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Information on EC 4.1.1.112 - oxaloacetate decarboxylase
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EC Tree
4.1.1.112 oxaloacetate decarboxylaseIUBMB Comments
Requires a divalent metal cation. The enzymes from the fish Gadus morhua (Atlantic cod) and the bacterium Micrococcus luteus prefer Mn2+, while those from the bacteria Pseudomonas putida and Pseudomonas aeruginosa prefer Mg2+. Unlike EC 7.2.4.2 [oxaloacetate decarboxylase (Na+ extruding)], there is no evidence of the enzyme's involvement in Na+ transport.
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Word Map
- 4.1.1.112
-
klebsiella
- biotin
- carboxybiotin
-
biotin-containing
-
avidin-sepharose
- carboxyltransferase
-
biotin-dependent
- transcarboxylase
-
citps
- modestum
- synthesis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
oxaloacetate decarboxylase, fahd1, oxalacetate decarboxylase, oxaloacetate decarboxylase na+ pump, oad-2, oad-1, pa4872, fah domain-containing protein 1, oxaloacetate carboxylyase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CitM
EC 4.1.1.3
-
-
formerly, part transferred
-
OAD
OAD-1
OAD-2
OADC
ODx
Oxalacetate decarboxylase
-
-
-
-
Oxalacetic acid decarboxylase
-
-
-
-
Oxalacetic beta-decarboxylase
-
-
-
-
Oxalacetic carboxylase
-
-
-
-
Oxalate beta-decarboxylase
-
-
-
-
oxaloacetate carboxylase Na+ pump
-
membrane-bound multiprotein complex that couples oxaloacetate decarboxylation to sodium ion transport across the membrane
Oxaloacetate carboxylyase
-
-
-
-
oxaloacetate decarboxylase Na+ pump
oxaloacetate decarboxylase OAD-1
oxaloacetate decarboxylase OAD-2
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
oxaloacetate = pyruvate + CO2
catalytic mechanism, overview. Carboxybiotin transits to the membrane-bound beta-subunit where it is decarboxylated to biotin and CO2 in a reaction that consumes a periplasmic proton and is coupled to Na+ translocation from the cytoplasm to the periplasm. The reaction is initiated by the enzyme-catalyzed decarboxylation of oxaloacetate in the carboxyltransferase domain of the alpha-subunit, yielding pyruvate and carboxybiotin. Subsequently, the C-terminal biotin carboxyl carrier protein domain on the alpha-subunit translocates to the beta-subunit where its decarboxylation is coupled to Na+ translocation. The OADC pump is reversible: at high concentrations of extracellular Na+, the pump will couple the downhill movement of Na+ into the cytosol with the carboxylation of pyruvate, to form oxaloacetate
-
oxaloacetate = pyruvate + CO2
catalytic mechanism, overview. Carboxybiotin transits to the membrane-bound beta-subunit where it is decarboxylated to biotin and CO2 in a reaction that consumes a periplasmic proton and is coupled to Na+ translocation from the cytoplasm to the periplasm. The reaction is initiated by the enzyme-catalyzed decarboxylation of oxaloacetate in the carboxyltransferase domain of the alpha-subunit, yielding pyruvate and carboxybiotin. Subsequently, the C-terminal biotin carboxyl carrier protein domain on the alpha-subunit translocates to the beta-subunit where its decarboxylation is coupled to Na+ translocation. The OADC pump is reversible: at high concentrations of extracellular Na+, the pump will couple the downhill movement of Na+ into the cytosol with the carboxylation of pyruvate, to form oxaloacetate
-
oxaloacetate = pyruvate + CO2
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxylation
-
-
-
-
decarboxylation
decarboxylation
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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SYSTEMATIC NAME
IUBMB Comments
oxaloacetate carboxy-lyase (pyruvate-forming)
Requires a divalent metal cation. The enzymes from the fish Gadus morhua (Atlantic cod) and the bacterium Micrococcus luteus prefer Mn2+, while those from the bacteria Pseudomonas putida and Pseudomonas aeruginosa prefer Mg2+. Unlike EC 7.2.4.2 [oxaloacetate decarboxylase (Na+ extruding)], there is no evidence of the enzyme's involvement in Na+ transport.
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CAS REGISTRY NUMBER
COMMENTARY
9024-98-0
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Oxaloacetate
Pyruvate + CO2
bi-functional enzyme displaying both acylpyruvate hydrolase and oxaloacetate decarboxylase activity
-
-
?
Oxaloacetate
Pyruvate + CO2
-
one Na+ is transported into the periplasm and one H+ is transported into the cytoplasm during the reaction
-
?
Oxaloacetate
Pyruvate + CO2
-
two Na+ are transported into the periplasm and one H+ is transported into the cytoplasm during the reaction
-
?
Oxaloacetate
Pyruvate + CO2
-
one Na+ is transported into the periplasm and one H+ is transported into the cytoplasm during the reaction
-
?
additional information
?
-
-
decarboxylation and sodium transport by the biotin-dependent oxaloacetate decarboxylase complex, overview
-
-
?
additional information
?
