KEGG   ENZYME: 1.3.2.3
Entry
EC 1.3.2.3                  Enzyme                                 
Name
L-galactonolactone dehydrogenase;
galactonolactone dehydrogenase;
L-galactono-gamma-lactone dehydrogenase;
L-galactono-gamma-lactone:ferricytochrome-c oxidoreductase;
GLDHase;
GLDase
Class
Oxidoreductases;
Acting on the CH-CH group of donors;
With a cytochrome as acceptor
Sysname
L-galactono-1,4-lactone:ferricytochrome-c oxidoreductase
Reaction(IUBMB)
L-galactono-1,4-lactone + 4 ferricytochrome c = L-dehydroascorbate + 4 ferrocytochrome c + 4 H+ (overall reaction) [RN:R12144];
(1a) L-galactono-1,4-lactone + 2 ferricytochrome c = L-ascorbate + 2 ferrocytochrome c + 2 H+ [RN:R00640];
(1b) L-ascorbate + 2 ferricytochrome c = L-dehydroascorbate + 2 ferrocytochrome c + 2 H+ (spontaneous) [RN:R07679]
Reaction(KEGG)
Substrate
L-galactono-1,4-lactone [CPD:C01115];
ferricytochrome c [CPD:C00125];
L-ascorbate [CPD:C00072]
Product
L-dehydroascorbate [CPD:C05422];
ferrocytochrome c [CPD:C00126];
H+ [CPD:C00080];
L-ascorbate [CPD:C00072]
Comment
This enzyme catalyses the final step in the biosynthesis of L-ascorbic acid in higher plants and in nearly all higher animals with the exception of primates and some birds [5]. The enzyme is very specific for its substrate L-galactono-1,4-lactone as D-galactono-gamma-lactone, D-gulono-gamma-lactone, L-gulono-gamma-lactone, D-erythronic-gamma-lactone, D-xylonic-gamma-lactone, L-mannono-gamma-lactone, D-galactonate, D-glucuronate and D-gluconate are not substrates [5]. FAD, NAD+, NADP+ and O2 (cf. EC 1.3.3.12, L-galactonolactone oxidase) cannot act as electron acceptor [5].
History
EC 1.3.2.3 created 1961, modified 2006
Pathway
ec00053  Ascorbate and aldarate metabolism
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
Orthology
K00225  L-galactono-1,4-lactone dehydrogenase
Genes
ATHAT3G47930(GLDH)
ALY9313653
CRB17884875
CSAT104711271 104780602 104791004
EUSEUTSA_v10010214mg
BRP103873188(GLDH)
BNA106389550 106410745 111211168
BOE106335860
RSZ108812165
THJ104816408
CPAP110822775
CIT102611546
CICCICLE_v100046031m
PVY116132103 116145983
MINC123217160
TCC18598808
GRA105761589
GHI107925893 107942591
GAB108473872
DZI111311469
EGR104444330
GMX100526948 100793515
GSJ114372241 114391681
PVUPHAVU_007G247900g
VRA106772555
VAR108326445
VUN114191879
CCAJ109805599
APRC113871303
MTRMTR_1g050360
CAM101498593
LJALj5g3v0931500.1(Lj5g3v0931500.1)
ADU107474610
AIP107625443
AHF112727599 112745243
LANG109336341
FVE101296499
RCN112187885
PPER18769548
PMUM103339235
PAVI110770247
PDUL117634125
MDM103423291
PXB103933975 103940638
ZJU107431670 107433785
MNT21398632
CSV101215955
CMO103497260
BHJ120073973
MCHA111021307
CMAX111465966
CMOS111432481
CPEP111781077
RCU8286649
JCU105645077
HBR110672781
MESC110620975
POP7464114
PEU105131724
PALZ118031930
JRE108981186
QSU112012043
QLO115952607
TWL119992580 119998352
VVI100233005
VRI117921229
SLY544206(gldh)
SPEN107002402
