Information on EC 3.7.1.1 - oxaloacetase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
3.7.1.1
-
RECOMMENDED NAME
GeneOntology No.
oxaloacetase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
oxaloacetate + H2O = oxalate + acetate
show the reaction diagram
-
-
-
-
oxaloacetate + H2O = oxalate + acetate
show the reaction diagram
unknown mechanism
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of C-C bond
-
-
-
-
hydrolysis of C-C bond
-
-
hydrolysis of C-C bond
-
-
hydrolysis of C-C bond
Q7Z986
-
hydrolysis of C-C bond
-, Q6PNM8
-
hydrolysis of C-C bond
-
-
PATHWAY
KEGG Link
MetaCyc Link
oxalate biosynthesis
-
SYSTEMATIC NAME
IUBMB Comments
oxaloacetate acetylhydrolase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
(2R,3S)-dimethylmalate lyase
-
-
An07g08390
-
-
OAH
Q7Z986
-
OAH-active petal death protein
-
-
oxalacetase
-
-
-
-
oxalacetate acetylhydrolase
D5LIR7
-
oxalacetic hydrolase
-
-
-
-
oxaloacetase
Q6PNM8
-
oxaloacetate acethylhydrolase
-
-
-
-
oxaloacetate acetylhydrolase
Q7Z986
-
oxaloacetate acetylhydrolase
Q6PNM8
-
oxaloacetate acetylhydrolase
-
-
oxaloacetate acetylhydrolase
-
-
oxaloacetate hydrolase
Q7Z986
-
oxaloacetate hydrolase
Q6PNM8
-
oxaloacetate hydrolase
-
-
CAS REGISTRY NUMBER
COMMENTARY
9024-89-9
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
inducible enzyme, expressed only at pH values higher than 4.0
-
-
Manually annotated by BRENDA team
gene oah is a single gene
UniProt
Manually annotated by BRENDA team
brown-rot fungus
-
-
Manually annotated by BRENDA team
formerly Tyromyces palustris
-
-
Manually annotated by BRENDA team
no activity in Saccharomyces cerevisiae
-
-
-
Manually annotated by BRENDA team
gene Pc22g24830
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
evolution
-, D5LIR7
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
-, D5LIR7
knockout of the oah gene in Cryphonectria parasitica, the chestnut blight fungus, reduces the ability of the fungus to form cankers on chestnut trees
metabolism
-
DMML is a key enzyme in bacterial nicotinate catabolism
physiological function
-
oxaloacetate hydrolase is generally responsible for oxalate production in filamentous fungi
physiological function
-, D5LIR7
oxalacetate acetylhydrolase plays a key role in virulence
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
oxaloacetate + H2O
oxalate + acetate
show the reaction diagram
-
-
-
?
oxaloacetate + H2O
oxalate + acetate
show the reaction diagram
-
-
-
?
oxaloacetate + H2O
oxalate + acetate
show the reaction diagram
-
-
-
-
?
oxaloacetate + H2O
oxalate + acetate
show the reaction diagram
-
-
-
?
oxaloacetate + H2O
oxalate + acetate
show the reaction diagram
-
-
-
?
oxaloacetate + H2O
oxalate + acetate
show the reaction diagram
-
-
-
-
-
oxaloacetate + H2O
oxalate + acetate
show the reaction diagram
-
-
-
?
oxaloacetate + H2O
oxalate + acetate
show the reaction diagram
-
-
-
-
?
oxaloacetate + H2O
oxalate + acetate
show the reaction diagram
-
-
-
-
ir
oxaloacetate + H2O
oxalate + acetate
show the reaction diagram
-
-
-
-
-
oxaloacetate + H2O
oxalate + acetate
show the reaction diagram
-, Q6PNM8
-
-
-
?
oxaloacetate + H2O
oxalate + acetate
show the reaction diagram
-
-
-
-
?
oxaloacetate + H2O
oxalate + acetate
show the reaction diagram
Q7Z986
-
-
-
?
oxaloacetate + H2O
oxalate + acetate
show the reaction diagram
-, D5LIR7
-
-
-
?
