KEGG   ENZYME: 1.1.1.316
Entry
EC 1.1.1.316                Enzyme                                 
Name
L-galactose 1-dehydrogenase;
L-GalDH;
L-galactose dehydrogenase
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With NAD+ or NADP+ as acceptor
Sysname
L-galactose:NAD+ 1-oxidoreductase
Reaction(IUBMB)
L-galactose + NAD+ = L-galactono-1,4-lactone + NADH + H+ [RN:R07675]
Reaction(KEGG)
R07675
Substrate
L-galactose [CPD:C01825];
NAD+ [CPD:C00003]
Product
L-galactono-1,4-lactone [CPD:C01115];
NADH [CPD:C00004];
H+ [CPD:C00080]
Comment
The enzyme catalyses a step in the ascorbate biosynthesis in higher plants (Smirnoff-Wheeler pathway). The activity with NADP+ is less than 10% of the activity with NAD+.
History
EC 1.1.1.316 created 2011
Pathway
ec00053  Ascorbate and aldarate metabolism
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
Orthology
K17744  L-galactose dehydrogenase
Genes
ATHAT4G33670
ALY9303236
CRB17878442
CSAT104716785 104721448 104729882
EUSEUTSA_v10025723mg
BRP103834464 103862253(GDH)
BNA106405751 106423369 106441159
BOE106303708
RSZ108822420 108830302 108854614 108854615
THJ104807192
CPAP110818987
CIT102621043
CICCICLE_v10028842mg
PVY116135288
MINC123214637 123227460
TCC18607308
GRA105763009
GHI107932176 107945119
GAB108479971
DZI111308642
EGR104453016
GMX100809400
GSJ114421349
PVUPHAVU_002G216600g
VRA106765834
VAR108332744
VUN114176640
CCAJ109809791
APRC113858444
MTRMTR_4g092750
CAM101495571
LJALj0g3v0243739.1(Lj0g3v0243739.1) Lj4g3v0410570.2(Lj4g3v0410570.2)
ADU107480539
AIP107626271
AHF112728671 112791338
LANG109331942
FVE101299720
RCN112173603
PPER18766583
PMUM103334968
PAVI110757233
PDUL117637213
MDM103436244
PXB103938180
ZJU107427462
MNT21384512
CSV101206435
CMO103495364
BHJ120078242
MCHA111022462
CMAX111471025
CMOS111455013
CPEP111776398
RCU8279173
JCU105635996
HBR110646467 110646472 110661187
MESC110619655
POP7469673 7470777
PEU105109729 105129751
PALZ118048615 118051811
JRE108995719
QSU112040078
QLO115969021
TWL120004024
VVI100263479(GDH)
VRI117911468
SLY101254135
SPEN107006598
SOT102599558
SSTN125844747
CANN107840121
NTA107806546 107824481
NSY104219974
NTO104103548
NAU109213589
INI109165254
ITR116031480
SIND105169328
OEU111388928
EGT105949697
SSPL121805512 121809633
HAN110877998
ECAD122600300
LSV111881024
CCAV112500306
DCR108224817
CSIN114284603
BVG104904801
SOE110788012
CQI110681692 110685042 110740027
NNU104607573
MING122083448
TSS122658162
PSOM113333373 113347404
NCOL116251589
OSA4352223
DOSAOs12t0482700-01(Os12g0482700)
OBR102719064
BDI100840848
ATS109753847
TDC119299280 119307458
TAES123102293 123110451 123119474
TUA125529237
SBI8063259
ZMA732776
SITA101762145
SVS117849804
PVIR120666191 120699475
PHAI112884567
PDA103707620
EGU105055920
MUS103979808
DCT110113925
PEQ110018172 110034538
AOF109834292
ATR18442443
SMOSELMODRAFT_109892 SELMODRAFT_123995 SELMODRAFT_124085 SELMODRAFT_153099
PPP112284227 112284471
CRECHLRE_14g630400v5
VCNVOLCADRAFT_93987
MNGMNEG_15134
CSLCOCSUDRAFT_18370 COCSUDRAFT_34922
CVRCHLNCDRAFT_25289
APROF751_2396
CCPCHC_T00010069001
 » show all
Reference
1  [PMID:15509850]
  Authors
Mieda T, Yabuta Y, Rapolu M, Motoki T, Takeda T, Yoshimura K, Ishikawa T, Shigeoka S
  Title
Feedback inhibition of spinach L-galactose dehydrogenase by L-ascorbate.
  Journal
Plant Cell Physiol 45:1271-9 (2004)
DOI:10.1093/pcp/pch152
  Sequence
Reference
2  [PMID:12047629]
  Authors
Gatzek S, Wheeler GL, Smirnoff N
  Title
Antisense suppression of l-galactose dehydrogenase in Arabidopsis thaliana provides evidence for its role in ascorbate synthesis and reveals light modulated l-galactose synthesis.
  Journal
Plant J 30:541-53 (2002)
DOI:10.1046/j.1365-313X.2002.01315.x
  Sequence
[ath:AT4G33670]
Reference
3  [PMID:9620799]
  Authors
Wheeler GL, Jones MA, Smirnoff N
  Title
The biosynthetic pathway of vitamin C in higher plants.
  Journal
Nature 393:365-9 (1998)
DOI:10.1038/30728
Reference
4  [PMID:19297184]
  Authors
Oh MM, Carey EE, Rajashekar CB
  Title
Environmental stresses induce health-promoting phytochemicals in lettuce.
  Journal
Plant Physiol Biochem 47:578-83 (2009)
DOI:10.1016/j.plaphy.2009.02.008
Other DBs
ExplorEnz - The Enzyme Database: 1.1.1.316
IUBMB Enzyme Nomenclature: 1.1.1.316
ExPASy - ENZYME nomenclature database: 1.1.1.316
BRENDA, the Enzyme Database: 1.1.1.316

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