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Information on EC 1.3.2.3 - L-galactonolactone dehydrogenase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9SU56
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1.3.2.3 L-galactonolactone dehydrogenaseIUBMB Comments
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 . 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 . FAD, NAD+, NADP+ and O2 (cf. EC 1.3.3.12, L-galactonolactone oxidase) cannot act as electron acceptor .
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Word Map
- 1.3.2.3
- asa
- l-galactose
- dehydroascorbate
- monodehydroascorbate
-
l-galactose-1-phosphate
- l-gulono-1,4-lactone
- galdh
- gdp-d-mannose
- mdhar
- gdp-l-galactose
- aldonolactone
- d-galacturonate
-
ascorbate-glutathione
-
smirnoff-wheeler
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
l-galactono-1,4-lactone dehydrogenase, galldh, l-galactono-gamma-lactone dehydrogenase, ferricytochrome c oxidoreductase, l-galldh, gldhase, galactono-1,4-lactone dehydrogenase, galactonolactone dehydrogenase, gldase, l-galactonolactone dehydrogenase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dehydrogenase, galactonolactone
-
-
-
-
L-galactono-1,4-lactone dehydrogenase
-
-
L-galactono-gamma-lactone dehydrogenase
L-galactono-gamma-lactone dehydrogenase
-
-
-
-
L-galactono-gamma-lactone dehydrogenase
-
catalyzes the final step in the biosynthesis of vitamin C in plants
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
reduction
oxidation
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-
-
-
reduction
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-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
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-, -
SYSTEMATIC NAME
IUBMB Comments
L-galactono-1,4-lactone:ferricytochrome-c oxidoreductase
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].
CAS REGISTRY NUMBER
COMMENTARY
9029-02-1
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-galactono-1,4-lactone + 4 ferricytochrome c
L-dehydroascorbate + 4 ferrocytochrome c + 4 H+
overall reaction
-
-
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c + H+
-
-
-
?
L-galactono-1,4-lactone + 1,4-benzoquinone
L-ascorbate + reduced 1,4-benzoquinone
-
-
-
-
?
L-galactono-1,4-lactone + cytochrome c
L-ascorbate + reduced cytochrome c
-
-
-
-
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
-
-
-
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c + H+
-
-
-
-
?
L-galactono-1,4-lactone + phenazine methosulfate
L-ascorbate + reduced phenazine methosulfate
-
-
-
-
?
L-gulono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
-
-
-
?
L-galactono-1,4-lactone + 2 ferricytochrome c
L-ascorbate + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
L-galactono-1,4-lactone + 2 ferricytochrome c
L-ascorbate + 2 ferrocytochrome c + 2 H+
-
final enzyme in synthesis of ascorbic acid
-
-
?
additional information
?
-
-
D-galactono-1,4-lactone, D-gulono-1,4-lactone, L-mannono-1,4-lactone, and D-galacturonic acid are no substrates, molecular oxygen can not serve as efficient electron acceptor for the mutant enzymes
-
-
?
additional information
?
-
-
a kinetic and thermodynamic study of the GALDH-cytochrome c interaction and electron-transfer reactions by using laser-flash photolysis and stopped-flow kinetic analysis as well as isothermal titration calorimetry (ITC) and NMR spectroscopy are performed. Results show a transient, highly dynamic GALDH- cytochrome c interaction, similar for all partner redox states
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-galactono-1,4-lactone + 4 ferricytochrome c
L-dehydroascorbate + 4 ferrocytochrome c + 4 H+
overall reaction
-
-
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c + H+
-
-
-
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c + H+
-
-
-
-
?
