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D-arabinono-1,4-lactone + ferrocytochrome c + H+
?
-
-
-
-
?
L-galactono-1,4-lactone + 1,4-benzoquinone
L-ascorbate + reduced 1,4-benzoquinone
-
-
-
-
?
L-galactono-1,4-lactone + 2 ferricytochrome c
L-ascorbate + 2 ferrocytochrome c + 2 H+
L-galactono-1,4-lactone + 4 ferricytochrome c
L-dehydroascorbate + 4 ferrocytochrome c + 4 H+
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-gulono-gamma-lactone + ferricytochrome
D-ascorbate + ferricytochrome c
L-mannono-gamma-lactone + ferricytochrome c
D-ascorbate + ferricytochrome c
-
18% activity of that with L-galactono-gamma-lactone
-
-
?
additional information
?
-
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
-
-
?
L-galactono-1,4-lactone + 2 ferricytochrome c
L-ascorbate + 2 ferrocytochrome c + 2 H+
-
terminal step in L-ascorbic acid biosynthesis
-
?
L-galactono-1,4-lactone + 2 ferricytochrome c
L-ascorbate + 2 ferrocytochrome c + 2 H+
terminal step in L-ascorbic acid biosynthesis
-
?
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+
-
terminal step in L-ascorbic acid biosynthesis
-
?
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+
-
-
-
?
L-galactono-1,4-lactone + 2 ferricytochrome c
L-ascorbate + 2 ferrocytochrome c + 2 H+
-
ascorbic acid biosynthesis precursors are L-galactono-gamma-lactone and L-gulono-gamma-lactone
-
?
L-galactono-1,4-lactone + 2 ferricytochrome c
L-ascorbate + 2 ferrocytochrome c + 2 H+
-
activity is inducible by addition of D-glucose, D-galactose or L-gulono-gamma-lactone in vivo
-
?
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+
-
terminal step in L-ascorbic acid biosynthesis
-
?
L-galactono-1,4-lactone + 4 ferricytochrome c
L-dehydroascorbate + 4 ferrocytochrome c + 4 H+
overall reaction
-
-
?
L-galactono-1,4-lactone + 4 ferricytochrome c
L-dehydroascorbate + 4 ferrocytochrome c + 4 H+
overall reaction
-
-
?
L-galactono-1,4-lactone + 4 ferricytochrome c
L-dehydroascorbate + 4 ferrocytochrome c + 4 H+
overall reaction
-
-
?
L-galactono-1,4-lactone + 4 ferricytochrome c
L-dehydroascorbate + 4 ferrocytochrome c + 4 H+
overall reaction
-
-
?
L-galactono-1,4-lactone + 4 ferricytochrome c
L-dehydroascorbate + 4 ferrocytochrome c + 4 H+
overall reaction
-
-
?
L-galactono-1,4-lactone + 4 ferricytochrome c
L-dehydroascorbate + 4 ferrocytochrome c + 4 H+
overall reaction
-
-
?
L-galactono-1,4-lactone + cytochrome c
L-ascorbate + reduced cytochrome c
-
-
-
-
?
L-galactono-1,4-lactone + cytochrome c
L-ascorbate + reduced cytochrome c
-
-
-
-
?
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
specific for cytochrome c as electron acceptor
-
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
native and recombinant from yeast
-
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
reduces only phenazine methosulfate and cytochrome c
-
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
specific for L-galactono-gamma-lactone
-
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
specific for L-galactono-gamma-lactone
-
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
final enzyme in synthesis of ascorbic acid, expression is regulated by light
-
-
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
-
-
-
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
infiltration of the substrate through the fruit petiole at the small green and turning stage results in a 50% increase in total L-ascorbate content, but in no differences in enzyme activity and expression
-
-
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
-
-
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
specific for L-galactono-gamma-lactone
-
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
-
-
-
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
-
-
-
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
final enzyme in synthesis of ascorbic acid
-
-
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
-
-
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
native and recombinant enzyme
-
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
specific for L-galactono-gamma-lactone
-
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
-
-
-
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
specific for cytochrome c as electron acceptor
-
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
final enzyme in synthesis of ascorbic acid
-
-
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
-
-
-
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
final enzyme in synthesis of ascorbic acid. L-Galactono-gamma-lactone dehydrogenase and vitamin C content in fresh-cut potatoes stored under controlled atmospheres: fresh-cutting provoces an increase in enzyme activity in potato strips in all atmospheres tested. Highest induction, 15.5fold, is observed in strips stored in air
-
-
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
the pI 4.3 enzyme form is much more effective than that of potato tuber pI 5 enzyme to catalyze the synthesis of ascorbic acid
-
-
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
reduces only phenazine methosulfate and cytochrome c
-
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
specific for L-galactono-gamma-lactone
-
?