oxaloacetate + H2O
oxalate + acetate
show the reaction diagram
-
hydrolysis of oxaloacetate strongly preferred
-
r
oxaloacetate + H2O
oxalate + acetate
show the reaction diagram
-
could be involved in pathogenesis and keeping pH low in vicinity of the fungus
-
?
oxaloacetate + H2O
oxalate + acetate
show the reaction diagram
-
DMML also possesses significant oxaloacetate acetyl hydrolase activity
-
-
?
oxaloacetate + H2O
oxalate + acetate
show the reaction diagram
-, D5LIR7
oxalate binds in a planar conformation, but the gating loop is largely disordered
-
-
?
(2R,3S)-2,3-dimethylmalate
pyruvate + propionic acid
show the reaction diagram
-
-
-
-
?
additional information
?
-
-, D5LIR7
OAH also exhibits C-C bond cleavagea activity with (2R,3S)-dimethylmalate with 1000fold lower efficacy compared to oxaloacetate hydrolysis. Structural features of substrate binding, overview
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(2R,3S)-2,3-dimethylmalate
pyruvate + propionic acid
show the reaction diagram
-
-
-
-
?
oxaloacetate + H2O
oxalate + acetate
show the reaction diagram
-
-
-
?
oxaloacetate + H2O
oxalate + acetate
show the reaction diagram
-
-
-
?
oxaloacetate + H2O
oxalate + acetate
show the reaction diagram
-
-
-
-
?
oxaloacetate + H2O
oxalate + acetate
show the reaction diagram
-
-
-
?
oxaloacetate + H2O
oxalate + acetate
show the reaction diagram
-
-
-
?
oxaloacetate + H2O
oxalate + acetate
show the reaction diagram
-
-
-
-
?
oxaloacetate + H2O
oxalate + acetate
show the reaction diagram
-, Q6PNM8
-
-
-
?
oxaloacetate + H2O
oxalate + acetate
show the reaction diagram
-
-
-
-
?
oxaloacetate + H2O
oxalate + acetate
show the reaction diagram
Q7Z986
-
-
-
?
oxaloacetate + H2O
oxalate + acetate
show the reaction diagram
-, D5LIR7
-
-
-
?
oxaloacetate + H2O
oxalate + acetate
show the reaction diagram
-
could be involved in pathogenesis and keeping pH low in vicinity of the fungus
-
?
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-, D5LIR7
required, in addition to the active site metal cofactors, two additional Ca2+-binding sites mediate intermolecular interactions
Mg2+
-
required for activity (5 mM)
Mg2+
-, D5LIR7
can partially substitute for Mn2+
Mn2+
-
maximal activity at 0.2 mM Mn2+
Mn2+
-
activity strictly depending on Mn2+
Mn2+
-, D5LIR7
required, active site metal ion
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3,3-difluorooxalacetate
-, D5LIR7
a mechanism-based inhibitor that binds in a gem-diol form analogous to the oxalacetate intermediate/transition state, binding structure, overview
-
3,3-difluorooxaloacetate
Q7Z986
-
3,3-difluorooxaloacetate
-
-
oxalate
-
competitive inhibition
oxalate
-
weak binding competitive inhibitor
Phosphonopyruvate
-
-
3,3-difluoroxaloacetate
-
tight binding competitive inhibitor
additional information
-
(2R,3S)-isocitrate, (R)-malate, (S)-malate, and carboxyphosphoenolpyruvate are not inhibitors
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
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 25C)
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
-, D5LIR7
in presence of Mg2+, pH 7.5, 25C
0.15
-
oxaloacetate
-
mutant S260P, trial 1
0.17
-
oxaloacetate
-
-
0.22
-
oxaloacetate
-
-
0.22
-
oxaloacetate
-
mutant S260P, trial 2
0.22
-
oxaloacetate
-
wild type enzyme, in 50 mM K+-HEPES (pH 7.5 and 25C)
0.234
-
oxaloacetate
-
wild type enzyme, in 0.1 M imidazole (pH 7.6 and 25C)
0.24
-
oxaloacetate
-
cofactor Mn2+, buffer imidazole
0.48
-
oxaloacetate
-, D5LIR7
in presence of Mn2+, pH 7.5, 25C
0.7
-
oxaloacetate
-
mutant S260A, trial 1
0.84
-
oxaloacetate