L-galactono-1,4-lactone + 2 ferricytochrome c
L-ascorbate + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
L-galactono-1,4-lactone + 2 ferricytochrome c
L-ascorbate + 2 ferrocytochrome c + 2 H+
-
final enzyme in synthesis of ascorbic acid
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
H2O2
GALDH is inactivated by hydrogen peroxide due to selective oxidation of cysteine 340, located in the cap domain
additional information
-
no substrate inhibition with L-gulono-1,4-lactone at concentrations up to 100 mM, D-galactono-1,4-lactone, D-gulono-1,4-lactone, L-mannono-1,4-lactone, and D-galacturonic acid do not inhibit the oxidation of L-galactono-1,4-lactone, no specific inhibition by cations or anions is observed
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additional information
-
the transcript levels of L-galactono-1,4-lactone dehydrogenase is down-regulated in the dark
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.28
1,4-benzoquinone
-
wild type enzyme, in the presence of L-galactono-1,4-lactone, in 50 mM sodium phosphate (pH 8.8), at 25°C
0.034
cytochrome c
-
wild type enzyme, in the presence of L-galactono-1,4-lactone, in 50 mM sodium phosphate (pH 8.8), at 25°C
0.026
phenazine methosulfate
-
wild type enzyme, in the presence of L-galactono-1,4-lactone, in 50 mM sodium phosphate (pH 8.8), at 25°C
0.12
L-galactono-1,4-lactone
-
mutant enzyme L56H, in the presence of cytochrome c, in 50 mM sodium phosphate (pH 8.8), at 25°C
0.17
L-galactono-1,4-lactone
-
wild type enzyme, in the presence of cytochrome c, in 50 mM sodium phosphate (pH 8.8), at 25°C
0.32
L-galactono-1,4-lactone
-
mutant enzyme L56I, in the presence of cytochrome c, in 50 mM sodium phosphate (pH 8.8), at 25°C
0.56
L-galactono-1,4-lactone
-
mutant enzyme L56F in the presence of cytochrome c, in 50 mM sodium phosphate (pH 8.8), at 25°C
0.99
L-galactono-1,4-lactone
-
mutant enzyme L56C, in the presence of cytochrome c, in 50 mM sodium phosphate (pH 8.8), at 25°C
1.7
L-galactono-1,4-lactone
-
mutant enzyme L56IA in the presence of cytochrome c, in 50 mM sodium phosphate (pH 8.8), at 25°C
13.1
L-gulono-1,4-lactone
-
wild type enzyme, in the presence of cytochrome c, in 50 mM sodium phosphate (pH 8.8), at 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
108
1,4-benzoquinone
-
in the presence of L-galactono-1,4-lactone, in 50 mM sodium phosphate (pH 8.8), at 25°C
151
cytochrome c
-
in the presence of L-galactono-1,4-lactone, in 50 mM sodium phosphate (pH 8.8), at 25°C
64
phenazine methosulfate
-
in the presence of L-galactono-1,4-lactone, in 50 mM sodium phosphate (pH 8.8), at 25°C
32
L-galactono-1,4-lactone
-
mutant enzyme L56H, in the presence of cytochrome c, in 50 mM sodium phosphate (pH 8.8), at 25°C
45
L-galactono-1,4-lactone
-
mutant enzyme L56IA in the presence of cytochrome c, in 50 mM sodium phosphate (pH 8.8), at 25°C
76
L-galactono-1,4-lactone
-
mutant enzyme L56C, in the presence of cytochrome c, in 50 mM sodium phosphate (pH 8.8), at 25°C
126
L-galactono-1,4-lactone
-
mutant enzyme L56F in the presence of cytochrome c, in 50 mM sodium phosphate (pH 8.8), at 25°C
134
L-galactono-1,4-lactone
-
wild type enzyme, in the presence of cytochrome c, in 50 mM sodium phosphate (pH 8.8), at 25°C
240
L-galactono-1,4-lactone
-
mutant enzyme L56I, in the presence of cytochrome c, in 50 mM sodium phosphate (pH 8.8), at 25°C
4
L-gulono-1,4-lactone
-
in the presence of cytochrome c, in 50 mM sodium phosphate (pH 8.8), at 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
Arabidopsis ppr40-1 mutant which presents a strongly reduced electron flow through complex III, shows a higher activity of GLDH
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.8
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
AtGLDH mRNA level exhibits diurnal change. The level is low in the morning and increases during the day. Its level at 18.00 is about 2fold that in the morning at 6.00. Then the level decreases during the night until dawn of the next day. The diurnal change is regulated by light
