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0.022 - 0.14
(2R,3S)-2,3-dimethylmalate
0.53 - 0.66
(2R,3S)-2-ethyl-3-methylmalate
0.027 - 20.14
oxaloacetate
additional information
additional information
-
0.022
(2R,3S)-2,3-dimethylmalate
mutant S260P
0.054
(2R,3S)-2,3-dimethylmalate
mutant S260A
0.14
(2R,3S)-2,3-dimethylmalate
wild-type protein
0.53
(2R,3S)-2-ethyl-3-methylmalate
-
wild-type protein
0.56
(2R,3S)-2-ethyl-3-methylmalate
-
mutant S257A
0.66
(2R,3S)-2-ethyl-3-methylmalate
-
mutant S257P
0.004
Mn2+
-
-
0.027
oxaloacetate
-
mutant enzyme C124S, in 50 mM K+-HEPES (pH 7.5 and 25°C)
0.062
oxaloacetate
cofactor Mg2+, buffer imidazole
0.064
oxaloacetate
cofactor Mg2+, buffer Hepes
0.065
oxaloacetate
wild-type protein
0.084
oxaloacetate
cofactor Mg2+, buffer Tris
0.13
oxaloacetate
-
wild-type protein
0.134
oxaloacetate
in presence of Mg2+, pH 7.5, 25°C
0.15
oxaloacetate
mutant S260P, trial 1
0.22
oxaloacetate
mutant S260P, trial 2
0.22
oxaloacetate
-
wild type enzyme, in 50 mM K+-HEPES (pH 7.5 and 25°C)
0.234
oxaloacetate
-
wild type enzyme, in 0.1 M imidazole (pH 7.6 and 25°C)
0.24
oxaloacetate
cofactor Mn2+, buffer imidazole
0.48
oxaloacetate
in presence of Mn2+, pH 7.5, 25°C
0.7
oxaloacetate
mutant S260A, trial 1
0.84
oxaloacetate
-
mutant S257P
1.11
oxaloacetate
-
mutant enzyme P240S, in 50 mM K+-HEPES (pH 7.5 and 25°C)
1.22
oxaloacetate
-
mutant enzyme P240T, in 50 mM K+-HEPES (pH 7.5 and 25°C)
1.248
oxaloacetate
in presence of Ca2+, pH 7.5, 25°C
1.307
oxaloacetate
mutant S260A, trial 2
1.53
oxaloacetate
-
mutant S257A
2.6
oxaloacetate
-
mutant S257T, trial 2
3.6
oxaloacetate
-
mutant S257T, trial 1
7
oxaloacetate
mutant S260T, trial 1
7.7
oxaloacetate
mutant S260T, trial 2
20.14
oxaloacetate
-
mutant enzyme C124A, in 50 mM K+-HEPES (pH 7.5 and 25°C)
additional information
additional information
steady-state kinetic constants for divalent metal-activated OAH from
-
additional information
additional information
-
steady-state kinetic constants for divalent metal-activated OAH from
-
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0.0249 - 0.074
(2R,3S)-2,3-dimethylmalate
5.4 - 8.4
(2R,3S)-2-ethyl-3-methylmalate
0.00001 - 50
oxaloacetate
0.0249
(2R,3S)-2,3-dimethylmalate
mutant S260A
0.0293
(2R,3S)-2,3-dimethylmalate
wild-type protein
0.074
(2R,3S)-2,3-dimethylmalate
mutant S260P
5.4
(2R,3S)-2-ethyl-3-methylmalate
-
mutant S257A
8.3
(2R,3S)-2-ethyl-3-methylmalate
-
mutant S257P
8.4
(2R,3S)-2-ethyl-3-methylmalate
-
wild-type protein
0.00001
oxaloacetate
-
mutant enzyme Y44F, in 50 mM K+-HEPES (pH 7.5 and 25°C)
0.081
oxaloacetate
-
mutant enzyme C124S, in 50 mM K+-HEPES (pH 7.5 and 25°C)
0.082
oxaloacetate
-
mutant enzyme P240T, in 50 mM K+-HEPES (pH 7.5 and 25°C)
0.125
oxaloacetate
-
mutant enzyme C124A, in 50 mM K+-HEPES (pH 7.5 and 25°C)
0.35
oxaloacetate
cofactor Ca2+, buffer imidazole
0.357
oxaloacetate
-
mutant enzyme P240S, in 50 mM K+-HEPES (pH 7.5 and 25°C)
0.48
oxaloacetate
-
wild type enzyme, in 50 mM K+-HEPES (pH 7.5 and 25°C)
0.505
oxaloacetate
-
wild type enzyme, in 0.1 M imidazole (pH 7.6 and 25°C)
0.71
oxaloacetate
mutant S260A, trial 2
0.83
oxaloacetate
mutant S260A, trial 1
0.96
oxaloacetate
mutant S260P, trial 1
0.98
oxaloacetate
mutant S260P, trial 2
1.14
oxaloacetate
-
mutant S257T, trial 1
1.16
oxaloacetate
-
mutant S257T, trial 2
1.9
oxaloacetate
in presence of Ca2+, pH 7.5, 25°C
2.59
oxaloacetate
mutant S260T, trial 1
2.72
oxaloacetate
-
wild-type protein
2.91
oxaloacetate
-
mutant S257A
3.6
oxaloacetate
mutant S260T, trial 2
3.6
oxaloacetate
in presence of Mg2+, pH 7.5, 25°C
4.1
oxaloacetate
-
mutant S257P
9.5
oxaloacetate
cofactor Mg2+, buffer Tris
9.6
oxaloacetate
cofactor Mg2+, buffer Hepes
10.3
oxaloacetate
cofactor Mg2+, buffer imidazole
11.8
oxaloacetate
cofactor Mg2+, buffer imidazole
12.5
oxaloacetate
cofactor Mg2+, buffer Hepes
17.4
