Cloned (Comment) | Organism |
---|---|
gene GDH-A1, from the nulli-tetrasomic lines of CS, chromosome 5A, exon and intron structure among TaGLDH-A1, -B1 and -D1 homologues, sequence comparisons, recombinant ectopic expression in transgenic Nicotiana benthamiana using the viral vector based on pea early browning virus (PEBV), the GLDH homologue confers increased GLDH activity when ectopically expressed in tobacco, quantitative and semi-quantitative RT-PCR expression analysis, functional recombinant expression of GFP-tagged enzyme from BSMV:GFP virus in seedlings | Triticum aestivum |
gene GDH-B1, from the nulli-tetrasomic lines of CS, chromosome 5B, exon and intron structure among TaGLDH-A1, -B1 and -D1 homologues, sequence comparisons, recombinant ectopic expression in transgenic Nicotiana benthamiana using the viral vector based on pea early browning virus (PEBV), the GLDH homologue confers increased GLDH activity when ectopically expressed in tobacco, quantitative and semi-quantitative RT-PCR expression analysis, functional recombinant expression of GFP-tagged enzyme from BSMV:GFP virus in seedlings | Triticum aestivum |
gene GDH-D1, from the nulli-tetrasomic lines of CS, chromosome 5D, exon and intron structure among TaGLDH-A1, -B1 and -D1 homologues, sequence comparisons, recombinant ectopic expression in transgenic Nicotiana benthamiana using the viral vector based on pea early browning virus (PEBV), the GLDH homologue confers increased GLDH activity when ectopically expressed in tobacco, quantitative and semi-quantitative RT-PCR expression analysis, functional recombinant expression of GFP-tagged enzyme from BSMV:GFP virus in seedlings | Triticum aestivum |
Protein Variants | Comment | Organism |
---|---|---|
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 | Triticum aestivum |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.061 | - |
L-galactono-1,4-lactone | recombinant wild-type TaGLDH-A1a variant, pH 8.0, temperature not specified in the publication | Triticum aestivum | |
0.181 | - |
L-galactono-1,4-lactone | recombinant mutant TaGLDH-A1b variant, pH 8.0, temperature not specified in the publication | Triticum aestivum |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
mitochondrion | the enzyme contains a putative mitochondrial targeting signal peptide | Triticum aestivum | 5739 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-galactono-1,4-lactone + 4 ferricytochrome c | Triticum aestivum | overall reaction | L-dehydroascorbate + 4 ferrocytochrome c + 4 H+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Triticum aestivum | A0A1B1X3I2 | var. Xiaoyan 54, CS, and NT | - |
Triticum aestivum | W5FJN8 | var. Xiaoyan 54, CS, and NT | - |
Triticum aestivum | W5FUB4 | var. Xiaoyan 54, CS, and NT | - |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
leaf | - |
Triticum aestivum | - |
additional information | enzyme expression pattern, overview | Triticum aestivum | - |
root | low enzyme expression | Triticum aestivum | - |
seedling | - |
Triticum aestivum | - |
spikelet | young and mature | Triticum aestivum | - |
stem | low enzyme expression | Triticum aestivum | - |
stoma | - |
Triticum aestivum | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-galactono-1,4-lactone + 4 ferricytochrome c | overall reaction | Triticum aestivum | L-dehydroascorbate + 4 ferrocytochrome c + 4 H+ | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 66100, about, preprotein with putative mitochondrial targeting signal peptide, sequence calculation, x * 57500, about, mature protein without putative mitochondrial targeting signal peptide, sequence calculation | Triticum aestivum |
Synonyms | Comment | Organism |
---|---|---|
GLDH | - |
Triticum aestivum |
GLDH-A1 | - |
Triticum aestivum |
GLDH-B1 | - |
Triticum aestivum |
GLDH-D1 | - |
Triticum aestivum |
L-galactono-1,4-lactone dehydrogenase | - |
Triticum aestivum |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Triticum aestivum |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
cytochrome c | - |
Triticum aestivum | |
FAD | - |
Triticum aestivum |
Organism | Comment | Expression |
---|---|---|
Triticum aestivum | exogenous application of L-galactono-1,4-lactone can substantially stimulate ascorbic acid biosynthesis in plant tissues | up |
General Information | Comment | Organism |
---|---|---|
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 | Triticum aestivum |
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 | Triticum aestivum |