-
after reconstitution into proteoliposomes, the enzyme acts as a Na+ pump
-
-
?
additional information
?
-
after reconstitution into proteoliposomes, the enzyme acts as a Na+ pump
-
-
?
additional information
?
-
after reconstitution into proteoliposomes, the enzyme acts as a Na+ pump
-
-
?
additional information
?
-
after reconstitution into proteoliposomes, the enzyme acts as a Na+ pump
-
-
?
additional information
?
-
after reconstitution into proteoliposomes, the enzyme acts as a Na+ pump
-
-
?
additional information
?
-
after reconstitution into proteoliposomes, the enzyme acts as a Na+ pump
-
-
?
additional information
?
-
-
after reconstitution into proteoliposomes, the enzyme acts as a Na+ pump
-
-
?
additional information
?
-
after reconstitution into proteoliposomes, the enzyme acts as a Na+ pump
-
-
?
additional information
?
-
after reconstitution into proteoliposomes, the enzyme acts as a Na+ pump
-
-
?
additional information
?
-
after reconstitution into proteoliposomes, the enzyme acts as a Na+ pump
-
-
?
additional information
?
-
after reconstitution into proteoliposomes, the enzyme acts as a Na+ pump
-
-
?
additional information
?
-
after reconstitution into proteoliposomes, the enzyme acts as a Na+ pump
-
-
?
additional information
?
-
after reconstitution into proteoliposomes, the enzyme acts as a Na+ pump
-
-
?
additional information
?
-
-
decarboxylation and sodium transport by the biotin-dependent oxaloacetate decarboxylase complex, overview
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Oxaloacetate
Pyruvate + CO2
-
one Na+ is transported into the periplasm and one H+ is transported into the cytoplasm during the reaction
-
?
Oxaloacetate
Pyruvate + CO2
-
two Na+ are transported into the periplasm and one H+ is transported into the cytoplasm during the reaction
-
?
Oxaloacetate
Pyruvate + CO2
-
one Na+ is transported into the periplasm and one H+ is transported into the cytoplasm during the reaction
-
?
additional information
?
-
-
decarboxylation and sodium transport by the biotin-dependent oxaloacetate decarboxylase complex, overview
-
-
?
additional information
?
-
after reconstitution into proteoliposomes, the enzyme acts as a Na+ pump
-
-
?
additional information
?
-
after reconstitution into proteoliposomes, the enzyme acts as a Na+ pump
-
-
?
additional information
?
-
after reconstitution into proteoliposomes, the enzyme acts as a Na+ pump
-
-
?
additional information
?
-
after reconstitution into proteoliposomes, the enzyme acts as a Na+ pump
-
-
?
additional information
?
-
after reconstitution into proteoliposomes, the enzyme acts as a Na+ pump
-
-
?
additional information
?
-
after reconstitution into proteoliposomes, the enzyme acts as a Na+ pump
-
-
?
additional information
?
-
-
after reconstitution into proteoliposomes, the enzyme acts as a Na+ pump
-
-
?
additional information
?
-
after reconstitution into proteoliposomes, the enzyme acts as a Na+ pump
-
-
?
additional information
?
-
after reconstitution into proteoliposomes, the enzyme acts as a Na+ pump
-
-
?
additional information
?
-
after reconstitution into proteoliposomes, the enzyme acts as a Na+ pump
-
-
?
additional information
?
-
after reconstitution into proteoliposomes, the enzyme acts as a Na+ pump
-
-
?
additional information
?
-
after reconstitution into proteoliposomes, the enzyme acts as a Na+ pump
-
-
?
additional information
?
-
after reconstitution into proteoliposomes, the enzyme acts as a Na+ pump
-
-
?
additional information
?
-
-
decarboxylation and sodium transport by the biotin-dependent oxaloacetate decarboxylase complex, overview
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
biotin
-
dependent on, the enzyme utilizes a carboxyltransferase domain to catalyze the biotin-dependent decarboxylation of oxaloacetate
biotin
-
dependent on, the enzyme utilizes a carboxyltransferase domain to catalyze the biotin-dependent decarboxylation of oxaloacetate
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Mg2+
Mn2+
Na+
Ni2+
Zn2+
Mn2+
the enzyme is dependent on divalent metal ions with 100% activity at 20 mM Mn2+
Mn2+
-
or Mg2+, absolutely required, Km-value 0.02 mM, inhibitory above 0.46 mM
Zn2+
-
bound at the gamma-subunit, coordinated by several residues at the hydrophilic C-terminus
Zn2+
-
bound at the gamma-subunit, coordinated by several residues at the hydrophilic C-terminus
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
-
carboxylation competitively inhibited, decarboxylation non-competitively, Ki: 2.2 mM, possibly involved in regulation
citrate
-
0.5 mM inhibitor or 2 mM inhibitor in presence of 10 mM Mn2+, 24% inhibition
NaCl
-
OAD tertiary structure is sensitive to the presence of NaCl
oxalate
half-maximal inhibition at 0.01 mM
oxomalonate
half-maximal inhibition at 0.2 mM
oxomalonate
-
competitive inhibitor of OAD with respect to oxaloacetate
p-hydroxymercuribenzoate
-
complete inactivation after preincubation at 0.2 mM
additional information
-
no effect is observed after addition of ADP (2.4 mM), GDP (3.6 mM), or succinate (5.6 mM) or after addition of phosphoenolpyruvate, L-fructose-6-phosphate, L-fructose-1,6-bisphosphate, L-malate, acetate, citrate, fumarate, L-aspartate, or acetyl coenzyme A (5 mM each)
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Chagas Disease
Crystal structure of the dimeric phosphoenolpyruvate carboxykinase (PEPCK) from Trypanosoma cruzi at 2 A resolution.
