BRENDA - Enzyme Database show
show all sequences of 3.7.1.1

Oxaloacetate hydrolase, the C-C bond lyase of oxalate secreting fungi

Han, Y.; Joosten, H.J.; Niu, W.; Zhao, Z.; Mariano, P.S.; McCalman, M.; van Kan, J.; Schaap, P.J.; Dunaway-Mariano, D.; J. Biol. Chem. 282, 9581-9590 (2007)

Data extracted from this reference:

Application
Application
Commentary
Organism
food industry
oxalate toxicity is a concern for the commercial application of fungi in the food and drug industries
Aspergillus niger
food industry
oxalate toxicity is a concern for the commercial application of fungi in the food and drug industries
Botrytis cinerea
Cloned(Commentary)
Commentary
Organism
into the vector pGEM-T Easy for sequencing
Aspergillus niger
into the vector pGEM-T Easy for sequencing, and into pET-3c for expression in Escherichia coli BL21DE3 cells
Botrytis cinerea
Inhibitors
Inhibitors
Commentary
Organism
Structure
3,3-difluorooxaloacetate
-
Aspergillus niger
3,3-difluorooxaloacetate
-
Botrytis cinerea
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.062
-
oxaloacetate
cofactor Mg2+, buffer imidazole
Botrytis cinerea
0.064
-
oxaloacetate
cofactor Mg2+, buffer Hepes
Botrytis cinerea
0.084
-
oxaloacetate
cofactor Mg2+, buffer Tris
Botrytis cinerea
0.24
-
oxaloacetate
cofactor Mn2+, buffer imidazole
Botrytis cinerea
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
34360
-
theoretical molecular mass
Botrytis cinerea
35000
-
determined by SDS-PAGE
Botrytis cinerea
100000
-
determined by gel filtration, indicative of a homotrimeric quaternary structure
Botrytis cinerea
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
oxaloacetate + H2O
Botrytis cinerea
-
oxalate + acetate
-
-
?
oxaloacetate + H2O
Aspergillus niger
-
oxalate + acetate
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Aspergillus niger
Q7Z986
-
-
Botrytis cinerea
Q6PNM8
-
-
Purification (Commentary)
Commentary
Organism
by ammonium sulfate-induced protein precipitation, and by using of a DEAE-cellulose and a butyl-Sepharose column
Botrytis cinerea
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.62
-
cell extract
Botrytis cinerea
4.6
-
purification step ammonium sulfate precipitation
Botrytis cinerea
15
-
purification step DEAE-cellulose column
Botrytis cinerea
20
-
purification step butyl-Sepharose column
Botrytis cinerea
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
oxaloacetate + H2O
-
687682
Botrytis cinerea
oxalate + acetate
-
-
-
?
oxaloacetate + H2O
-
687682
Aspergillus niger
oxalate + acetate
-
-
-
?
Subunits
Subunits
Commentary
Organism
More
the results are consistent with the existence of a monomer-dimer-tetramer equilibrium
Botrytis cinerea
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
oxaloacetate hydrolase assay
Botrytis cinerea
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.35
-
oxaloacetate
cofactor Ca2+, buffer imidazole
Botrytis cinerea
9.5
-
oxaloacetate
cofactor Mg2+, buffer Tris
Botrytis cinerea
9.6
-
oxaloacetate
cofactor Mg2+, buffer Hepes
Botrytis cinerea
10.3
-
oxaloacetate
cofactor Mg2+, buffer imidazole
Botrytis cinerea
11.8
-
oxaloacetate
cofactor Mg2+, buffer imidazole
Botrytis cinerea
12.5
-
oxaloacetate
cofactor Mg2+, buffer Hepes
Botrytis cinerea
32
-
oxaloacetate
cofactor Mn2+, buffer Hepes
Botrytis cinerea
37
-
oxaloacetate
cofactor Mn2+, buffer imidazole
Botrytis cinerea
50
-
oxaloacetate
cofactor Mn2+, buffer imidazole
Botrytis cinerea
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.6
-
oxaloacetate hydrolase assay
Botrytis cinerea
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.000068
-
3,3-difluorooxaloacetate
-
Botrytis cinerea
Application (protein specific)
Application
Commentary
Organism
food industry
oxalate toxicity is a concern for the commercial application of fungi in the food and drug industries
Aspergillus niger
food industry
oxalate toxicity is a concern for the commercial application of fungi in the food and drug industries
Botrytis cinerea
Cloned(Commentary) (protein specific)
Commentary
Organism
into the vector pGEM-T Easy for sequencing
Aspergillus niger
into the vector pGEM-T Easy for sequencing, and into pET-3c for expression in Escherichia coli BL21DE3 cells
Botrytis cinerea
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
3,3-difluorooxaloacetate
-
Aspergillus niger
3,3-difluorooxaloacetate
-
Botrytis cinerea
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.000068
-
3,3-difluorooxaloacetate
-
Botrytis cinerea
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.062
-
oxaloacetate
cofactor Mg2+, buffer imidazole
Botrytis cinerea
0.064
-
oxaloacetate
cofactor Mg2+, buffer Hepes
Botrytis cinerea
0.084
-
oxaloacetate
cofactor Mg2+, buffer Tris
Botrytis cinerea
0.24
-
oxaloacetate
cofactor Mn2+, buffer imidazole
Botrytis cinerea
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
34360
-
theoretical molecular mass
Botrytis cinerea
35000
-
determined by SDS-PAGE
Botrytis cinerea
100000
-
determined by gel filtration, indicative of a homotrimeric quaternary structure
Botrytis cinerea
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
oxaloacetate + H2O
Botrytis cinerea
-
oxalate + acetate
-
-
?