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 + ferricytochrome c
L-ascorbate + ferrocytochrome c + H+
-
-
-
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c + H+
-
-
-
-
r
L-gulono-gamma-lactone + ferricytochrome
D-ascorbate + ferricytochrome c
-
very low activity
-
-
?
L-gulono-gamma-lactone + ferricytochrome
D-ascorbate + ferricytochrome c
-
recombinant enzyme: 7% activity of the activity with L-galactono-gamma-lactone
-
-
?
L-gulono-gamma-lactone + ferricytochrome
D-ascorbate + ferricytochrome c
-
23% activity of that with L-galactono-gamma-lactone
-
-
?
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
-
-
?
additional information
?
-
-
incubation of leaf discs in a L-galactonolactone solution leads to a rapid 2 to 3fold increase in the L-ascorbate content in both GLDH-transformed and non-transformed plants in the same manner
-
-
?
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L-galactono-1,4-lactone + 2 ferricytochrome c
L-ascorbate + 2 ferrocytochrome c + 2 H+
L-galactono-1,4-lactone + 4 ferricytochrome c
L-dehydroascorbate + 4 ferrocytochrome c + 4 H+
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+
additional information
?
-
-
incubation of leaf discs in a L-galactonolactone solution leads to a rapid 2 to 3fold increase in the L-ascorbate content in both GLDH-transformed and non-transformed plants in the same manner
-
-
?
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
-
-
?
L-galactono-1,4-lactone + 2 ferricytochrome c
L-ascorbate + 2 ferrocytochrome c + 2 H+
-
terminal step in L-ascorbic acid biosynthesis
-
?
L-galactono-1,4-lactone + 2 ferricytochrome c
L-ascorbate + 2 ferrocytochrome c + 2 H+
terminal step in L-ascorbic acid biosynthesis
-
?
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+
-
terminal step in L-ascorbic acid biosynthesis
-
?
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+
-
-
-
?
L-galactono-1,4-lactone + 2 ferricytochrome c
L-ascorbate + 2 ferrocytochrome c + 2 H+
-
ascorbic acid biosynthesis precursors are L-galactono-gamma-lactone and L-gulono-gamma-lactone
-
?
L-galactono-1,4-lactone + 2 ferricytochrome c
L-ascorbate + 2 ferrocytochrome c + 2 H+
-
activity is inducible by addition of D-glucose, D-galactose or L-gulono-gamma-lactone in vivo
-
?
L-galactono-1,4-lactone + 2 ferricytochrome c
L-ascorbate + 2 ferrocytochrome c + 2 H+
-
terminal step in L-ascorbic acid biosynthesis
-
?
L-galactono-1,4-lactone + 4 ferricytochrome c
L-dehydroascorbate + 4 ferrocytochrome c + 4 H+
overall reaction
-
-
?
L-galactono-1,4-lactone + 4 ferricytochrome c
L-dehydroascorbate + 4 ferrocytochrome c + 4 H+
overall reaction
-
-
?
L-galactono-1,4-lactone + 4 ferricytochrome c
L-dehydroascorbate + 4 ferrocytochrome c + 4 H+
overall reaction
-
-
?
L-galactono-1,4-lactone + 4 ferricytochrome c
L-dehydroascorbate + 4 ferrocytochrome c + 4 H+
overall reaction
-
-
?