Infections
[Study on the value of mitochondrial associated protein fumarylacetoacetate domain containing protein 1 and growth differentiation factor-15 in the diagnosis of sepsis: test results from the patients of a multicenter study].
oxaloacetate decarboxylase deficiency
Oxalacetic carboxylase deficiency of the succinate-requiring mutants of Neurospora crassa.
Pneumonia
The sodium ion translocating oxaloacetate decarboxylase of Klebsiella pneumoniae. Sequence of the integral membrane-bound subunits beta and gamma.
Sepsis
[Study on the value of mitochondrial associated protein fumarylacetoacetate domain containing protein 1 and growth differentiation factor-15 in the diagnosis of sepsis: test results from the patients of a multicenter study].
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.63
3-methyloxaloacetate
wild type enzyme, in 0.2 mM NADH, 5 mM MgCl2 and 50 mM K+HEPES (pH 7.5), at 25°C
0.0003
oxaloacetate
-
Y235A mutant, Vmax = 0.2 micromol/min/mg. In the presence of GDP
0.0003
oxaloacetate
-
Y235S mutant, Vmax = 0.1 micromol/min/mg. In the presence of GDP
0.0004
oxaloacetate
-
wild-type, Vmax = 3 micromol/min/mg. In the presence of GDP
0.0004
oxaloacetate
-
Y235F mutant, Vmax = 3 micromol/min/mg. In the presence of GDP
0.087
oxaloacetate
mutant enzyme Y212F, in 0.2 mM NADH, 5 mM MgCl2 and 50 mM K+HEPES (pH 7.5), at 25°C
0.62
oxaloacetate
calculated value at pH 4.5, temperature not specified in the publication
1.02
oxaloacetate
mutant enzyme H235A, in 0.2 mM NADH, 5 mM MgCl2 and 50 mM K+HEPES (pH 7.5), at 25°C
1.39
oxaloacetate
-
in 100 mM Tris-HCl (pH 7.3), 10 mM MgCl2, 2.5 mM EDTA, at 30°C
2.2
oxaloacetate
wild type enzyme, in 0.2 mM NADH, 5 mM MgCl2 and 50 mM K+HEPES (pH 7.5), at 25°C
2.5
oxaloacetate
mutant enzyme H235Q, in 0.2 mM NADH, 5 mM MgCl2 and 50 mM K+HEPES (pH 7.5), at 25°C
additional information
additional information
-
positive cooperativity for oxaloacetate
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
250
3-methyloxaloacetate
in 0.2 mM NADH, 5 mM MgCl2 and 50 mM K+HEPES (pH 7.5), at 25°C
11.2
oxaloacetate
calculated value at pH 4.5, temperature not specified in the publication
104
oxaloacetate
-
in 100 mM Tris-HCl (pH 7.3), 10 mM MgCl2, 2.5 mM EDTA, at 30°C
7500
oxaloacetate
in 0.2 mM NADH, 5 mM MgCl2 and 50 mM K+HEPES (pH 7.5), at 25°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
22.3
oxaloacetate
calculated value at pH 4.5, temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Ki-values given for inhibition with NaCl for all mutant enzymes at 3-4 different pH
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5 - 5.5
-
pH 3.5: about 55% of maximal activity, pH 5.5: about 40% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
oxaloacetate decarboxylase OAD-1, alpha subunit; O395-N1
SwissProt
brenda
oxaloacetate decarboxylase OAD-1, beta subunit; O395-N1
SwissProt
brenda
oxaloacetate decarboxylase OAD-1, gamma subunit; O395-N1
SwissProt
brenda
oxaloacetate decarboxylase OAD-2, alpha subunit; O395-N1
SwissProt
brenda
oxaloacetate decarboxylase OAD-2, beta subunit; O395-N1
SwissProt
brenda
oxaloacetate decarboxylase OAD-2, gamma subunit; O395-N1
SwissProt
brenda
oxaloacetate decarboxylase OAD-1, alpha subunit; O395-N1
SwissProt
brenda
oxaloacetate decarboxylase OAD-1, beta subunit; O395-N1
SwissProt
brenda
oxaloacetate decarboxylase OAD-1, gamma subunit; O395-N1
SwissProt
brenda
oxaloacetate decarboxylase OAD-2, alpha subunit; O395-N1
SwissProt
brenda
oxaloacetate decarboxylase OAD-2, beta subunit; O395-N1
SwissProt
brenda
oxaloacetate decarboxylase OAD-2, gamma subunit; O395-N1
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
upon anaerobic growth of Vibrio cholerae on citrate, exclusivle the oad-2 gene is expressed
brenda
-
upon anaerobic growth of Vibrio cholerae on citrate, exclusivle the oad-2 gene is expressed
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
subunits Ef-A, Ef-D, and Ef-H form a cytoplasmic soluble complex, Ef-AHD, which is also associated with the membrane
brenda
-
subunits Ef-A, Ef-D, and Ef-H form a cytoplasmic soluble complex, Ef-AHD, which is also associated with the membrane
-
brenda
-
Ef-B is a membrane-bound subunit, while subunits Ef-A, Ef-D, and Ef-H form a cytoplasmic soluble complex, Ef-AHD, which is also associated with the membrane
brenda
-
Ef-B is a membrane-bound subunit, while subunits Ef-A, Ef-D, and Ef-H form a cytoplasmic soluble complex, Ef-AHD, which is also associated with the membrane
-
brenda
-
membrane-bound oxaloacetate decarboxylase complex, the alpha-subunit is a peripheral membrane protein on the cytosolic side of the membrane, where it associates with beta- and gamma-subunits that are embedded in the membrane. The beta-subunit is an integral membrane protein with nine transmembrane segments. The small gamma-subunit is an integral membrane protein with a single membrane-spanning helix at the N-terminus
