BRENDA - Enzyme Database show
show all sequences of 3.7.1.1

Identification of fungal oxaloacetate hydrolyase within the isocitrate lyase/PEP mutase enzyme superfamily using a sequence marker-based method

Joosten, H.J.; Han, Y.; Niu, W.; Vervoort, J.; Dunaway-Mariano, D.; Schaap, P.J.; Proteins 70, 157-166 (2008)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
into the vector pET-3c
Botrytis cinerea
into the vector pET-3c
Dianthus caryophyllus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.022
-
(2R,3S)-2,3-dimethylmalate
mutant S260P
Botrytis cinerea
0.054
-
(2R,3S)-2,3-dimethylmalate
mutant S260A
Botrytis cinerea
0.065
-
oxaloacetate
wild-type protein
Botrytis cinerea
0.13
-
oxaloacetate
wild-type protein
Dianthus caryophyllus
0.14
-
(2R,3S)-2,3-dimethylmalate
wild-type protein
Botrytis cinerea
0.15
-
oxaloacetate
mutant S260P, trial 1
Botrytis cinerea
0.22
-
oxaloacetate
mutant S260P, trial 2
Botrytis cinerea
0.53
-
(2R,3S)-2-ethyl-3-methylmalate
wild-type protein
Dianthus caryophyllus
0.56
-
(2R,3S)-2-ethyl-3-methylmalate
mutant S257A
Dianthus caryophyllus
0.66
-
(2R,3S)-2-ethyl-3-methylmalate
mutant S257P
Dianthus caryophyllus
0.7
-
oxaloacetate
mutant S260A, trial 1
Botrytis cinerea
0.84
-
oxaloacetate
mutant S257P
Dianthus caryophyllus
1.307
-
oxaloacetate
mutant S260A, trial 2
Botrytis cinerea
1.53
-
oxaloacetate
mutant S257A
Dianthus caryophyllus
2.6
-
oxaloacetate
mutant S257T, trial 2
Dianthus caryophyllus
3.6
-
oxaloacetate
mutant S257T, trial 1
Dianthus caryophyllus
7
-
oxaloacetate
mutant S260T, trial 1
Botrytis cinerea
7.7
-
oxaloacetate
mutant S260T, trial 2
Botrytis cinerea
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(2R,3S)-2,3-dimethylmalate
Botrytis cinerea
-
pyruvate + propionic acid
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Botrytis cinerea
Q6PNM8
-
-
Dianthus caryophyllus
-
-
-
Purification (Commentary)
Commentary
Organism
proteins are purified to homogeneity
Botrytis cinerea
proteins are purified to homogeneity
Dianthus caryophyllus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(2R,3S)-2,3-dimethylmalate
-
689936
Botrytis cinerea
pyruvate + propionic acid
-
-
-
?
oxaloacetate + H2O
-
689936
Dianthus caryophyllus
oxalate + acetate
-
-
-
-
oxaloacetate + H2O
-
689936
Botrytis cinerea
oxalate + acetate
-
-
-
-
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
activity assay
Botrytis cinerea
25
-
activity assay
Dianthus caryophyllus
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.0249
-
(2R,3S)-2,3-dimethylmalate
mutant S260A
Botrytis cinerea
0.0293
-
(2R,3S)-2,3-dimethylmalate
wild-type protein
Botrytis cinerea
0.074
-
(2R,3S)-2,3-dimethylmalate
mutant S260P
Botrytis cinerea
0.71
-
oxaloacetate
mutant S260A, trial 2
Botrytis cinerea
0.83
-
oxaloacetate
mutant S260A, trial 1
Botrytis cinerea
0.96
-
oxaloacetate
mutant S260P, trial 1
Botrytis cinerea
0.98
-
oxaloacetate
mutant S260P, trial 2
Botrytis cinerea
1.14
-
oxaloacetate
mutant S257T, trial 1
Dianthus caryophyllus
1.16
-
oxaloacetate
mutant S257T, trial 2
Dianthus caryophyllus
2.59
-
oxaloacetate
mutant S260T, trial 1
Botrytis cinerea
2.72
-
oxaloacetate
wild-type protein
Dianthus caryophyllus
2.91
-
oxaloacetate
mutant S257A
Dianthus caryophyllus
3.6
-
oxaloacetate
mutant S260T, trial 2
Botrytis cinerea
4.1
-
oxaloacetate
mutant S257P
Dianthus caryophyllus
5.4
-
(2R,3S)-2-ethyl-3-methylmalate
mutant S257A
Dianthus caryophyllus
8.3
-
(2R,3S)-2-ethyl-3-methylmalate
mutant S257P
Dianthus caryophyllus
8.4
-
(2R,3S)-2-ethyl-3-methylmalate
wild-type protein
Dianthus caryophyllus
17.4
-
oxaloacetate
wild-type protein
Botrytis cinerea
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
activity assay
Botrytis cinerea
7.5
-
activity assay
Dianthus caryophyllus
Cloned(Commentary) (protein specific)
Commentary
Organism
into the vector pET-3c
Botrytis cinerea
into the vector pET-3c
Dianthus caryophyllus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.022
-
(2R,3S)-2,3-dimethylmalate
mutant S260P
Botrytis cinerea
0.054
-
(2R,3S)-2,3-dimethylmalate
mutant S260A
Botrytis cinerea
0.065
-
oxaloacetate
wild-type protein
Botrytis cinerea
0.13
-
oxaloacetate
wild-type protein
Dianthus caryophyllus
0.14
-
(2R,3S)-2,3-dimethylmalate
wild-type protein
Botrytis cinerea
0.15
-
oxaloacetate
mutant S260P, trial 1
Botrytis cinerea
0.22
-
oxaloacetate
mutant S260P, trial 2
Botrytis cinerea
0.53
-
(2R,3S)-2-ethyl-3-methylmalate
wild-type protein
Dianthus caryophyllus
0.56
-
(2R,3S)-2-ethyl-3-methylmalate
mutant S257A
Dianthus caryophyllus
0.66
-
(2R,3S)-2-ethyl-3-methylmalate
mutant S257P
Dianthus caryophyllus
0.7
-
oxaloacetate
mutant S260A, trial 1
Botrytis cinerea
0.84
-
oxaloacetate
mutant S257P
Dianthus caryophyllus
1.307
-
oxaloacetate
mutant S260A, trial 2
Botrytis cinerea
1.53
-
oxaloacetate
mutant S257A
Dianthus caryophyllus
2.6
-
oxaloacetate
mutant S257T, trial 2
Dianthus caryophyllus
3.6
-
oxaloacetate
mutant S257T, trial 1
Dianthus caryophyllus
7
-
oxaloacetate
mutant S260T, trial 1
Botrytis cinerea
7.7
-
oxaloacetate
mutant S260T, trial 2
Botrytis cinerea
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(2R,3S)-2,3-dimethylmalate
Botrytis cinerea
-
pyruvate + propionic acid
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
proteins are purified to homogeneity
Botrytis cinerea
proteins are purified to homogeneity
Dianthus caryophyllus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(2R,3S)-2,3-dimethylmalate
-
689936
Botrytis cinerea
pyruvate + propionic acid
-
-
-
?