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at high light, maximal extractable L-GalLDH activity is twice that measured in low light leaves under the same conditions, similarly, intermediate light leaves have 60% higher L-GalLDH activities than low light leaves, however abundance of L-GalLDH mRNA is similar for all light treatments
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GLDH behaves as an integral protein of the inner membrane facing the intermembrane space
additional information
in a mutant ndufs4 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 4 of Arabidopsis thaliana Col-0, the enzyme is located in the 400 and 450 kDa carbonic anhydrase-containing complexes accumulating in the ndufs4 mutant
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
the enzyme catalyzes the last step of ascorbate synthesis by oxidising L-galactone-1,4-lactone to ascorbate and transferring two electrons to cytochrome c
physiological function
the enzyme can play two distinct roles during complex I assembly. First, it can play a structural or stabilizing role for specific assembly intermediates. Second, it can indirectly be essential through providing the ascorbate that might be required during the assembly process. Enzyme GLDH is not required for the early stages of complex I assembly, but it is important for at least one step of the assembly process (transition from the 200 kDa intermediate to the 400 kDa intermediate), it is associated with some assembly intermediates, but it is absent from the mature complex
physiological function
-
the chlorophyll fluorescence parameters are significantly higher in enzyme-overexpressing mutants than that in wild type after 14 day high light. The degradation of photosynthetic pigment in wild type is more severe than that in the mutant. GLDH-236OE accumulates more ascorbate, anthocyanins, flavonoids, and phenolics, while wild type accumulates more reactive oxygen species during high light
malfunction
analysis of the vtc2-1 mutant shows that complex I assembly is not affected in this mutant, while it is affected in the mutant ndufs4 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 4 of Arabidopsis thaliana Col-0, in ndufs4, complex I is not assembled and GLDH is not present in any intermediate larger than 450 kDa. This suggests that the 450 kDa intermediate is a precursor of complex I. Very low amounts of complex I and other assembly intermediates in the gldh mutant, suggesting that the assembly of complex I is not completely arrested, but it is severely impaired in the absence of GLDH
malfunction
homozygous Arabidopsis thaliana mutant gldhRNAi3-11 plants show approximately 40% of the GLDH activity of wild-type controls and are viable under standard laboratory conditions. Mutant gldhRNAi3-11 plants show about 20% decrease in the contents of reduced ascorbic acid and total ascorbic acid. Partial suppression of GLDH activity confers significant reduction in leaf water loss through decreasing stomatal aperture size in Arabidopsis thaliana, phenotype, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GLDH_ARATH
610
0
68555
Swiss-Prot
Mitochondrion (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
420000
-
three distinct GLDH containing protein complexes of 850, 470, and 420 kDa are discovered using a newly developed in gel GLDH activity assay and immunoblotting. Subunits of the novel 470 and 420 kDa complexes are identified by mass spectrometry. Like the 850-kDa complex, they also include complex I subunits
470000
-
three distinct GLDH containing protein complexes of 850, 470, and 420 kDa are discovered using a newly developed in gel GLDH activity assay and immunoblotting. Subunits of the novel 470 and 420 kDa complexes are identified by mass spectrometry. Like the 850-kDa complex, they also include complex I subunits
850000
-
three distinct GLDH containing protein complexes of 850, 470, and 420 kDa are discovered using a newly developed in gel GLDH activity assay and immunoblotting. The 850-kDa complex represents the known smaller version of mitochondrial complex I. GLDH is shown to be attached to the membrane arm of the 850-kDa complex I
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
GLDH forms part of the 850-kDa complex I and part of a rotein complexes of 470 and 420 kDa
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C340A
