Information on EC 4.1.1.3 - Oxaloacetate decarboxylase

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

EC NUMBER
COMMENTARY
4.1.1.3
-
RECOMMENDED NAME
GeneOntology No.
Oxaloacetate decarboxylase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
oxaloacetate = pyruvate + CO2
show the reaction diagram
not
-
oxaloacetate = pyruvate + CO2
show the reaction diagram
Keq: 0.00213 1/mM, decarboxylation favored
-
oxaloacetate = pyruvate + CO2
show the reaction diagram
pyruvate + CO2 = oxaloacetae
-
oxaloacetate = pyruvate + CO2
show the reaction diagram
pyruvate + CO2 = oxaloacetae
-
oxaloacetate = pyruvate + CO2
show the reaction diagram
pyruvate + CO2 = oxaloacetae
-
oxaloacetate = pyruvate + CO2
show the reaction diagram
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
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxylation
-
-
-
-
decarboxylation
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
gluconeogenesis
-
-
Metabolic pathways
-
-
methylgallate degradation
-
-
protocatechuate degradation I (meta-cleavage pathway)
-
-
Pyruvate metabolism
-
-
syringate degradation
-
-
SYSTEMATIC NAME
IUBMB Comments
oxaloacetate carboxy-lyase (pyruvate-forming)
The enzyme from Klebsiella aerogenes is a biotinyl protein and also decarboxylates glutaconyl-CoA and methylmalonyl-CoA. The process is accompanied by the extrusion of two sodium ions from cells. Some animal enzymes require Mn2+.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Oxalacetate decarboxylase
-
-
-
-
Oxalacetic acid decarboxylase
-
-
-
-
Oxalacetic beta-decarboxylase
-
-
-
-
Oxalacetic carboxylase
-
-
-
-
Oxalate beta-decarboxylase
-
-
-
-
Oxaloacetate carboxylyase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9024-98-0
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
guinea pig
-
-
Manually annotated by BRENDA team
strain ATCC 13032
-
-
Manually annotated by BRENDA team
genes oadA, oadB, oadC, and oadD
-
-
Manually annotated by BRENDA team
strain ATCC 29212
-
-
Manually annotated by BRENDA team
genes oadA, oadB, oadC, and oadD
-
-
Manually annotated by BRENDA team
sunflower
-
-
Manually annotated by BRENDA team
subspecies Lactococcus lactis lactis, strain IL1403
-
-
Manually annotated by BRENDA team
Lactococcus lactis CRL264
CRL264
-
-
Manually annotated by BRENDA team
formerly Micrococcus lysodeiktikus
-
-
Manually annotated by BRENDA team
pig
-
-
Manually annotated by BRENDA team
oxaloacetate decarboxylase OAD-1, alpha subunit; O395-N1
SwissProt
Manually annotated by BRENDA team
oxaloacetate decarboxylase OAD-1, beta subunit; O395-N1
SwissProt
Manually annotated by BRENDA team
oxaloacetate decarboxylase OAD-1, gamma subunit; O395-N1
SwissProt
Manually annotated by BRENDA team
oxaloacetate decarboxylase OAD-2, alpha subunit; O395-N1
SwissProt
Manually annotated by BRENDA team
oxaloacetate decarboxylase OAD-2, beta subunit; O395-N1
SwissProt
Manually annotated by BRENDA team
oxaloacetate decarboxylase OAD-2, gamma subunit; O395-N1
SwissProt
Manually annotated by BRENDA team
Vibrio cholerae O395-N1
oxaloacetate decarboxylase OAD-1, alpha subunit; O395-N1
SwissProt
Manually annotated by BRENDA team
Vibrio cholerae O395-N1
oxaloacetate decarboxylase OAD-1, beta subunit; O395-N1
SwissProt
Manually annotated by BRENDA team
Vibrio cholerae O395-N1
oxaloacetate decarboxylase OAD-1, gamma subunit; O395-N1
SwissProt
Manually annotated by BRENDA team
Vibrio cholerae O395-N1
oxaloacetate decarboxylase OAD-2, alpha subunit; O395-N1
SwissProt
Manually annotated by BRENDA team
Vibrio cholerae O395-N1
oxaloacetate decarboxylase OAD-2, beta subunit; O395-N1
SwissProt
Manually annotated by BRENDA team
Vibrio cholerae O395-N1
oxaloacetate decarboxylase OAD-2, gamma subunit; O395-N1
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
Q82YW6
the citrate fermentation phenotype is not affected by citM deletion
metabolism
Q82YW6
CitM is not required for efficient citrate utilization
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
-
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
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
-
?
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
-
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
-
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
-
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
-
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
?
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
-
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
-
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
-
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
-
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
-
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
-
?
