EC Number |
General Information |
Reference |
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3.7.1.1 | evolution |
oxalacetate acetylhydrolase is a member of the phosphoenolpyruvate mutase/isocitrate lyase superfamily |
719879 |
3.7.1.1 | malfunction |
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 |
719546 |
3.7.1.1 | 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 |
-, 757082 |
3.7.1.1 | 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 |
-, 734735 |
3.7.1.1 | 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 |
719879 |
3.7.1.1 | metabolism |
DMML is a key enzyme in bacterial nicotinate catabolism |
693684 |
3.7.1.1 | 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 |
735295 |
3.7.1.1 | physiological function |
oxalacetate acetylhydrolase plays a key role in virulence |
719879 |
3.7.1.1 | 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 |
-, 734735 |
3.7.1.1 | physiological function |
oxaloacetate hydrolase is generally responsible for oxalate production in filamentous fungi |
719546 |