oxaloacetate + H2O
Aspergillus niger
-
oxalate + acetate
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
by ammonium sulfate-induced protein precipitation, and by using of a DEAE-cellulose and a butyl-Sepharose column
Botrytis cinerea
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.62
-
cell extract
Botrytis cinerea
4.6
-
purification step ammonium sulfate precipitation
Botrytis cinerea
15
-
purification step DEAE-cellulose column
Botrytis cinerea
20
-
purification step butyl-Sepharose column
Botrytis cinerea
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
oxaloacetate + H2O
-
687682
Botrytis cinerea
oxalate + acetate
-
-
-
?
oxaloacetate + H2O
-
687682
Aspergillus niger
oxalate + acetate
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
More
the results are consistent with the existence of a monomer-dimer-tetramer equilibrium
Botrytis cinerea
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
oxaloacetate hydrolase assay
Botrytis cinerea
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.35
-
oxaloacetate
cofactor Ca2+, buffer imidazole
Botrytis cinerea
9.5
-
oxaloacetate
cofactor Mg2+, buffer Tris
Botrytis cinerea
9.6
-
oxaloacetate
cofactor Mg2+, buffer Hepes
Botrytis cinerea
10.3
-
oxaloacetate
cofactor Mg2+, buffer imidazole
Botrytis cinerea
11.8
-
oxaloacetate
cofactor Mg2+, buffer imidazole
Botrytis cinerea
12.5
-
oxaloacetate
cofactor Mg2+, buffer Hepes
Botrytis cinerea
32
-
oxaloacetate
cofactor Mn2+, buffer Hepes
Botrytis cinerea
37
-
oxaloacetate
cofactor Mn2+, buffer imidazole
Botrytis cinerea
50
-
oxaloacetate
cofactor Mn2+, buffer imidazole
Botrytis cinerea
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.6
-
oxaloacetate hydrolase assay
Botrytis cinerea
Other publictions for EC 3.7.1.1
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
734735
Liang
Oxaloacetate acetylhydrolase g ...
Sclerotinia sclerotiorum 1980, Sclerotinia sclerotiorum
Mol. Plant Pathol.
16
559-571
2015
-
-
1
-
1
-
-
-
-
-
-
2
-
5
-
-
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-
1
-
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2
-
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1
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1
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2
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1
-
-
2
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
734415
Kobayashi
Oxalic acid production by citr ...
Aspergillus niger, Aspergillus niger CBS 513.88, Aspergillus niger WU-2223L
J. Ind. Microbiol. Biotechnol.
41
749-756
2014
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-
1
-
1
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2
-
8
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2
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3
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1
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2
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2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
735295
Hisamori
-
Cloning and expression analysi ...
Fomitopsis palustris
Sustainable Humanosphere
9
57-64
2013
-
-
1
-
-
-
-
-
-
1
-
1
-
1
-
-
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1
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1
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1
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1
-
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1
-
1
-
-
-
1
-
-
-
-
1
1
-
-
-
719546
Gombert
Functional characterization of ...
no activity in Saccharomyces cerevisiae, Penicillium chrysogenum
Fungal Genet. Biol.
48
831-839
2011
-
-
1
-
-
-
-
-
-
1
-
1
-
6
-
-
-
-
-
-
-
-
1
-
1
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-
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1
-
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1
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1
-
1
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-
-
-
1
-
1
-
-
-
1
-
-
-
-
2
2
-
-
-
719879
Chen
Structure of oxalacetate acety ...
