BRENDA - Enzyme Database show
show all sequences of 3.7.1.1

Cloning and expression analysis of a cDNA encoding an oxaloacetate acetylhydrolase from the brown-rot fungus Fomitopsis palustris

Hisamori, H.; Watanabe, T.; Suzuki, S.; Okawa, K.; Sakai, H.; Yoshimura, T.; Umezawa, T.; Hattori, T.; Sustainable Humanosphere 9, 57-64 (2013)
No PubMed abstract available

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene oahA, phylogenetic tree, recombinant expression in Escherichia coli strain BL21(DE3)
Fomitopsis palustris
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mn2+
required
Fomitopsis palustris
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
oxaloacetate + H2O
Fomitopsis palustris
-
oxalate + acetate
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Fomitopsis palustris
M5AIH9
gene oahA
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
mycelium
-
Fomitopsis palustris
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
oxaloacetate + H2O
-
735295
Fomitopsis palustris
oxalate + acetate
-
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Fomitopsis palustris
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.6
-
assay at
Fomitopsis palustris
Cloned(Commentary) (protein specific)
Commentary
Organism
gene oahA, phylogenetic tree, recombinant expression in Escherichia coli strain BL21(DE3)
Fomitopsis palustris
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mn2+
required
Fomitopsis palustris
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
oxaloacetate + H2O
Fomitopsis palustris
-
oxalate + acetate
-
-
?
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
mycelium
-
Fomitopsis palustris
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
oxaloacetate + H2O
-
735295
Fomitopsis palustris
oxalate + acetate
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Fomitopsis palustris
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.6
-
assay at
Fomitopsis palustris
General Information
General Information
Commentary
Organism
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
Fomitopsis palustris
General Information (protein specific)
General Information
Commentary
Organism
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
Fomitopsis palustris
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
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1
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1
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5
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2
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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
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735295
Hisamori
-
Cloning and expression analysi ...
Fomitopsis palustris
Sustainable Humanosphere
9
57-64
2013
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1
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719546
Gombert
Functional characterization of ...
no activity in Saccharomyces cerevisiae, Penicillium chrysogenum
Fungal Genet. Biol.
48
831-839
2011
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1
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1
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1
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6
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1
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2
2
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719879
Chen
Structure of oxalacetate acety ...
Cryphonectria parasitica
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285
26685-26696
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1
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1
4
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3
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1
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3
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2
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1
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3
2
1
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3
1
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3
3
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-
693684
Narayanan
Structure and function of 2,3- ...
Aspergillus niger
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486-503
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1
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6
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4
6
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1
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1
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1
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5
5
686268
do Rio
Production of Calcium Oxalate ...
Moniliophthora perniciosa FA553
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363-370
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1
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689936
Joosten
Identification of fungal oxalo ...
Botrytis cinerea, Dianthus caryophyllus
Proteins
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157-166
2008
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2
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18
1
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6
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18
2
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18
1
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18
2
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687682
Han
Oxaloacetate hydrolase, the C- ...
Aspergillus niger, Botrytis cinerea
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9581-9590
2007
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2
2
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2
4
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2
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6
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1
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9
1
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2
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2
1
4
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1
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9
1
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-
668669
Sexton
Comparison of transcription of ...
Sclerotinia sclerotiorum
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150-160
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670169
Sakai
Subcellular localization of gl ...
Fomitopsis palustris
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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
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98
11126-11130
2001
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210608
Pedersen
Cloning and characterization o ...
Aspergillus niger
Mol. Gen. Genet.
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281-286
2000
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210609
Ruijter
-
Oxalic acid production by Aspe ...
Aspergillus niger
Microbiology
145
2569-2576
1999
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1
1
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210610
Houck
Oxalic acid biosynthesis and o ...
Cryphonectria parasitica, Streptomyces cattleya
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58-65
1987
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1
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210611
Muller
Utilization of gluconate by As ...
Aspergillus niger
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210612
Lenz
Partial purification and some ...
Aspergillus niger
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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
-
Oxalate formation in Whetzelin ...
Sclerotinia sclerotiorum
Physiol. Plant Pathol.
3
279-288
1973
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210615
Hayaishi
-
Enzymatic formation of oxalate ...
Aspergillus niger
J. Am. Chem. Soc.
78
5126-5127
1956
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