-
mutant S257P
1
2
oxaloacetate
-
-
1.11
-
oxaloacetate
-
mutant enzyme P240S, in 50 mM K+-HEPES (pH 7.5 and 25C)
1.22
-
oxaloacetate
-
mutant enzyme P240T, in 50 mM K+-HEPES (pH 7.5 and 25C)
1.248
-
oxaloacetate
-, D5LIR7
in presence of Ca2+, pH 7.5, 25C
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 25C)
0.021
-
Mn2+
-
-
additional information
-
additional information
-, D5LIR7
steady-state kinetic constants for divalent metal-activated OAH from
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
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 25C)
0.081
-
oxaloacetate
-
mutant enzyme C124S, in 50 mM K+-HEPES (pH 7.5 and 25C)
0.082
-
oxaloacetate
-
mutant enzyme P240T, in 50 mM K+-HEPES (pH 7.5 and 25C)
0.125
-
oxaloacetate
-
mutant enzyme C124A, in 50 mM K+-HEPES (pH 7.5 and 25C)
0.35
-
oxaloacetate
-
cofactor Ca2+, buffer imidazole
0.357
-
oxaloacetate
-
mutant enzyme P240S, in 50 mM K+-HEPES (pH 7.5 and 25C)
0.48
-
oxaloacetate
-
wild type enzyme, in 50 mM K+-HEPES (pH 7.5 and 25C)
0.505
-
oxaloacetate
-
wild type enzyme, in 0.1 M imidazole (pH 7.6 and 25C)
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
-, D5LIR7
in presence of Ca2+, pH 7.5, 25C
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
-, D5LIR7
in presence of Mg2+, pH 7.5, 25C
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
-, D5LIR7
in presence of Mn2+, pH 7.5, 25C
37
-
oxaloacetate
-
cofactor Mn2+, buffer imidazole
50
-
oxaloacetate
-
cofactor Mn2+, buffer imidazole
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2
-
oxaloacetate
-
wild type enzyme, in 0.1 M imidazole (pH 7.6 and 25C); wild type enzyme, in 50 mM K+-HEPES (pH7.5 and 25C)
14857
70000
-
oxaloacetate
-
mutant enzyme P240T, in 50 mM K+-HEPES (pH 7.5 and 25C)
14857
300000
-
oxaloacetate
-
mutant enzyme P240S, in 50 mM K+-HEPES (pH 7.5 and 25C)
14857
900000
-
oxaloacetate
-
mutant enzyme C124A, in 50 mM K+-HEPES (pH 7.5 and 25C)
14857
3000000
-
oxaloacetate
-
mutant enzyme C124S, in 50 mM K+-HEPES (pH 7.5 and 25C)
14857
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.000068
-
3,3-difluorooxaloacetate
-
-
0.0025
-
3,3-difluoroxaloacetate
-
in 50 mM K+-HEPES (pH 7.5 and 25C)
1.6
-
oxalate
-
in 50 mM K+-HEPES (pH 7.5 and 25C)
0.0024
-
Phosphonopyruvate
-
in 50 mM K+-HEPES (pH 7.5 and 25C)
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.3
-
-
specific activity determined for fungus grown for 4 days on ammonium tartrate-containing medium
0.62
-
-
cell extract
4.6
-
-
purification step ammonium sulfate precipitation
15
-
-
purification step DEAE-cellulose column
20
-
-
purification step butyl-Sepharose column
58
-
-
partially purified enzyme
additional information
-
-
relative activity, supernatant fraction obtained from centrifugation at 3000 g 100%, supernatant at 20000 g 70%, pellet 10% activity
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
-
-
assay at
7.5
-
-, D5LIR7
assay at
7.6
-
-
in imidazol buffer
7.6
-
-
oxaloacetate hydrolase assay
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
9
-
in MES, piperazine-N,N'-bis(2-ethansulfonic acid), Tris and triethanolamine
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
oxaloacetate hydrolase assay
25
-
-, D5LIR7
assay at
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
34360
-
-
theoretical molecular mass
35000
-
-
determined by SDS-PAGE
100000
-
-
determined by gel filtration, indicative of a homotrimeric quaternary structure
110000
-
-
gel filtration
250000
-
-
gel filtration
360000
440000
-
two major bands, native PAGE
420000
-
-
zonal centrifugation