mutant, insensitive toward thiol oxidation, exhibits poor affinity for L-galactono-1,4-lactone
C340S
mutant, insensitive toward thiol oxidation, exhibits poor affinity for L-galactono-1,4-lactone
E386A
-
mutant, catalytically far less efficient than wild-type GALDH, Glu386 is involved in productive substrate binding
E386D
-
mutant, catalytically far less efficient than wild-type GALDH, Glu386 is involved in productive substrate binding
L56H
-
less active than the wild type enzyme and releases its FAD cofactor more easily than wild type GALDH
L56I
-
the mutant displays a higher turnover rate with L-galactono-1,4-lactone than the wild type enzyme
R388A
-
inactive mutant, Arg388 is crucial for the stabilization of the anionic form of the reduced FAD cofactor
R388K
-
mutant, shows significant activity, Arg388 is crucial for the stabilization of the anionic form of the reduced FAD cofactor
additional information
additional information
analysis of the vtc2-1 mutant shows that complex I assembly is not affected in this mutant, while it is affected in the mutant ndufs4 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 4 of Arabidopsis thaliana Col-0, the enzyme is located in the 400 and 450 kDa carbonic anhydrase-containing complexes accumulating in the ndufs4 mutant. Very low amounts of complex I and other assembly intermediates in the gldh mutant, suggesting that the assembly of complex I is not completely arrested, but it is severely impaired in the absence of GLDH
additional information
homozygous Arabidopsis thaliana mutant (gldhRNAi3-11) plants with approximately 40% of the GLDH activity of wild-type controls are developed by RNA interference (three genotypes), and are viable under standard laboratory conditions. Mutant gldhRNAi3-11 plants show about 20% decrease in the contents of reduced ascorbic acid and total ascorbic acid. Partial suppression of GLDH activity in RNAi lines confers significant reduction in leaf water loss through decreasing stomatal aperture size in Arabidopsis thaliana, phenotype, overview
additional information
-
transgenic plant lines with altered levels of mitochondrial alternative oxidase protein have similar levels of L-GalLDH activity whether leaves are measured at low light, or after 4 h exposure to high light
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
52
-
the recombinant enzyme has a half-life of 20 min at 52°C, in the presence of excess FAD the half-life at 52°C is increased to 115 min
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, 50 mM sodium phosphate and 300 mM NaCl (pH 7.4), more than 12 months, 30-50% loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crude membrane extracts from Arabidopsis thaliana leaves and roots are prepared
Ni-NTA agarose column chromatography and Q-Sepharose column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene GLDH, quantitative real-time RT-PCR enzyme expression analysis
into a pET-His6 vector for expression in Escherichia coli BL21DE3 cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
relative mRNA expression levels of galactono-1,4-lactone dehydrogenase shows no difference between wild type and ppr40-1 mutant plants
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
despite limitations on L-GalL synthesis by regulation of early steps in the ascorbic acid synthesis pathway, the regulation of L-GalLDH activity via the interaction of light and respiratory controls is a crucial determinant of the overall ability of leaves to produce and accumulate ascorbic acid
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tamaoki, M.; Mukai, F.; Asai, N.; Nakajima, N.; Kubo, A.; Aono, M.; Saji, H.
Light-controlled expression of a gene encoding L-galactono-gamma-lactone dehydrogenase which affects ascorbate pool size in Arabidopsis thaliana
Plant Sci.
164
1111-1117
2003
Arabidopsis thaliana
-
Bartoli, C.G.; Yu, J.; Gomez, F.; Fernandez, L.; McIntosh, L.; Foyer, C.H.
Inter-relationships between light and respiration in the control of ascorbic acid synthesis and accumulation in Arabidopsis thaliana leaves
J. Exp. Bot.
57
1621-1631
2006
Arabidopsis thaliana
Leferink, N.G.; van den Berg, W.A.; van Berkel, W.J.