Cryphonectria parasitica
J. Biol. Chem.
285
26685-26696
2010
-
-
-
1
-
-
1
4
-
3
-
1
-
3
-
-
-
-
-
-
-
-
3
2
1
-
-
3
1
-
-
-
-
-
-
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-
-
1
-
-
-
1
-
4
-
3
-
1
-
-
-
-
-
-
-
-
3
2
1
-
-
3
1
-
-
-
-
3
3
-
-
-
693684
Narayanan
Structure and function of 2,3- ...
Aspergillus niger
J. Mol. Biol.
386
486-503
2009
-
-
1
1
6
-
4
6
-
1
4
-
-
1
-
-
1
-
-
-
-
-
1
1
-
-
-
7
1
1
-
-
3
-
-
-
-
1
-
1
6
-
-
4
3
6
-
1
4
-
-
-
-
1
-
-
-
-
1
1
-
-
-
7
1
1
-
-
-
1
1
-
5
5
686268
do Rio
Production of Calcium Oxalate ...
Moniliophthora perniciosa FA553
Curr. Microbiol.
56
363-370
2008
-
1
-
-
-
-
-
-
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1
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6
-
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1
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1
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1
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1
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1
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1
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-
-
-
-
-
-
-
-
689936
Joosten
Identification of fungal oxalo ...
Botrytis cinerea, Dianthus caryophyllus
Proteins
70
157-166
2008
-
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2
-
-
-
-
18
1
-
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1
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6
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2
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3
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2
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18
2
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2
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18
1
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1
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2
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3
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2
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18
2
-
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-
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-
-
-
-
687682
Han
Oxaloacetate hydrolase, the C- ...
Aspergillus niger, Botrytis cinerea
J. Biol. Chem.
282
9581-9590
2007
-
2
2
-
-
-
2
4
-
-
3
2
-
6
-
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1
-
-
-
4
-
2
1
1
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-
9
1
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1
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2
2
-
-
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2
1
4
-
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3
2
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1
-
-
4
-
2
1
1
-
-
9
1
-
-
-
-
-
-
-
-
-
668669
Sexton
Comparison of transcription of ...
Sclerotinia sclerotiorum
FEMS Microbiol. Lett.
258
150-160
2006
-
-
-
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-
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6
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1
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1
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670169
Sakai
Subcellular localization of gl ...
Fomitopsis palustris
Microbiology
152
1857-1866
2006
-
-
-
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1
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1
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3
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1
1
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1
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668652
Yoon
A metabolic role of the glyoxy ...
Fomitopsis palustris
FEMS Microbiol. Lett.
217
9-14
2002
-
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670718
Munir
A physiological role for oxali ...
Fomitopsis palustris
Proc. Natl. Acad. Sci. USA
98
11126-11130
2001
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-
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2
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1
1
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1
1
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1
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-
210608
Pedersen
Cloning and characterization o ...
Aspergillus niger
Mol. Gen. Genet.
263
281-286
2000
-
-
1
-
-
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-
1
-
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2
1
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2
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1
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1
1
1
1
1
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1
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1
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1
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2
1
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1
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1
1
1
1
1
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1
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-
210609
Ruijter
-
Oxalic acid production by Aspe ...
Aspergillus niger
Microbiology
145
2569-2576
1999
-
-
-
-
-
-
1
1
1
1
1
1
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1
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1
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1
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1
1
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1
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1
1
1
1
1
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1
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1
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1
1
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-
210610
Houck
Oxalic acid biosynthesis and o ...
Cryphonectria parasitica, Streptomyces cattleya
Arch. Biochem. Biophys.
259
58-65
1987
-
-
-
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-
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-
1
-
1
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210611
Muller
Utilization of gluconate by As ...
Aspergillus niger
Zentralbl. Mikrobiol.
141
461-469
1986
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210612
Lenz
Partial purification and some ...
Aspergillus niger
Eur. J. Biochem.
65
225-236
1976
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210613
Muller
Oxalate accumulation from citr ...
Aspergillus niger
Arch. Microbiol.
103
185-189
1975
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210614
Maxwell
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Oxalate formation in Whetzelin ...
Sclerotinia sclerotiorum
Physiol. Plant Pathol.
3
279-288
1973
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210615
Hayaishi
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Enzymatic formation of oxalate ...
Aspergillus niger
J. Am. Chem. Soc.
78
5126-5127
1956
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