brenda
-
beta and gamma subunits are integral membrane proteins, alpha subunit is attached to the gamma subunit
brenda
-
membrane-bound oxaloacetate decarboxylase complex, the alpha-subunit is a peripheral membrane protein on the cytosolic side of the membrane, where it associates with beta- and gamma-subunits that are embedded in the membrane. The beta-subunit is an integral membrane protein with nine transmembrane segments. The small gamma-subunit is an integral membrane protein with a single membrane-spanning helix at the N-terminus
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
-
the enzyme belongs to the class II decarboxylases of the biotin-dependent enzyme family. Class II enzymes facilitate sodium transport from the cytoplasm to the periplasm in some archaea and anaerobic bacteria
evolution
-
the enzyme belongs to the class II decarboxylases of the biotin-dependent enzyme family. Class II enzymes facilitate sodium transport from the cytoplasm to the periplasm in some archaea and anaerobic bacteria
malfunction
-
inactivation of the odx gene does not improve L-lysine production
malfunction
the citrate fermentation phenotype is not affected by citM deletion
metabolism
CitM is not required for efficient citrate utilization
metabolism
-
OAD of Vibrio cholerae catalyses a key step in citrate fermentation, converting the chemical energy of the decarboxylation reaction into an electrochemical gradient of Na+ ions across the membrane, which drives endergonic membrane reactions such as ATP synthesis, transport and motility
metabolism
the enzyme is important for mitochondrial function. It acts antagonistically to pyruvate carboxylase, a key metabolic enzyme
physiological function
-
presence of the membrane-bound Ef-B subunit is required for full alkalinization of the internal medium of Enterococcus faecalis cells during citrate fermentation
physiological function
-
the membrane-bound oxaloacetate decarboxylase complex of Klebsiella aerogenes catalyzes the biotin-dependent decarboxylation of oxaloacetate, while also serves as a primary Na+ pump. The enzyme complex plays an essential role in the citrate or tartrate fermentation pathways of certain archaea and bacteria, contributing to the generation of an electrochemical gradient of Na+ ions along with one mol of ATP per mol of citrate/tartrate. The resulting Na+ gradient is used to power the import of nutrients and the synthesis of ATP
physiological function
-
presence of the membrane-bound Ef-B subunit is required for full alkalinization of the internal medium of Enterococcus faecalis cells during citrate fermentation
-
additional information
-
oxaloacetate decarboxylase complex structure, modeling, overview. The gamma-subunit is essential for the overall stability of the complex, and likely serves as an anchor to hold the alpha- and beta-subunits in place. The gamma-subunit significantly accelerates the rate of oxaloacetate decarboxylation in the alpha-subunit, which correlates with the coordination of a Zn2+ metal ion by several residues at the hydrophilic C-terminus. The 65 kDa hydrophilic alpha-subunit consists of an N-terminal carboxyltransferase domain connected to a C-terminal biotin carboxyl carrier protein domain. The 45 kDa beta-subunit is an integral membrane protein with nine transmembrane segments, which serves to couple the decarboxylation of carboxybiotin to the translocation of Na+ from the cytoplasm to the periplasm. The small 9 kDa gamma-subunit is an integral membrane protein with a single membrane-spanning helix at the N-terminus, followed by a hydrophilic C-terminal domain which interacts with the alpha-subunit. The gamma-subunit is essential for the overall stability of the complex, and likely serves as an anchor to hold the alpha- and beta-subunits in place
additional information
-
oxaloacetate decarboxylase complex structure, modeling, overview. The gamma-subunit is essential for the overall stability of the complex, and likely serves as an anchor to hold the alpha- and beta-subunits in place. The gamma-subunit significantly accelerates the rate of oxaloacetate decarboxylation in the alpha-subunit, which correlates with the coordination of a Zn2+ metal ion by several residues at the hydrophilic C-terminus. The 65 kDa hydrophilic alpha-subunit consists of an N-terminal carboxyltransferase domain connected to a C-terminal biotin carboxyl carrier protein domain. The 45 kDa beta-subunit is an integral membrane protein with nine transmembrane segments, which serves to couple the decarboxylation of carboxybiotin to the translocation of Na+ from the cytoplasm to the periplasm. The small 9 kDa gamma-subunit is an integral membrane protein with a single membrane-spanning helix at the N-terminus, followed by a hydrophilic C-terminal domain which interacts with the alpha-subunit. The gamma-subunit is essential for the overall stability of the complex, and likely serves as an anchor to hold the alpha- and beta-subunits in place