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
Q9HUU1
-
-
-
r
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
-
?
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
-
ir
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
-
?
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
-
?
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
-
?
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
-
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
-
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
-
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
-
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
-
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
-
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
-
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
?
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
?
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
?
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
?
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
?
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
-
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
-
?
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
-
ir
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
-
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
-
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
-
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
-
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
-
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
-
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
-
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
-
?
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
-
r
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
Q82YW6
-
-
-
?
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
reaction mechanism
-
-
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
reaction mechanism
-
-
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
reaction mechanism
-
-
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
stereochemistry
-
-
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
reaction is catalyzed at low rate by the alpha subunit alone, much higher activity with the complete enzyme
-
?
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
one Na+ is transported into the periplasm and one H+ is transported into the cytoplasm during the reaction
-
?
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
one Na+ is transported into the periplasm and one H+ is transported into the cytoplasm during the reaction
-
?
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
one Na+ is transported into the periplasm and one H+ is transported into the cytoplasm during the reaction
-
?
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
one Na+ is transported into the periplasm and one H+ is transported into the cytoplasm during the reaction
-
?
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
one Na+ is transported into the periplasm and one H+ is transported into the cytoplasm during the reaction
-
?
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
one Na+ is transported into the periplasm and one H+ is transported into the cytoplasm during the reaction
-
?
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
two Na+ are transported into the periplasm and one H+ is transported into the cytoplasm during the reaction
-
?
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
-
?
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
Lactococcus lactis CRL264
-
-
-
-
ir
oxaloacetate
?
show the reaction diagram
-
-
-
-
-
oxaloacetate
?
show the reaction diagram
-
-
-
-
-
oxaloacetate
?
show the reaction diagram
-
-
-
-
-
oxaloacetate
?
show the reaction diagram
-
-
-
-
-
oxaloacetate
?
show the reaction diagram
-
-
-
-
-
oxaloacetate
?
show the reaction diagram
-
-
-
-
-
oxaloacetate
?
show the reaction diagram
-
-
-
-
-
oxaloacetate
?
show the reaction diagram
-
-
-
-
-
oxaloacetate
?
show the reaction diagram
-
-
-
-
-
oxaloacetate
?
show the reaction diagram
-
-
-
-
-
oxaloacetate
?
show the reaction diagram
-
-
-
-
-
oxaloacetate
?
show the reaction diagram
-
-
-
-
-
oxaloacetate
?
show the reaction diagram
-
-
-
-
-
oxaloacetate
?
show the reaction diagram
-
part of citrate fermentation pathway, amount of Na+ transported depends on decarboxylation rate, but decoupling at very high decarboxylation rates, electrochemical gradient equals membrane driving force of 114 mV
-
-
-
oxaloacetate
?
show the reaction diagram
-
high activity in ethanol- or acetate-grown bacteria
-
-
-
oxaloacetate
?
show the reaction diagram
-
decarboxylation energy used for active Na+ transport
-
-
-
oxaloacetate
?
show the reaction diagram
-
decarboxylation energy used for active Na+ transport
-
-
-
oxaloacetate
?
show the reaction diagram
-
Na+ transport coupled to oxaloacetate decarboxylation
-
-
-
oxaloacetate
?
show the reaction diagram
-
involved in citrate fermentation
-
-
-
oxaloacetate
?
show the reaction diagram
-
involved in citrate fermentation
-
-
-
Pyruvate + CO2
Oxaloacetate
show the reaction diagram
-
-
-
-
Pyruvate + CO2
Oxaloacetate
show the reaction diagram
-
-
-
-
Pyruvate + CO2
Oxaloacetate
show the reaction diagram
-
-
-
-
Pyruvate + CO2
Oxaloacetate
show the reaction diagram
-
reversal of reaction with whole enzyme by appropriate transmembrane Na+ gradient
-
-
3-methyloxaloacetate
3-methylpyruvate + CO2
show the reaction diagram
Q9HUU1
-
-
-
?
additional information
?
-
-
transmembrane transport of Na+
-
-
-
additional information
?
-
-
transmembrane transport of Na+
-
-
-
additional information
?
-
-
transmembrane transport of Na+
-
-
-
additional information
?
-
-
no substrate: phosphoenolpyruvate
-
-
-
additional information
?
-
Q6A1F5, Q6A1F6, Q6A1F7, Q6A1G0, Q9KUH0, Q9KUH1
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
-
-
-
additional information
?
-
Vibrio cholerae O395-N1
Q6A1F5, Q6A1F6, Q6A1F7, Q6A1G0, Q9KUH0, Q9KUH1
after reconstitution into proteoliposomes, the enzyme acts as a Na+ pump
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
-
?
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
-
?
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
-
?