L-galactono-1,4-lactone + 4 ferricytochrome c
L-dehydroascorbate + 4 ferrocytochrome c + 4 H+
overall reaction
-
-
?
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
final enzyme in synthesis of ascorbic acid, expression is regulated by light
-
-
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
final enzyme in synthesis of ascorbic acid
-
-
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
final enzyme in synthesis of ascorbic acid
-
-
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c
-
final enzyme in synthesis of ascorbic acid. L-Galactono-gamma-lactone dehydrogenase and vitamin C content in fresh-cut potatoes stored under controlled atmospheres: fresh-cutting provoces an increase in enzyme activity in potato strips in all atmospheres tested. Highest induction, 15.5fold, is observed in strips stored in air
-
-
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c + H+
-
-
-
-
?
L-galactono-1,4-lactone + ferricytochrome c
L-ascorbate + ferrocytochrome c + H+
-
-
-
?
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malfunction
-
a change in ascorbic acid content caused by silencing or overexpressing GLDH, respectively, in rice plants leads to a changed plant growth and seed set
malfunction
-
GLDH-suppressed transgenic rices, GI-1 and GI-2, which have constitutively low (between 30% and 50%) leaf ascorbic acid content compared with the wild-type plants, exhibit a significantly reduced tiller number
malfunction
-
overexpression of L-galactono-gamma-lactone dehydrogenase increases vitamin C, total phenolics and antioxidant activity in lettuce through bio-fortification
malfunction
transgenic tobacco plants overexpressing GalLDH show an enhanced GalLDH transcript levels, GalLDH activities, and L-ascorbic acid accumulation as compared to wild-type plants. Abiotic stress tolerance is enhanced in transgenic plants compared to wild-type plants
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
ascorbic acid deficiency in L-GalLDH-suppressed transgenic rice, GI-1 and GI-2, which have constitutively low (between 30% and 50%) leaf and grain ascorbic acid content compared with the wild-type, leads to increased grain chalkiness in the transgenic rice. Deficiency of ascorbic acid also results in a higher lipid peroxidation and H2O2 content, accompanied by a lower hydroxyl radical scavenging rate, total antioxidant capacity and photosynthetic ability. Changes of the enzyme activities and gene transcript abundances related to starch synthesis are also observed in GI-1 and GI-2 grains. Phenotypes, detailed overview
malfunction
decreasing TaGLDH expression in wheat significantly reduces GLDH activity and ascorbic acid content, but in the leaf tissues undergoing TaGLDH silencing, the reductions of total and reduced ascorbic acid contents are considerably below the decreases in TaGLDH expression and GLDH activity. Association of the mutant TaGLDH-A1b variant with enhanced tolerance to water deficiency stress, overview
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
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
-
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
-
metabolism
-
GLDH catalyzes the last step of L-ascorbate, AsA, biosynthesis in plants, but the upstream genes in the AsA biosynthetic pathway are responsible for enhancing the AsA content in plants, regulation, overview
metabolism
L-galactono-1,4-lactone dehydrogenase is one of the enzymes of the Smirnoff-Wheeler's branch of ascorbic acid biosynthetic pathway, overview
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
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
GalLDH is a key modulation point of the physiology of pepper plants. GalLDH might have a pivotal role which allows the interaction with several neighboring respiratory oxidases. GalLDH is an unstable protein, and this contributes to maintain and even increase the ascorbate levels, it has also an important role during development and fruit ripening. Respiration can control ascorbate synthesis in plants and for its optimum biosynthesis is necessary an electron flux through the complex I of the mitochondrial electron transport chain. In vitro experiments on GalLDH activity in the presence of GSH show, the ascorbate levels in pepper fruits also depend on the redox chemical surrounding of the GalLDH, since this enzyme activity is inhibited by GSH
physiological function