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oligomer
-
10-12 * 39000, SDS-PAGE
tetramer
-, D5LIR7
OAH assembles into a dimer of dimers with each subunit exhibiting an (alpha/beta)8 barrel fold and each pair swapping the 8th alpha-helix
homotetramer
-
4 * 31986, mass spectrometry; 4 * 32000, SDS-PAGE; 4 * 32117, calculated from amino acid sequence
additional information
-
the results are consistent with the existence of a monomer-dimer-tetramer equilibrium
additional information
-, D5LIR7
an active site gating loop exhibits conformational disorder in the ligand-free structure
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
DMML in complex with Mg2+ and in complex with Mg2+ and 3,3-difluorooxalacetate, hanging drop vapor diffusion method, using 0.2 M potassium thiocyanate, 0.1 M bis-Tris propane (pH 7.5), and 20k polyethylene glycol 3350, or using 14k polyethylene glycol 6000 and 0.1 M MES (pH 6.5)
-
OAH alone, in complex with a inhibitor 3,3-difluorooxalacetate, and in complex with reaction product oxalate, soaking of ligand-free OAH crystals in solution containing 0.2 M MnCl2 or 0.2 M MgCl2, 10 mM CaCl2, 2 mM 3,3-difluorooxalacetate, 0.1 M Na-HEPES, pH 7.5, and 30% v/v PEG 400 for 5-10 min yielded the desired enzyme inhibitor complex, X-ray diffraction structure determination and analysis at resolution limit of 1.30, 1.55, and 1.65 A , respectively, molecular replacement
-, D5LIR7
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.8
-
-
loss of activity below
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
unstable if Mn2+ concentration is low
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-18C, lyophilized, 3 months
-
4C, 50 mM Tris-HCL, pH 7.5, 2 mM MnCl2, 20 mM DTT 5% sucrose, 7 days
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Phenyl Sepharose, Q-Sepharose
-
Q-Sepharose column chromatography, ammonium sulfate precipitation, butyl Sepharose column chromatography, and phenyl Sepharose column chromatography
-
by ammonium sulfate-induced protein precipitation, and by using of a DEAE-cellulose and a butyl-Sepharose column
-
proteins are purified to homogeneity
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
cloned by inverse PCR into Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
-
into the vector pGEM-T Easy for sequencing
Q7Z986
into the vector pET-3c
-
into the vector pGEM-T Easy for sequencing, and into pET-3c for expression in Escherichia coli BL21DE3 cells
-
into the vector pET-3c
-
gene Pc22g24830, DNA and amino acid sequence determination and analysis, cloning in Escherichia coli strain DH5alpha, functional expression in Saccharomyces cerevisiae strain IME043, IME046, and IME047
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C124A
-
the mutant shows decreased kcat compared to the wild type enzyme
C124S
-
the mutant shows decreased kcat compared to the wild type enzyme
D59A
-
the mutant shows decreased kcat compared to the wild type enzyme
D59S
-
the mutant shows decreased kcat compared to the wild type enzyme
P240S
-
the mutant shows decreased kcat compared to the wild type enzyme
P240T
-
the mutant shows decreased kcat compared to the wild type enzyme
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
food industry
Q7Z986
oxalate toxicity is a concern for the commercial application of fungi in the food and drug industries
food industry
-
oxalate toxicity is a concern for the commercial application of fungi in the food and drug industries
agriculture
-
oxalate production by Moniliophthora perniciosa may play a role in the Witches' Broom disease pathogenesis mechanism