SOT102577860(GLDH)
CANN107843896(GLDH1)
NTA107787357 107793071(GLDHase) 107806941
NSY104221614
NTO104110446
NAU109233051
INI109182270
ITR116006922
SIND105159882
OEU111392244
EGT105949321
SSPL121749499 121753111
HAN110897681
ECAD122581438
LSV111904091
CCAV112512576
DCR108227887
CSIN114256949
BVG104889449
SOE110778008
CQI110710509 110712825
NNU104608844
MING122065810
TSS122649967 122650837 122651937
PSOM113322103
NCOL116246335
OSA4349749 4351464
DOSAOs11t0143500-01(Os11g0143500) Os12t0139600-01(Os12g0139600)
OBR102701949 102720290
BDI100840661
ATS109745724
TDC119308312
TAES123103035 123111215 123120310
SBI110435654
ZMA100381436
SITA101756029 101769296
SVS117833525 117863849
PVIR120643526 120684672
PHAI112887043 112902336
PDA103720720
EGU105045546
MUS103988691
DCT110114488
PEQ110018206
AOF109827193
ATR18433193
SMOSELMODRAFT_105274 SELMODRAFT_98882
PPP112290963
CRECHLRE_13g567100v5
VCNVOLCADRAFT_88191
MNGMNEG_10953
CSLCOCSUDRAFT_38144
CVRCHLNCDRAFT_28225
APROF751_5711
OLUOSTLU_1854
OTAOT_ostta04g02660
BPGBathy06g04900
MISMICPUN_58063
MPPMICPUCDRAFT_57072
CMECYME_CMD093C
CCPCHC_T00000692001
MBRMONBRDRAFT_38173
SREPTSG_03222
PTIPHATRDRAFT_23292
FCYFRACYDRAFT_227121(GLDH)
TPSTHAPSDRAFT_268544
NGDNGA_2082000
AAFAURANDRAFT_70295
PIFPITG_05465
PSOJPHYSODRAFT_485337
SPARSPRG_04571
EHXEMIHUDRAFT_70809
 » show all
Reference
1
  Authors
Mapson, L.W. and Breslow, E.
  Title
Properties of partially purified L-galactono-gamma-lactone dehydrogenase.
  Journal
Biochem J 65:29 (1957)
Reference
2  [PMID:13126087]
  Authors
MAPSON LW, ISHERWOOD FA, CHEN YT.
  Title
Biological synthesis of L-ascorbic acid: the conversion of L-galactono-gamma-lactone into L-ascorbic acid by plant mitochondria.
  Journal
Biochem J 56:21-8 (1954)
DOI:10.1042/bj0560021
Reference
3  [PMID:13126085]
  Authors
ISHERWOOD FA, CHEN YT, MAPSON LW.
  Title
Synthesis of L-ascorbic acid in plants and animals.
  Journal
Biochem J 56:1-15 (1954)
DOI:10.1042/bj0560001
Reference
4  [PMID:7775377]
  Authors
Oba K, Ishikawa S, Nishikawa M, Mizuno H, Yamamoto T.
  Title
Purification and properties of L-galactono-gamma-lactone dehydrogenase, a key enzyme for ascorbic acid biosynthesis, from sweet potato roots.
  Journal
J Biochem (Tokyo) 117:120-4 (1995)
DOI:10.1093/oxfordjournals.jbchem.a124697
Reference
5  [PMID:9374475]
  Authors
Ostergaard J, Persiau G, Davey MW, Bauw G, Van Montagu M
  Title
Isolation of a cDNA coding for L-galactono-gamma-lactone dehydrogenase, an enzyme involved in the biosynthesis of ascorbic acid in plants. Purification, characterization, cDNA cloning, and expression in yeast.
  Journal
J Biol Chem 272:30009-16 (1997)
DOI:10.1074/jbc.272.48.30009
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 1.3.2.3
IUBMB Enzyme Nomenclature: 1.3.2.3
ExPASy - ENZYME nomenclature database: 1.3.2.3
BRENDA, the Enzyme Database: 1.3.2.3
CAS: 9029-02-1
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