in higher plants, L-galactono-1,4-lactone dehydrogenase (GLDH) plays important roles in ascorbic acid biosynthesis and assembly of respiration complex I. GLDH is essential for the final steps of biosynthesis of ascorbic acid, a vital and abundant antioxidant, through the D-mannose/L-galactose pathway. GLDH activities are required for the normal growth and development of plant cells and organs and their efficient response to adverse environmental factors. The enzyme is important for regulation of water stress via the ascorbic acid level in guard cells, because H2O2 accumulation in the guard cells is vital for stomata closing, and ascorbic acid, being the most abundant water-soluble antioxidant in plant cells, plays a critical role in regulating cellular level of H2O2
physiological function
L-galactono-1,4-lactone dehydrogenase catalyzes the ultimate step of ascorbic acid biosynthesis in higher plants. L-GalLDH is attached to complex I of the mitochondrial electron transport chain, which uses L-galactono-1,4-lactone as an electron donor to reduce cytochrome c between complexes III and IV, while l-GalLis converted into ascorbic acid. Role of L-GalLDH in the control of cell, organ, and plant growth
physiological function
L-galactono-1,4-lactone dehydrogenase catalyzes the ultimate step of ascorbic acid biosynthesis in higher plants. L-GalLDH is attached to complex I of the mitochondrial electron transport chain,which uses L-galactono-1,4-lactone as an electron donor to reduce cytochrome c between complexes III and IV, while l-GalLis converted into ascorbic acid. Role of L-GalLDH in the control of cell, organ, and plant growth
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
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
-
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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
GLDH-236OE
-
homozygote mutant with enzyme overexpression
L56A
-
less active than the wild type enzyme
L56C
-
less active than the wild type enzyme
L56F
-
less active than the wild type enzyme
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
-
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
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
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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
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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
transgenic tobacco BY-2 cells, overexpression of levels of GalLDH, GalLDH mRNA in S-type cells is much higher than in wild-type and EM-type cells, moreover, resistance to methyl viologen
additional information
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transgenic tobacco BY-2 cells, overexpression of levels of GalLDH, GalLDH mRNA in S-type cells is much higher than in wild-type and EM-type cells, moreover, resistance to methyl viologen
additional information
significant differences in grain chalkiness degree are observed between mutant GI and WT. GI-1 kernels display an increased (25.78%) grain chalkiness degree, as well as GI-2 kernels (16.33%), but wild-type kernels display 9.37%. In addition, the GI-1 and GI-2 grains show a lower starch content when compared with wild-type , which is decreased to 51.06% and 82.64% of the wild-type level, respectively. Similarly, significant lower amylose content is also observed in GI-1 and GI-2 grains (3.08% and 3.90%) when compared with wild-type (5.12%). As chalkiness may be affected by grain size, grain length, grain width, and grain length-to-width ratio (GLWR) of GI, and wild-type are measured, with the results showing that no significant difference between GI-1, GI-2 and wild-type in grain length, grain width, or GLWR is observed. Phenotypes, overview
additional information
significant differences in grain chalkiness degree are observed between mutant GI and WT. GI-1 kernels display an increased (25.78%) grain chalkiness degree, as well as GI-2 kernels (16.33%), but wild-type kernels display 9.37%. In addition, the GI-1 and GI-2 grains show a lower starch content when compared with wild-type , which is decreased to 51.06% and 82.64% of the wild-type level, respectively. Similarly, significant lower amylose content is also observed in GI-1 and GI-2 grains (3.08% and 3.90%) when compared with wild-type (5.12%). As chalkiness may be affected by grain size, grain length, grain width, and grain length-to-width ratio (GLWR) of GI, and wild-type are measured, with the results showing that no significant difference between GI-1, GI-2 and wild-type in grain length, grain width, or GLWR is observed. Phenotypes, overview