oxaloacetate
wild-type protein
32
oxaloacetate
cofactor Mn2+, buffer Hepes
35.2
oxaloacetate
in presence of Mn2+, pH 7.5, 25°C
37
oxaloacetate
cofactor Mn2+, buffer imidazole
50
oxaloacetate
cofactor Mn2+, buffer imidazole
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evolution
oxalacetate acetylhydrolase is a member of the phosphoenolpyruvate mutase/isocitrate lyase superfamily
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
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
-
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
-
metabolism
-
DMML is a key enzyme in bacterial nicotinate catabolism
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
physiological function
oxalacetate acetylhydrolase plays a key role in virulence
physiological function
-
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
-
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
-
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Cloning and characterization of oah, the gene encoding oxaloacetate hydrolase in Aspergillus niger
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Oxalic acid production by Aspergillus niger: an oxalate-non-producing mutant produces citric acid at pH 5 and in the presence of manganese
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Houck, D.R.; Inamine, E.
Oxalic acid biosynthesis and oxalacetate acetylhydrolase activity in Streptomyces cattleya
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1987
Cryphonectria parasitica, Streptomyces cattleya
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Utilization of gluconate by Aspergillus niger. II. Enzymes of degradation pathways and main end products
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Partial purification and some properties of oxalacetase from Aspergillus niger
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Aspergillus niger
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Oxalate accumulation from citrate by Aspergillus niger. I. Biosynthesis of oxalate from its ultimate precursor
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Maxwell, D.P.
Oxalate formation in Whetzelinia sclerotiorum by oxalacetate acetylhydrolase
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1973
Sclerotinia sclerotiorum
-
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Hayaishi, O.; Shimazono, H.; Katagiri, M.; Saito, Y.
Enzymatic formation of oxalate and acetate from oxaloacetate
J. Am. Chem. Soc.
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Aspergillus niger
-
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Yoon, J.; Hattori, T.; Shimada, M.
A metabolic role of the glyoxylate and tricarboxylic acid cycles for development of the copper-tolerant brown-rot fungus Fomitopsis palustris
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2002
Fomitopsis palustris
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Comparison of transcription of multiple genes at three developmental stages of the plant pathogen Sclerotinia sclerotiorum
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258
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Sclerotinia sclerotiorum
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Subcellular localization of glyoxylate cycle key enzymes involved in oxalate biosynthesis of wood-destroying basidiomycete Fomitopsis palustris grown on glucose
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Fomitopsis palustris
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A physiological role for oxalic acid biosynthesis in the wood-rotting basidiomycete Fomitopsis palustris
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98
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Fomitopsis palustris
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do Rio, M.C.; de Oliveira, B.V.; de Tomazella, D.P.; da Silva, J.A.; Pereira, G.A.