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
530000
-
the most prominent band at 530 kDa is likely composed of a tetrameric Oad-alpha/gamma plus a dimeric (or tetrameric) Oad-beta subunit, SDS-PAGE
570000
oxaloacetate decarboxylase OAD-2, gel filtration
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
heterotrimer
homodimer
tetramer
trimer
additional information
-
the alpha-subunit binds the gamma-subunit with a distinct association domain which is flanked on both sides with proline- and alanine-rich linker peptides
dimer
-
in the absence of beta- or alpha-subunits, the gamma-subunit forms a homodimer through a dimerization interface in the carboxyltransferase domain
heterotrimer
-
OAD contains three different subunits: Oad-alpha, a biotinylated extrinsic protein that catalyzes the alpha-ketodecarboxylation of oxaloacetate; Oad-gamma, a structural bitopic membrane protein whose cytosolic tail (named as Oad-gamma) binds tightly to Oad-alpha, and Oad-beta, a multispan transmembrane-alpha-helical protein that constitutes the Na+-channel
tetramer
-
the enzyme is constituted of four subunits: catalytic subunit OadA (termed Ef-A), membrane pump Ef-B, biotin acceptor protein Ef-D, and subunit Ef-H. Subunits Ef-A, Ef-D, and Ef-H form a cytoplasmic soluble complex, Ef-AHD, which is also associated with the membrane. The Ef-H subunit is involved in the cytoplasmic Ef-AHD complex formation. Analysis of subunit interactions and complex formation, overview
tetramer
-
the enzyme is constituted of four subunits: catalytic subunit OadA (termed Ef-A), membrane pump Ef-B, biotin acceptor protein Ef-D, and subunit Ef-H. Subunits Ef-A, Ef-D, and Ef-H form a cytoplasmic soluble complex, Ef-AHD, which is also associated with the membrane. The Ef-H subunit is involved in the cytoplasmic Ef-AHD complex formation. Analysis of subunit interactions and complex formation, overview
-
tetramer
-
the enzyme consists of alpha-, beta-, and gamma-subunits as well as a biotin carboxyl carrier protein domain. The 65 kDa hydrophilic alpha-subunit consists of an N-terminal carboxyltransferase domain connected to a C-terminal biotin carboxyl carrier protein domain. The 45 kDa beta-subunit is an integral membrane protein with nine transmembrane segments, which serves to couple the decarboxylation of carboxybiotin to the translocation of Na+ from the cytoplasm to the periplasm. The small 9 kDa gamma-subunit is an integral membrane protein with a single membrane-spanning helix at the N-terminus, followed by a hydrophilic C-terminal domain which interacts with the alpha-subunit. The gamma-subunit is essential for the overall stability of the complex, and likely serves as an anchor to hold the alpha- and beta-subunits in place
tetramer
oxaloacetate decarboxylase OAD-2
tetramer
-
the enzyme consists of alpha-, beta-, and gamma-subunits as well as a biotin carboxyl carrier protein domain. The about 65 kDa hydrophilic alpha-subunit consists of an N-terminal carboxyltransferase domain connected to a C-terminal biotin carboxyl carrier protein domain. The about 45 kDa beta-subunit is an integral membrane protein with nine transmembrane segments, which serves to couple the decarboxylation of carboxybiotin to the translocation of Na+ from the cytoplasm to the periplasm. the site of interaction with the gamma-subunit in Vibrio cholerae OADC is located in an intervening region between the carboxyltransferase and biotin carboxyl carrier protein domains of the alpha-subunit, termed the association domain. Tetramerization of alpha-OADC is mediated by an interaction between the association domain of the alpha-subunit and the cytosolic portion of the gamma-subunit in a manner. A biotin binding pocket, termed the exo-binding site, is located at the interface between the association domain and the carboxyltransferase domain. The interaction is facilitated by the tetramerization of alpha-OADC through interactions between the association domain and the the cytosolic portion of the gamma-subunit, which maintain two of the four alpha-OADC molecules in close proximity to the membrane-bound beta-subunit
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 0.2 M MgCl2, 0.1 M Bis-Tris pH 6.0, 25% (w/v) polyethylene glycol 3350
-
