BRENDA - Enzyme Database
show all sequences of 4.1.1.112

Structure and function of PA4872 from Pseudomonas aeruginosa, a novel class of oxaloacetate decarboxylase from the PEP mutase/isocitrate lyase superfamily

Narayanan, B.C.; Niu, W.; Han, Y.; Zou, J.; Mariano, P.S.; Dunaway-Mariano, D.; Herzberg, O.; Biochemistry 47, 167-182 (2008)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
expressed in Escherichia coli BL21 (DE3) cells
Pseudomonas aeruginosa
Crystallization (Commentary)
Crystallization (Commentary)
Organism
hanging drop vapour diffusion method, aliquots of 10 mg/ml protein in 5 mM MgCl2, 5 mM phosphonopyruvate and 10 mM NaHEPES (pH 7.0) mixed with equal volumes of reservoir solution containing 12% polyethylene glycol 20000 and 0.1 M MES (pH 6.0)
Pseudomonas aeruginosa
Engineering
Protein Variants
Commentary
Organism
H235A
the kcat value for catalysis of oxaloacetate decarboxylation is less than an order of magnitude smaller compared to the wild type enzyme
Pseudomonas aeruginosa
H235Q
the kcat value for catalysis of oxaloacetate decarboxylation is less than an order of magnitude smaller compared to the wild type enzyme
Pseudomonas aeruginosa
Y212F
25fold reduction of the Km value compared to the wild type enzyme
Pseudomonas aeruginosa
Inhibitors
Inhibitors
Commentary
Organism
Structure
3,3-difluoroxaloacetate
-
Pseudomonas aeruginosa
Acetopyruvate
-
Pseudomonas aeruginosa
alpha-ketovalerate
-
Pseudomonas aeruginosa
oxalate
-
Pseudomonas aeruginosa
Phosphonopyruvate
-
Pseudomonas aeruginosa
pyruvate
-
Pseudomonas aeruginosa
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.087
-
oxaloacetate
mutant enzyme Y212F, in 0.2 mM NADH, 5 mM MgCl2 and 50 mM K+HEPES (pH 7.5), at 25C
Pseudomonas aeruginosa
0.63
-
3-methyloxaloacetate
wild type enzyme, in 0.2 mM NADH, 5 mM MgCl2 and 50 mM K+HEPES (pH 7.5), at 25C
Pseudomonas aeruginosa
1.02
-
oxaloacetate
mutant enzyme H235A, in 0.2 mM NADH, 5 mM MgCl2 and 50 mM K+HEPES (pH 7.5), at 25C
Pseudomonas aeruginosa
2.2
-
oxaloacetate
wild type enzyme, in 0.2 mM NADH, 5 mM MgCl2 and 50 mM K+HEPES (pH 7.5), at 25C
Pseudomonas aeruginosa
2.5
-
oxaloacetate
mutant enzyme H235Q, in 0.2 mM NADH, 5 mM MgCl2 and 50 mM K+HEPES (pH 7.5), at 25C
Pseudomonas aeruginosa
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
cofactor
Pseudomonas aeruginosa
Organism
Organism
UniProt
Commentary
Textmining
Pseudomonas aeruginosa
Q9HUU1
-
-
Purification (Commentary)
Purification (Commentary)
Organism
DEAE-cellulose column chromatography, phenyl-Sepharose columnn chromatography, and butyl-Sepharose column chromatography
Pseudomonas aeruginosa
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
3-methyloxaloacetate
-
678331
Pseudomonas aeruginosa
2-oxobutanoate + CO2
-
-
-
?
