIHUDRAFT_455406(VDE)
GTTGUITHDRAFT_109359
 » 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

DBGET integrated database retrieval system