hanging drop vapor diffusion method at 18°C, crystal structure of the enzyme (FAHD1) protein in complex with its cofactor Mg2+, cocrystallization with oxalate and high resolution for the enzyme (FAHD1) in complex with oxalate
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)
sitting drop vapour diffusion method using 0.1 M sodium cacodylate (pH 6.5), 0.2 M (NH4)2SO4, 5% (v/v) glycerol and 25% (w/v) PEG 8000
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E33A
H30A
K123A
oxaloacetate decarboxylase activity and acylpyruvate hydrolase activity are abolished
A383C
-
beta subunit, very low activity, low activity after modification with 2-aminoethyl methanethiosulfonate
G377C
-
beta subunit, no activity even after modification with 2-aminoethyl methanethiosulfonate
G380C
-
beta subunit, very low activity, low activity after modification with 2-aminoethyl methanethiosulfonate
N373L
-
beta subunit, very low activity, no protection against tryptic digestion by Na+
R389C
-
beta subunit, increased pH-optimum, reduced activity, activity and pH-optimum can be restored to wild type value by modification with 2-aminoethyl methanethiosulfonate
S382A
-
beta subunit, no activity below 20 mM Na+, active with 400 mM NaCl, no protection against tryptic digestion by Na+, no Na+ transport
S382C
-
beta subunit, no activity even after modification with 2-aminoethyl methanethiosulfonate
H235A
the kcat value for catalysis of oxaloacetate decarboxylation is less than an order of magnitude smaller compared to the wild type enzyme
H235Q
the kcat value for catalysis of oxaloacetate decarboxylation is less than an order of magnitude smaller compared to the wild type enzyme
Y212F
25fold reduction of the Km value compared to the wild type enzyme
additional information
E33A
significant reduction in oxaloacetate decarboxylase activity and complete abrogation of the acylpyruvate hydrolase activity
H30A
significant reduction in oxaloacetate decarboxylase activity and complete abrogation of the acylpyruvate hydrolase activity
additional information
-
oadA, oadB, and oadD deletion mutants are constructed, while an oadH mutant strain cannot be obtained in spite of using different genetic strategies
additional information
-
oadA, oadB, and oadD deletion mutants are constructed, while an oadH mutant strain cannot be obtained in spite of using different genetic strategies
-
additional information
mutation of amino acids H30, E33 and K123 each had discernible influence on the acylpyruvate hydrolase and/or oxaloacetate decarboxylase activity of FAHD1, suggesting distinct catalytic mechanisms for both activities
additional information
-
mutation of amino acids H30, E33 and K123 each had discernible influence on the acylpyruvate hydrolase and/or oxaloacetate decarboxylase activity of FAHD1, suggesting distinct catalytic mechanisms for both activities
additional information
-
mutant [ILCitM (pFL3)] is constructed by double homologous recombination, during culture with citrate the growth rate of the mutant is lower than the willd type enzyme
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
25°C, 50 mM triethanolamine/HCl, pH 7.0, 5 days, almost complete inactivation, presence of 1 mM Mn2+ and 50% v/v glycerol stabilize
-
4°C, phosphate buffer or arsenate buffer, pH 7, with mercaptoethanol, N2-atmosphere, 2 months
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, HiPrep column chromatography, Mono Q column chromatography, and Superdex-200 gel filtration
-
DEAE-cellulose column chromatography, phenyl-Sepharose columnn chromatography, and butyl-Sepharose column chromatography
enzyme from Vibrio cholerae and heterologously expressed enzyme
recombinnat maltose-binding protein fusion protein OadH from Escherichia coli by amylase affinity chromatography, recombinant His-tagged subunits from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression of gene oadH as maltose-binding protein fusion protein in Escherichia coli, genes oadA-oadD, expression of recombinant His-tagged subunits in Escherichia coli strain BL21(DE3)
-
when subunit alpha-2 of oxaloacetate decarboxylase OAD-2 and the C-terminal domain of gamma-2 are synthesized together in Escherichia coli they form a complex that is stable at neutral pH and dissociates at pH-values below 5.0
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
-
optimization of oxaloacetate may increase lysine productivity of commercially used strains
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ng, S.K.; Wong, M.; Hamilton, I.R.
Properties of oxaloacetate decarboxylase from veillonella parvula
J. Bacteriol.
150
1252-1258
1982
Veillonella parvula
brenda
Schwitzguebel, J.P.; Ettlinger, L.
Oxaloacetate decarboxylase from Acetobacter aceti
Arch. Microbiol.
124
63-68
1980
Acetobacter aceti
-
brenda
Benziman, M.; Russo, A.; Hochmann, S.; Weinhouse, H.