L-galactono-gamma-lactone dehydrogenase from Arabidopsis thaliana, a flavoprotein involved in vitamin C biosynthesis
FEBS J.
275
713-726
2008
Arabidopsis thaliana
Yabuta, Y.; Mieda, T.; Rapolu, M.; Nakamura, A.; Motoki, T.; Maruta, T.; Yoshimura, K.; Ishikawa, T.; Shigeoka, S.
Light regulation of ascorbate biosynthesis is dependent on the photosynthetic electron transport chain but independent of sugars in Arabidopsis
J. Exp. Bot.
58
2661-2671
2007
Arabidopsis thaliana
Leferink, N.G.; Jose, M.D.; van den Berg, W.A.; van Berkel, W.J.
Functional assignment of Glu386 and Arg388 in the active site of L-galactono-gamma-lactone dehydrogenase
FEBS Lett.
583
3199-3203
2009
Arabidopsis thaliana
Pineau, B.; Layoune, O.; Danon, A.; De Paepe, R.
L-galactono-1,4-lactone dehydrogenase is required for the accumulation of plant respiratory complex I
J. Biol. Chem.
283
32500-32505
2008
Arabidopsis thaliana (Q9SU56), Arabidopsis thaliana, Nicotiana sylvestris
Leferink, N.G.; van Duijn, E.; Barendregt, A.; Heck, A.J.; van Berkel, W.J.
Galactonolactone dehydrogenase requires a redox-sensitive thiol for optimal production of vitamin C
Plant Physiol.
150
596-605
2009
Arabidopsis thaliana (Q9SU56), Arabidopsis thaliana
Hervas, M.; Bashir, Q.; Leferink, N.G.; Ferreira, P.; Moreno-Beltran, B.; Westphal, A.H.; Diaz-Moreno, I.; Medina, M.; de la Rosa, M.A.; Ubbink, M.; Navarro, J.A.; van Berkel, W.J.
Communication between (L)-galactono-1,4-lactone dehydrogenase and cytochrome c
FEBS J.
280
1830-1840
2013
Arabidopsis thaliana
Schertl, P.; Sunderhaus, S.; Klodmann, J.; Grozeff, G.E.; Bartoli, C.G.; Braun, H.P.
L-galactono-1,4-lactone dehydrogenase (GLDH) forms part of three subcomplexes of mitochondrial complex I in Arabidopsis thaliana
J. Biol. Chem.
287
14412-14419
2012
Arabidopsis thaliana
Zsigmond, L.; Tomasskovics, B.; Deak, V.; Rigo, G.; Szabados, L.; Banhegyi, G.; Szarka, A.
Enhanced activity of galactono-1,4-lactone dehydrogenase and ascorbate-glutathione cycle in mitochondria from complex III deficient Arabidopsis
Plant Physiol. Biochem.
49
809-815
2011
Arabidopsis thaliana
Li, B.; Yang, Y.; Yu, C.; Li, S.; Chen, J.; Liu, X.; Qin, H.; Wang, D.
Partial suppression of L-galactono-1,4-lactone dehydrogenase causes significant reduction in leaf water loss through decreasing stomatal aperture size in Arabidopsis
Plant Growth Regul.
72
171-179
2014
Arabidopsis thaliana (Q9SU56), Arabidopsis thaliana Col-0 (Q9SU56)
-
Schimmeyer, J.; Bock, R.; Meyer, E.H.
L-Galactono-1,4-lactone dehydrogenase is an assembly factor of the membrane arm of mitochondrial complex I in Arabidopsis
Plant Mol. Biol.
90
117-126
2016
Arabidopsis thaliana (Q9SU56), Arabidopsis thaliana Col-0 (Q9SU56)
Zheng, X.; Zhang, X.; Wang, Y.; Cai, M.; Li, M.; Zhang, T.; Peng, C.
Identification of a GLDH-overexpressing arabidopsis mutant and its responses to high-light stress
Photosynthetica
57
332-341
2019
Arabidopsis thaliana
-
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