Production of Calcium Oxalate Crystals by the Basidiomycete Moniliophthora perniciosa, the Causal Agent of Witches Broom Disease of Cacao
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Moniliophthora perniciosa FA553
brenda
Han, Y.; Joosten, H.J.; Niu, W.; Zhao, Z.; Mariano, P.S.; McCalman, M.; van Kan, J.; Schaap, P.J.; Dunaway-Mariano, D.
Oxaloacetate hydrolase, the C-C bond lyase of oxalate secreting fungi
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Botrytis cinerea (Q6PNM8), Botrytis cinerea, Aspergillus niger (Q7Z986), Aspergillus niger
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Joosten, H.J.; Han, Y.; Niu, W.; Vervoort, J.; Dunaway-Mariano, D.; Schaap, P.J.
Identification of fungal oxaloacetate hydrolyase within the isocitrate lyase/PEP mutase enzyme superfamily using a sequence marker-based method
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70
157-166
2008
Dianthus caryophyllus, Botrytis cinerea (Q6PNM8), Botrytis cinerea
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Narayanan, B.; Niu, W.; Joosten, H.J.; Li, Z.; Kuipers, R.K.; Schaap, P.J.; Dunaway-Mariano, D.; Herzberg, O.
Structure and function of 2,3-dimethylmalate lyase, a PEP mutase/isocitrate lyase superfamily member
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386
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2009
Aspergillus niger
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Gombert, A.K.; Veiga, T.; Puig-Martinez, M.; Lamboo, F.; Nijland, J.G.; Driessen, A.J.; Pronk, J.T.; Daran, J.M.
Functional characterization of the oxaloacetase encoding gene and elimination of oxalate formation in the beta-lactam producer Penicillium chrysogenum
Fungal Genet. Biol.
48
831-839
2011
no activity in Saccharomyces cerevisiae, Penicillium chrysogenum
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Chen, C.; Sun, Q.; Narayanan, B.; Nuss, D.L.; Herzberg, O.
Structure of oxalacetate acetylhydrolase, a virulence factor of the chestnut blight fungus
J. Biol. Chem.
285
26685-26696
2010
Cryphonectria parasitica (D5LIR7), Cryphonectria parasitica
brenda
Kobayashi, K.; Hattori, T.; Honda, Y.; Kirimura, K.
Oxalic acid production by citric acid-producing Aspergillus niger overexpressing the oxaloacetate hydrolase gene oahA
J. Ind. Microbiol. Biotechnol.
41
749-756
2014
Aspergillus niger (A2QP68), Aspergillus niger (Q2L886), Aspergillus niger (Q7Z986), Aspergillus niger, Aspergillus niger CBS 513.88 (A2QP68), Aspergillus niger CBS 513.88 (Q2L886), Aspergillus niger WU-2223L (Q7Z986)
brenda
Liang, X.; Liberti, D.; Li, M.; Kim, Y.T.; Hutchens, A.; Wilson, R.; Rollins, J.A.
Oxaloacetate acetylhydrolase gene mutants of Sclerotinia sclerotiorum do not accumulate oxalic acid, but do produce limited lesions on host plants
Mol. Plant Pathol.
16
559-571
2015
Sclerotinia sclerotiorum (A7ESB3), Sclerotinia sclerotiorum, Sclerotinia sclerotiorum 1980 (A7ESB3)
brenda
Hisamori, H.; Watanabe, T.; Suzuki, S.; Okawa, K.; Sakai, H.; Yoshimura, T.; Umezawa, T.; Hattori, T.
Cloning and expression analysis of a cDNA encoding an oxaloacetate acetylhydrolase from the brown-rot fungus Fomitopsis palustris
Sustainable Humanosphere
9
57-64
2013
Fomitopsis palustris (M5AIH9)
-
brenda
Gao, Y.; Feng, M.; Ying, S.
Oxaloacetate hydrolase gene links the cytoplasmic route of oxalate formation to differentiation and virulence of entomopathogenic fungus Beauveria bassiana
J. Asia Pac. Entomol.
21
211-216
2018
Beauveria bassiana (J4UKL8), Beauveria bassiana ARSEF 2860 (J4UKL8)
-
brenda
Yoshioka, I.; Kobayashi, K.; Kirimura, K.
Overexpression of the gene encoding alternative oxidase for enhanced glucose consumption in oxalic acid producing Aspergillus niger expressing oxaloacetate hydrolase gene
J. Biosci. Bioeng.
129
172-176
2019
Aspergillus niger
brenda