Purification and regulatory properties of the oxaloacetate decarboxylase of Acetobacter xylinum
J. Bacteriol.
134
1-9
1978
Komagataeibacter xylinus
brenda
Wojtczak, A.B.; Walajtys, E.
Mitochondrial oxaloacetate decarboxylase from rat liver
Biochim. Biophys. Acta
347
168-182
1974
Cavia aperea, Oryctolagus cuniculus, Rattus norvegicus
brenda
Dean, B.; Bartley, W.
Oxaloacetate decarboxylases of rat liver
Biochem. J.
135
667-672
1973
Rattus norvegicus
brenda
Morinaga, T.; Shirakawa, M.
Studies on oxalacetate carboxylase of pig heart muscle
Agric. Biol. Chem.
35
1166-1172
1971
Sus scrofa
-
brenda
Herbert, D.
Oxalacetic carboxylase of Micrococcus lysodeikticus
Methods Enzymol.
1
753-757
1955
Micrococcus luteus
-
brenda
Ivanishchev, V.V.; Kurganov, B.I.
Investigation of properties of oxaloacetate decarboxylase from chloroplasts of sunflower leaves
Biokhimiya
58
250-254
1993
Helianthus annuus
-
brenda
Jetten, M.S.M.; Sinskey, A.J.
Purification and properties of oxaloacetate decarboxylase from Corynebacterium glutamicum
Antonie van Leeuwenhoek
67
221-227
1995
Azotobacter vinelandii, Corynebacterium glutamicum, Micrococcus luteus
brenda
Guargliardi, A.; Moracci, M.; Manco, G.; Rossi, M.; Bartolucci, S.
Oxalacetate decarboxylase and pyruvate carboxylase activities, and effect of sulfhydryl reagents in malic enzyme from Sulfolobus solfataricus
Biochim. Biophys. Acta
957
301-311
1988
Saccharolobus solfataricus
brenda
Wild, M.R.; Pos, K.M.; Dimroth, P.
Site-directed sulfhydryl labeling of the oxaloacetate decarboxylase Na+ pump of Klebsiella pneumoniae: helix VIII comprises a portion of the sodium ion channel
Biochemistry
42
11615-11624
2003
Klebsiella pneumoniae
brenda
Schmid, M.; Vorburger, T.; Pos, K.M.; Dimroth, P.
Role of conserved residues within helices IV and VIII of the oxaloacetate decarboxylase beta subunit in the energy coupling mechanism of the Na+ pump
Eur. J. Biochem.
269
2997-3004
2002
Klebsiella pneumoniae
brenda
Trukhina, Y.O.; Metalnikova, E.A.; Popov, V.N.; Eprintsev, A.T.
Subcellular localization of oxaloacetate decarboxylase and its isolation from maize leaves
Russ. J. Plant Physiol.
49
635-640
2002
Zea mays
-
brenda
Labrou, N.E.; Clonis, Y.D.
Oxaloacetate decarboxylase from Pseudomonas stutzeri: purification and characterization
Arch. Biochem. Biophys.
365
17-24
1999
Pseudomonas stutzeri
brenda
Dahinden, P.; Pos, K.M.; Taralczak, M.; Dimroth, P.
Oxaloacetate decarboxylase of Archaeoglobus fulgidus: cloning of genes and expression in Escherichia coli
Arch. Microbiol.
182
414-420
2004
Archaeoglobus fulgidus
brenda
Dahinden, P.; Auchli, Y.; Granjon, T.; Taralczak, M.; Wild, M.; Dimroth, P.
Oxaloacetate decarboxylase of Vibrio cholerae: purification, characterization, and expression of the genes in Escherichia coli
Arch. Microbiol.
183
121-129
2005
Vibrio cholerae (Q6A1F5), Vibrio cholerae (Q6A1F6), Vibrio cholerae (Q6A1F7), Vibrio cholerae (Q6A1G0), Vibrio cholerae (Q9KUH0), Vibrio cholerae (Q9KUH1), Vibrio cholerae, Vibrio cholerae O395-N1 (Q6A1F5), Vibrio cholerae O395-N1 (Q6A1F6), Vibrio cholerae O395-N1 (Q6A1F7), Vibrio cholerae O395-N1 (Q6A1G0), Vibrio cholerae O395-N1 (Q9KUH0), Vibrio cholerae O395-N1 (Q9KUH1)
brenda
Dahinden, P.; Pos, K.M.; Dimroth, P.
Identification of a domain in the alpha-subunit of the oxaloacetate decarboxylase Na+ pump that accomplishes complex formation with the gamma-subunit
FEBS J.
272
846-855
2005
Vibrio cholerae serotype O1
brenda
Sender, P.D.; Martin, M.G.; Peiru, S.; Magni, C.
Characterization of an oxaloacetate decarboxylase that belongs to the malic enzyme family
FEBS Lett.
570
217-222
2004
Lactococcus lactis, Lactococcus lactis CRL264
brenda
Narayanan, B.C.; Niu, W.; Han, Y.; Zou, J.; Mariano, P.S.; Dunaway-Mariano, D.; Herzberg, O.