Oxaloacetate
-
678331
Pseudomonas aeruginosa
Pyruvate + CO2
-
-
-
r
Subunits
Subunits
Commentary
Organism
dimer
dimer of dimers, X-ray crystallography
Pseudomonas aeruginosa
Synonyms
Synonyms
Commentary
Organism
PA4872
member of the PEP mutase/isocitrate lyase superfamily
Pseudomonas aeruginosa
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
250
-
3-methyloxaloacetate
in 0.2 mM NADH, 5 mM MgCl2 and 50 mM K+HEPES (pH 7.5), at 25C
Pseudomonas aeruginosa
7500
-
oxaloacetate
in 0.2 mM NADH, 5 mM MgCl2 and 50 mM K+HEPES (pH 7.5), at 25C
Pseudomonas aeruginosa
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.043
-
oxalate
-
Pseudomonas aeruginosa
0.45
-
3,3-difluoroxaloacetate
-
Pseudomonas aeruginosa
1.09
-
Acetopyruvate
-
Pseudomonas aeruginosa
3
-
Phosphonopyruvate
-
Pseudomonas aeruginosa
6.7
-
alpha-ketovalerate
-
Pseudomonas aeruginosa
7.2
-
pyruvate
-
Pseudomonas aeruginosa
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli BL21 (DE3) cells
Pseudomonas aeruginosa
Crystallization (Commentary) (protein specific)
Crystallization
Organism
hanging drop vapour diffusion method, aliquots of 10 mg/ml protein in 5 mM MgCl2, 5 mM phosphonopyruvate and 10 mM NaHEPES (pH 7.0) mixed with equal volumes of reservoir solution containing 12% polyethylene glycol 20000 and 0.1 M MES (pH 6.0)
Pseudomonas aeruginosa
Engineering (protein specific)
Protein Variants
Commentary
Organism
H235A
the kcat value for catalysis of oxaloacetate decarboxylation is less than an order of magnitude smaller compared to the wild type enzyme
Pseudomonas aeruginosa
H235Q
the kcat value for catalysis of oxaloacetate decarboxylation is less than an order of magnitude smaller compared to the wild type enzyme
Pseudomonas aeruginosa
Y212F
25fold reduction of the Km value compared to the wild type enzyme
Pseudomonas aeruginosa
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
3,3-difluoroxaloacetate
-
Pseudomonas aeruginosa
Acetopyruvate
-
Pseudomonas aeruginosa
alpha-ketovalerate
-
Pseudomonas aeruginosa
oxalate
-
Pseudomonas aeruginosa
Phosphonopyruvate
-
Pseudomonas aeruginosa
pyruvate
-
Pseudomonas aeruginosa
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.043
-
oxalate
-
Pseudomonas aeruginosa
0.45
-
3,3-difluoroxaloacetate
-
Pseudomonas aeruginosa
1.09
-
Acetopyruvate
-
Pseudomonas aeruginosa
3
-
Phosphonopyruvate
-
Pseudomonas aeruginosa
6.7
-
alpha-ketovalerate
-
Pseudomonas aeruginosa
7.2
-
pyruvate
-
Pseudomonas aeruginosa
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.087
-
oxaloacetate
mutant enzyme Y212F, in 0.2 mM NADH, 5 mM MgCl2 and 50 mM K+HEPES (pH 7.5), at 25C
Pseudomonas aeruginosa
0.63
-
3-methyloxaloacetate
wild type enzyme, in 0.2 mM NADH, 5 mM MgCl2 and 50 mM K+HEPES (pH 7.5), at 25C
Pseudomonas aeruginosa
1.02
-
oxaloacetate
mutant enzyme H235A, in 0.2 mM NADH, 5 mM MgCl2 and 50 mM K+HEPES (pH 7.5), at 25C
Pseudomonas aeruginosa
2.2
-
oxaloacetate
wild type enzyme, in 0.2 mM NADH, 5 mM MgCl2 and 50 mM K+HEPES (pH 7.5), at 25C
Pseudomonas aeruginosa
2.5
-
oxaloacetate
mutant enzyme H235Q, in 0.2 mM NADH, 5 mM MgCl2 and 50 mM K+HEPES (pH 7.5), at 25C
Pseudomonas aeruginosa
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
cofactor
Pseudomonas aeruginosa
Purification (Commentary) (protein specific)
Commentary
Organism
DEAE-cellulose column chromatography, phenyl-Sepharose columnn chromatography, and butyl-Sepharose column chromatography
Pseudomonas aeruginosa
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
3-methyloxaloacetate
-
678331
Pseudomonas aeruginosa
2-oxobutanoate + CO2
-
-
-
?
