3.7.1.1: oxaloacetase
This is an abbreviated version!
For detailed information about oxaloacetase, go to the full flat file.
Word Map on EC 3.7.1.1
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3.7.1.1
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oxalic
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niger
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sclerotiorum
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sclerotinia
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mycelia
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glyoxylate
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food industry
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palustris
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agriculture
- 3.7.1.1
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oxalic
- niger
- sclerotiorum
- sclerotinia
- mycelia
- glyoxylate
- food industry
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palustris
- agriculture
Reaction
Synonyms
(2R,3S)-dimethylmalate lyase, An07g08390, BbOAH, DMML, FpOAH, OAH, OAH-active petal death protein, OAH-like protein, OXA, oxalacetase, oxalacetate acetylhydrolase, oxalacetic hydrolase, oxaloacetase, oxaloacetate acethylhydrolase, oxaloacetate acetylhydrolase, oxaloacetate hydrolase
ECTree
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General Information
General Information on EC 3.7.1.1 - oxaloacetase
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evolution
oxalacetate acetylhydrolase is a member of the phosphoenolpyruvate mutase/isocitrate lyase superfamily
malfunction
metabolism
physiological function
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deletion of gene Pc22g28430 in Penicillium chrysogenum leads to complete elimination of oxalate production, whilst improving yields of the cephalosporin precursor adipoyl-6-aminopenicillinic acid
malfunction
knockout of the oah gene in Cryphonectria parasitica, the chestnut blight fungus, reduces the ability of the fungus to form cankers on chestnut trees
malfunction
gene deletion DELTAss-oah1 mutants do not accumulate oxalate in culture or during plant infection. The defect in oxalate accumulation is fully restored on reintroduction of the wild-type Ss-oah1gene. The DELTAss-oah1 mutants are deficient in compound appressorium and sclerotium development and exhibit a severe radial growth defect on medium buffered at neutral pH. On a variety of plant hosts, the DELTAss-oah1 mutants establish very restricted lesions in which the infectious hyphae gradually lose viability. Cytological comparisons of wild-type and DELTAss-oah1 infections reveal low and no oxalate accumulation, respectively, in subcuticular hyphae. Both wild-type and mutant hyphae exhibit a transient association with viable host epidermal cells at the infection front. DELTAss-oah1 mutants exhibit significantly attenuated virulence, e.g. in infected soybean leaves. Lesions generated by the GFP-labelled DELTAss-oah1 mutants expand slowly and are delimited within 3 days
malfunction
disruption of oxaloacetate hydrolase gene results in a slight decrease (~30%) in oxalate production, but has no significant influence on fungal growth. The mutant strain displays a significant delay at early stage of conidial development, and a significant defect in dimorphic transition. Additionally, bioassay using the greater waxmoth as host indicated a slight (about 20%) decrease in mortality caused by the gene disruption strain
malfunction
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gene deletion DELTAss-oah1 mutants do not accumulate oxalate in culture or during plant infection. The defect in oxalate accumulation is fully restored on reintroduction of the wild-type Ss-oah1gene. The DELTAss-oah1 mutants are deficient in compound appressorium and sclerotium development and exhibit a severe radial growth defect on medium buffered at neutral pH. On a variety of plant hosts, the DELTAss-oah1 mutants establish very restricted lesions in which the infectious hyphae gradually lose viability. Cytological comparisons of wild-type and DELTAss-oah1 infections reveal low and no oxalate accumulation, respectively, in subcuticular hyphae. Both wild-type and mutant hyphae exhibit a transient association with viable host epidermal cells at the infection front. DELTAss-oah1 mutants exhibit significantly attenuated virulence, e.g. in infected soybean leaves. Lesions generated by the GFP-labelled DELTAss-oah1 mutants expand slowly and are delimited within 3 days
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malfunction
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disruption of oxaloacetate hydrolase gene results in a slight decrease (~30%) in oxalate production, but has no significant influence on fungal growth. The mutant strain displays a significant delay at early stage of conidial development, and a significant defect in dimorphic transition. Additionally, bioassay using the greater waxmoth as host indicated a slight (about 20%) decrease in mortality caused by the gene disruption strain
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metabolism
the organism contains two oxalate-producing enzymes: oxaloacetate acetylhydrolase, which catalyzes hydrolysis of oxaloacetate, and cytochrome c dependent glyoxylate dehydrogenase, which catalyzes dehydrogenation of glyoxylate. Oxaloacetate is regarded as the predominant precursor for oxalate, because it shows greater activity compared to the dependent glyoxylate dehydrogenase
oxalacetate acetylhydrolase plays a key role in virulence
physiological function
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oxaloacetate hydrolase is generally responsible for oxalate production in filamentous fungi
physiological function
oxalate biogenesis in Sclerotinia. sclerotiorum appears to rely exclusively on oxaloacteate hydrolase-mediated C-C cleavage of oxaloacetate. During pathogenesis, oxalic acid accumulation is critical to the broad host range necrotrophic pathogenicity
physiological function
the oxaloacetate hydrolase gene connects the cytoplasmic route of oxalate production to fungal development and virulence
physiological function
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oxalate biogenesis in Sclerotinia. sclerotiorum appears to rely exclusively on oxaloacteate hydrolase-mediated C-C cleavage of oxaloacetate. During pathogenesis, oxalic acid accumulation is critical to the broad host range necrotrophic pathogenicity
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physiological function
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the oxaloacetate hydrolase gene connects the cytoplasmic route of oxalate production to fungal development and virulence
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