1.3.2.3: L-galactonolactone dehydrogenase
This is an abbreviated version!
For detailed information about L-galactonolactone dehydrogenase, go to the full flat file.
Word Map on EC 1.3.2.3
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1.3.2.3
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asa
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l-galactose
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dehydroascorbate
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monodehydroascorbate
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l-galactose-1-phosphate
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l-gulono-1,4-lactone
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galdh
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gdp-d-mannose
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mdhar
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gdp-l-galactose
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aldonolactone
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d-galacturonate
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ascorbate-glutathione
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smirnoff-wheeler
- 1.3.2.3
- asa
- l-galactose
- dehydroascorbate
- monodehydroascorbate
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l-galactose-1-phosphate
- l-gulono-1,4-lactone
- galdh
- gdp-d-mannose
- mdhar
- gdp-l-galactose
- aldonolactone
- d-galacturonate
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ascorbate-glutathione
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smirnoff-wheeler
Reaction
Synonyms
dehydrogenase, galactonolactone, ferricytochrome c oxidoreductase, galactono-1,4-lactone dehydrogenase, galactonolactone dehydrogenase, GALDH, GalL dehydrogenase, GalLDH, GLDase, GLDH, GLDH-A1, GLDH-B1, GLDH-D1, GLDH1, GLDHase, L-galactone-1,4-lactone dehydrogenase, L-galactono-1, 4-lactone dehydrogenase, L-galactono-1,4-lactone dehydrogenase, L-galactono-gamma-lactone dehydrogenase, L-GalLDH, L-GalLDH1, L-GalLDH2, LsL-GalLDH, RrGalLDH
ECTree
1.3.2.3 L-galactonolactone dehydrogenaseAdvanced search results
results (
results (Engineering
Engineering on EC 1.3.2.3 - L-galactonolactone dehydrogenase
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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
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mutant, catalytically far less efficient than wild-type GALDH, Glu386 is involved in productive substrate binding
E386D
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mutant, catalytically far less efficient than wild-type GALDH, Glu386 is involved in productive substrate binding
L56H
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less active than the wild type enzyme and releases its FAD cofactor more easily than wild type GALDH
L56I
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the mutant displays a higher turnover rate with L-galactono-1,4-lactone than the wild type enzyme
R388A
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inactive mutant, Arg388 is crucial for the stabilization of the anionic form of the reduced FAD cofactor
R388K
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mutant, shows significant activity, Arg388 is crucial for the stabilization of the anionic form of the reduced FAD cofactor
additional information
additional information
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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
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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
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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
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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