Oxaloacetate
-
678331
Pseudomonas aeruginosa
Pyruvate + CO2
-
-
-
r
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
dimer of dimers, X-ray crystallography
Pseudomonas aeruginosa
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
250
-
3-methyloxaloacetate
in 0.2 mM NADH, 5 mM MgCl2 and 50 mM K+HEPES (pH 7.5), at 25C
Pseudomonas aeruginosa
7500
-
oxaloacetate
in 0.2 mM NADH, 5 mM MgCl2 and 50 mM K+HEPES (pH 7.5), at 25C
Pseudomonas aeruginosa
Other publictions for EC 4.1.1.112
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
Synonyms
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)
748206
Pircher
Identification of FAH domain- ...
Homo sapiens
J. Biol. Chem.
290
6755-6762
2015
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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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2
1
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726821
Lietzan
Functionally diverse biotin-de ...
Klebsiella aerogenes, Vibrio cholerae serotype O1
Arch. Biochem. Biophys.
544
75-86
2014
-
-
-
-
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2
2
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4
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5
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2
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3
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4
3
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5
5
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726737
Repizo
Biochemical and genetic charac ...
Enterococcus faecalis, Enterococcus faecalis JH2-2
Appl. Environ. Microbiol.
79
2882-2890
2013
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1
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1
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3
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2
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9
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1
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1
1
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2
1
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1
1
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713674
Ran
Expression, purification, crys ...
Corynebacterium glutamicum
Acta Crystallogr. Sect. F
67
968-970
2011
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1
1
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2
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1
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714979
Espariz
Identification of malic and so ...
Enterococcus faecalis
FEBS J.
278
2140-2151
2011
-
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1
-
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10
1
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1
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1
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1
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2
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1
1
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1
1
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10
-
1
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1
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1
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1
-
-
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1
1
1
-
-
-
2
2
-
1
1
715662
Balsera
Quaternary structure of the ox ...
Vibrio cholerae serotype O1
J. Biol. Chem.
286
9457-9467
2011
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1
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1
1
1
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2
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1
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1
1
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-
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704327
Klaffl
Genetic and functional analysi ...
Corynebacterium glutamicum
J. Bacteriol.
192
2604-2612
2010
-
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1
1
1
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3
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2
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1
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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
-
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-
716673
Granjon
Structure-function relations i ...
Vibrio cholerae serotype O1
PLoS ONE
5
e10935
2010
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1
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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
1
-
-
-
678331
Narayanan
Structure and function of PA48 ...
Pseudomonas aeruginosa
Biochemistry
47
167-182
2008
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1
1
3
-
6
5
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1
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3
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1
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2
1
1
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2
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6
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6
6
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1
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2
1
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2
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692317
Dharmarajan
Tyr235 of human cytosolic phos ...
Homo sapiens
FEBS J.
275
5810-5819
2008
-
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1
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3
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2
1
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692806
Augagneur
Mutation of the oxaloacetate d ...
Lactococcus lactis
J. Appl. Microbiol.
104
260-268
2008
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692884
Blancato
Transcriptional regulation of ...
Enterococcus faecalis
J. Bacteriol.
190
7419-7430
2008
1
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681424
Studer
Crystal structure of the carbo ...
Vibrio cholerae serotype O1
J. Mol. Biol.
367
547-557
2007
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1
10
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10
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679954
Kim
-
Determining citrate in fruit j ...
Pseudomonas sp.
Food Chem.
99
851-857
2006
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1
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663796
Dahinden
Oxaloacetate decarboxylase of ...
Vibrio cholerae, Vibrio cholerae O395-N1
Arch. Microbiol.
183
121-129
2005
-
-
1
-
-
-
2
-
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1
1
2
-
15
-
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1
-
1
1
1
-
2
1
6
-
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2
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2
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1
1
2
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1
1
1
1
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
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-
664904
Dahinden
Identification of a domain in ...
Vibrio cholerae serotype O1
FEBS J.
272
846-855
2005
-
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1
-
-
-
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2
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1
2
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1
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1
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663795
Dahinden
Oxaloacetate decarboxylase of ...
Archaeoglobus fulgidus
Arch. Microbiol.
182
414-420
2004
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1
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4
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664936
Sender
Characterization of an oxaloac ...
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Mitochondrial oxaloacetate dec ...
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