Structure and function of PA4872 from Pseudomonas aeruginosa, a novel class of oxaloacetate decarboxylase from the PEP mutase/isocitrate lyase superfamily
Biochemistry
47
167-182
2008
Pseudomonas aeruginosa (Q9HUU1), Pseudomonas aeruginosa
brenda
Kim, M.
Determining citrate in fruit juices using a biosensor with citrate lyase and oxaloacetate decarboxylase in a flow injection analysis system
Food Chem.
99
851-857
2006
Pseudomonas sp.
brenda
Studer, R.; Dahinden, P.; Wang, W.W.; Auchli, Y.; Li, X.D.; Dimroth, P.
Crystal structure of the carboxyltransferase domain of the oxaloacetate decarboxylase Na+ pump from Vibrio cholerae
J. Mol. Biol.
367
547-557
2007
Vibrio cholerae serotype O1
brenda
Dharmarajan, L.; Case, C.L.; Dunten, P.; Mukhopadhyay, B.
Tyr235 of human cytosolic phosphoenolpyruvate carboxykinase influences catalysis through an anion-quadrupole interaction with phosphoenolpyruvate carboxylate
FEBS J.
275
5810-5819
2008
Homo sapiens
brenda
Augagneur, Y.; Garmyn, D.; Guzzo, J.
Mutation of the oxaloacetate decarboxylase gene of Lactococcus lactis subsp. lactis impairs the growth during citrate metabolism
J. Appl. Microbiol.
104
260-268
2008
Lactococcus lactis
brenda
Blancato, V.S.; Repizo, G.D.; Suarez, C.A.; Magni, C.
Transcriptional regulation of the citrate gene cluster of Enterococcus faecalis involves the GntR family transcriptional activator CitO
J. Bacteriol.
190
7419-7430
2008
Enterococcus faecalis
brenda
Klaffl, S.; Eikmanns, B.J.
Genetic and functional analysis of the soluble oxaloacetate decarboxylase from Corynebacterium glutamicum
J. Bacteriol.
192
2604-2612
2010
Corynebacterium glutamicum
brenda
Ran, T.; Wang, Y.; Xu, D.; Wang, W.
Expression, purification, crystallization and preliminary crystallographic analysis of Cg1458: a novel oxaloacetate decarboxylase from Corynebacterium glutamicum
Acta Crystallogr. Sect. F
67
968-970
2011
Corynebacterium glutamicum
brenda
Espariz, M.; Repizo, G.; Blancato, V.; Mortera, P.; Alarcon, S.; Magni, C.
Identification of malic and soluble oxaloacetate decarboxylase enzymes in Enterococcus faecalis
FEBS J.
278
2140-2151
2011
Enterococcus faecalis (Q82YW6)
brenda
Balsera, M.; Buey, R.M.; Li, X.D.
Quaternary structure of the oxaloacetate decarboxylase membrane complex and mechanistic relationships to pyruvate carboxylases
J. Biol. Chem.
286
9457-9467
2011
Vibrio cholerae serotype O1
brenda
Granjon, T.; Maniti, O.; Auchli, Y.; Dahinden, P.; Buchet, R.; Marcillat, O.; Dimroth, P.
Structure-function relations in oxaloacetate decarboxylase complex. Fluorescence and infrared approaches to monitor oxomalonate and Na+ binding effect
PLoS ONE
5
e10935
2010
Vibrio cholerae serotype O1
brenda
Repizo, G.D.; Blancato, V.S.; Mortera, P.; Lolkema, J.S.; Magni, C.
Biochemical and genetic characterization of the Enterococcus faecalis oxaloacetate decarboxylase complex
Appl. Environ. Microbiol.
79
2882-2890
2013
Enterococcus faecalis, Enterococcus faecalis JH2-2
brenda
Lietzan, A.D.; St Maurice, M.
Functionally diverse biotin-dependent enzymes with oxaloacetate decarboxylase activity
Arch. Biochem. Biophys.
544
75-86
2014
Klebsiella aerogenes, Vibrio cholerae serotype O1
brenda
Pircher, H.; von Grafenstein, S.; Diener, T.; Metzger, C.; Albertini, E.; Taferner, A.; Unterluggauer, H.; Kramer, C.; Liedl, K.R.; Jansen-Duerr, P.
Identification of FAH domain-containing protein 1 (FAHD1) as oxaloacetate decarboxylase
J. Biol. Chem.
290
6755-6762
2015
Homo sapiens (Q6P587)
brenda
Weiss, A.K.H.; Naschberger, A.; Loeffler, J.R.; Gstach, H.; Bowler, M.W.; Holzknecht, M.; Cappuccio, E.; Pittl, A.; Etemad, S.; Dunzendorfer-Matt, T.; Scheffzek, K.; Liedl, K.R.; Jansen-Duerr, P.
Structural basis for the bi-functionality of human oxaloacetate decarboxylase FAHD1
Biochem. J.
475
3561-3576
2018
Homo sapiens (Q6P587), Homo sapiens
brenda
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