additional information
significant differences in grain chalkiness degree are observed between mutant GI and WT. GI-1 kernels display an increased (25.78%) grain chalkiness degree, as well as GI-2 kernels (16.33%), but wild-type kernels display 9.37%. In addition, the GI-1 and GI-2 grains show a lower starch content when compared with wild-type, which is decreased to 51.06% and 82.64% of the wild-type level, respectively. Similarly, significant lower amylose content is also observed in GI-1 and GI-2 grains (3.08% and 3.90%) when compared with wild-type (5.12%). As chalkiness may be affected by grain size, grain length, grain width, and grain length-to-width ratio (GLWR) of GI, and wild-type are measured, with the results showing that no significant difference between GI-1, GI-2 and wild-type in grain length, grain width, or GLWR is observed. Phenotypes, overview
additional information
significant differences in grain chalkiness degree are observed between mutant GI and WT. GI-1 kernels display an increased (25.78%) grain chalkiness degree, as well as GI-2 kernels (16.33%), but wild-type kernels display 9.37%. In addition, the GI-1 and GI-2 grains show a lower starch content when compared with wild-type, which is decreased to 51.06% and 82.64% of the wild-type level, respectively. Similarly, significant lower amylose content is also observed in GI-1 and GI-2 grains (3.08% and 3.90%) when compared with wild-type (5.12%). As chalkiness may be affected by grain size, grain length, grain width, and grain length-to-width ratio (GLWR) of GI, and wild-type are measured, with the results showing that no significant difference between GI-1, GI-2 and wild-type in grain length, grain width, or GLWR is observed. Phenotypes, overview
additional information
mutant variant TaGLDHA1b differs from wild-type allele TaGLDH-A1a by an in-frame deletion of three nucleotides. TaGLDHA1b is biochemically less active than TaGLDH-A1a, and the total GLDH activity levels are generally lower in the cultivars carrying TaGLDH-A1b relative to those with TaGLDH-A1a. Mutant TaGLDHA1b cultivars show stronger water deficiency tolerance than TaGLDH-A1a cultivars, and TaGLDH-A1b co-segregate with decreased leaf water loss in a F2 population. TaGLDH-A1b cultivars generally exhibit smaller leaf stomatal aperture than TaGLDH-A1a varieties in control or water deficiency environments
additional information
mutant variant TaGLDHA1b differs from wild-type allele TaGLDH-A1a by an in-frame deletion of three nucleotides. TaGLDHA1b is biochemically less active than TaGLDH-A1a, and the total GLDH activity levels are generally lower in the cultivars carrying TaGLDH-A1b relative to those with TaGLDH-A1a. Mutant TaGLDHA1b cultivars show stronger water deficiency tolerance than TaGLDH-A1a cultivars, and TaGLDH-A1b co-segregate with decreased leaf water loss in a F2 population. TaGLDH-A1b cultivars generally exhibit smaller leaf stomatal aperture than TaGLDH-A1a varieties in control or water deficiency environments
additional information
mutant variant TaGLDHA1b differs from wild-type allele TaGLDH-A1a by an in-frame deletion of three nucleotides. TaGLDHA1b is biochemically less active than TaGLDH-A1a, and the total GLDH activity levels are generally lower in the cultivars carrying TaGLDH-A1b relative to those with TaGLDH-A1a. Mutant TaGLDHA1b cultivars show stronger water deficiency tolerance than TaGLDH-A1a cultivars, and TaGLDH-A1b co-segregate with decreased leaf water loss in a F2 population. TaGLDH-A1b cultivars generally exhibit smaller leaf stomatal aperture than TaGLDH-A1a varieties in control or water deficiency environments
additional information
-
mutant variant TaGLDHA1b differs from wild-type allele TaGLDH-A1a by an in-frame deletion of three nucleotides. TaGLDHA1b is biochemically less active than TaGLDH-A1a, and the total GLDH activity levels are generally lower in the cultivars carrying TaGLDH-A1b relative to those with TaGLDH-A1a. Mutant TaGLDHA1b cultivars show stronger water deficiency tolerance than TaGLDH-A1a cultivars, and TaGLDH-A1b co-segregate with decreased leaf water loss in a F2 population. TaGLDH-A1b cultivars generally exhibit smaller leaf stomatal aperture than TaGLDH-A1a varieties in control or water deficiency environments
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