oxaloacetate + H2O
-
689936
Dianthus caryophyllus
oxalate + acetate
-
-
-
-
oxaloacetate + H2O
-
689936
Botrytis cinerea
oxalate + acetate
-
-
-
-
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
activity assay
Botrytis cinerea
25
-
activity assay
Dianthus caryophyllus
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.0249
-
(2R,3S)-2,3-dimethylmalate
mutant S260A
Botrytis cinerea
0.0293
-
(2R,3S)-2,3-dimethylmalate
wild-type protein
Botrytis cinerea
0.074
-
(2R,3S)-2,3-dimethylmalate
mutant S260P
Botrytis cinerea
0.71
-
oxaloacetate
mutant S260A, trial 2
Botrytis cinerea
0.83
-
oxaloacetate
mutant S260A, trial 1
Botrytis cinerea
0.96
-
oxaloacetate
mutant S260P, trial 1
Botrytis cinerea
0.98
-
oxaloacetate
mutant S260P, trial 2
Botrytis cinerea
1.14
-
oxaloacetate
mutant S257T, trial 1
Dianthus caryophyllus
1.16
-
oxaloacetate
mutant S257T, trial 2
Dianthus caryophyllus
2.59
-
oxaloacetate
mutant S260T, trial 1
Botrytis cinerea
2.72
-
oxaloacetate
wild-type protein
Dianthus caryophyllus
2.91
-
oxaloacetate
mutant S257A
Dianthus caryophyllus
3.6
-
oxaloacetate
mutant S260T, trial 2
Botrytis cinerea
4.1
-
oxaloacetate
mutant S257P
Dianthus caryophyllus
5.4
-
(2R,3S)-2-ethyl-3-methylmalate
mutant S257A
Dianthus caryophyllus
8.3
-
(2R,3S)-2-ethyl-3-methylmalate
mutant S257P
Dianthus caryophyllus
8.4
-
(2R,3S)-2-ethyl-3-methylmalate
wild-type protein
Dianthus caryophyllus
17.4
-
oxaloacetate
wild-type protein
Botrytis cinerea
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
activity assay
Botrytis cinerea
7.5
-
activity assay
Dianthus caryophyllus
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
-
-
-
-
-
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
-
-
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
-
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-
-
-
-
-
-
-
-
-
-
-
-
-
735295
Hisamori
-
Cloning and expression analysi ...
Fomitopsis palustris
Sustainable Humanosphere
9
57-64
2013
-
-
1
-
-
-
-
-
-
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
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-
1
-
-
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
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
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
-
-
-
-
-
-
-
-
-
-
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
-
-
-
-
-
-
-
-
-
1
-
6
-
-
-
-
-
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
-
-
2
-
-
-
-
18
1
-
-
1
-
6
-
-
2
-
-
-
-
-
3
-
2
-
-
18
2
-
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-
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2
-
-
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-
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-
-
18
1
-
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1
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2
-
-
-
-
3
-
2
-
-
18
2
-
-
-
-
-
-
-
-
-
687682
Han
Oxaloacetate hydrolase, the C- ...
Aspergillus niger, Botrytis cinerea
J. Biol. Chem.
282
9581-9590
2007
-
2
2
-
-
-
2
4
-
-
3
2
-
6
-
-
1
-
-
-
4
-
2
1
1
-
-
9
1
-
-
-
1
-
-
-
2
2
-
-
-
-
-
2
1
4
-
-
3
2
-
-
-
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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6
-
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1
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1
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-
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-
-
-
-
-
-
-
-
-
-
-
-
-
670169
Sakai
Subcellular localization of gl ...
Fomitopsis palustris
Microbiology
152
1857-1866
2006
-
-
-
-
-
-
-
-
1
-
-
1
-
3
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1
1
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2
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1
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-
1
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1
1
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
668652
Yoon
A metabolic role of the glyoxy ...
Fomitopsis palustris
FEMS Microbiol. Lett.
217
9-14
2002
-
-
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1
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2
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1
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2
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1
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-
-
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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
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1
1
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1
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Pedersen
Cloning and characterization o ...
Aspergillus niger
Mol. Gen. Genet.
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281-286
2000
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210609
Ruijter
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Oxalic acid production by Aspe ...
Aspergillus niger
Microbiology
145
2569-2576
1999
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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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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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