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
one Na+ is transported into the periplasm and one H+ is transported into the cytoplasm during the reaction
-
?
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
one Na+ is transported into the periplasm and one H+ is transported into the cytoplasm during the reaction
-
?
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
one Na+ is transported into the periplasm and one H+ is transported into the cytoplasm during the reaction
-
?
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
one Na+ is transported into the periplasm and one H+ is transported into the cytoplasm during the reaction
-
?
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
one Na+ is transported into the periplasm and one H+ is transported into the cytoplasm during the reaction
-
?
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
one Na+ is transported into the periplasm and one H+ is transported into the cytoplasm during the reaction
-
?
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
two Na+ are transported into the periplasm and one H+ is transported into the cytoplasm during the reaction
-
?
oxaloacetate
?
show the reaction diagram
-
-
-
-
-
oxaloacetate
?
show the reaction diagram
-
-
-
-
-
oxaloacetate
?
show the reaction diagram
-
-
-
-
-
oxaloacetate
?
show the reaction diagram
-
-
-
-
-
oxaloacetate
?
show the reaction diagram
-
-
-
-
-
oxaloacetate
?
show the reaction diagram
-
-
-
-
-
oxaloacetate
?
show the reaction diagram
-
-
-
-
-
oxaloacetate
?
show the reaction diagram
-
-
-
-
-
oxaloacetate
?
show the reaction diagram
-
-
-
-
-
oxaloacetate
?
show the reaction diagram
-
-
-
-
-
oxaloacetate
?
show the reaction diagram
-
-
-
-
-
oxaloacetate
?
show the reaction diagram
-
-
-
-
-
oxaloacetate
?
show the reaction diagram
-
-
-
-
-
oxaloacetate
?
show the reaction diagram
-
part of citrate fermentation pathway, amount of Na+ transported depends on decarboxylation rate, but decoupling at very high decarboxylation rates, electrochemical gradient equals membrane driving force of 114 mV
-
-
-
oxaloacetate
?
show the reaction diagram
-
high activity in ethanol- or acetate-grown bacteria
-
-
-
oxaloacetate
?
show the reaction diagram
-
decarboxylation energy used for active Na+ transport
-
-
-
oxaloacetate
?
show the reaction diagram
-
decarboxylation energy used for active Na+ transport
-
-
-
oxaloacetate
?
show the reaction diagram
-
Na+ transport coupled to oxaloacetate decarboxylation
-
-
-
oxaloacetate
?
show the reaction diagram
-
involved in citrate fermentation
-
-
-
oxaloacetate
?
show the reaction diagram
-
involved in citrate fermentation
-
-
-
Oxaloacetate
Pyruvate + CO2
show the reaction diagram
-
-
-
-
?
additional information
?
-
Q6A1F5, Q6A1F6, Q6A1F7, Q6A1G0, Q9KUH0, Q9KUH1
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
-
-
-
additional information
?
-
Vibrio cholerae O395-N1
Q6A1F5, Q6A1F6, Q6A1F7, Q6A1G0, Q9KUH0, Q9KUH1
after reconstitution into proteoliposomes, the enzyme acts as a Na+ pump
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
biotin
-
about 1 mol bound per alpha-chain
biotin
-
role in enzyme function
biotin
-
not
biotin
-
binds to the C-terminal domain of the alpha-subunit
biotin
-
-
NAD+
-
reaction enhancement, allosteric effector
NAD+
-
one pyridine nucleotide reduced for each pyruvate formed
NADP+
-
reaction enhancement
NADP+
-
one pyridine nucleotide reduced for each pyruvate formed
biotin
-
dependent on, the enzyme utilizes a carboxyltransferase domain to catalyze the biotin-dependent decarboxylation of oxaloacetate
additional information
Q82YW6
no nicotinamide cofactors required
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cd2+
-
activates
Co2+
-
activates
Co2+
-
activates
Li+
-
Km: 25 mM
Mg2+
-
required, decarboxylation Km: 0.17 mM, carboxylation Km: 1.85 mM
Mg2+
-
Km: 1.2 mM, can be substituted by Mn2+
Mg2+
-
only cytoplasmic enzyme
Mg2+
-
activates
Mg2+
-
inhibitory above 1 mM
Mg2+
-
or Mn2+, absolutely required, Km-value 0.08 mM
Mg2+
-
activates
Mg2+
Q9HUU1
cofactor
Mn2+
-
required
Mn2+
-
can be substituted by Mg2+, Km: 0.08 mM
Mn2+
-
only cytoplasmic enzyme
Mn2+
-
activates
Mn2+
-
Km: 1.2 mM; required, can be substituted by Mg2+, Co2+, Ni2+, Ca2+
Mn2+
-
required, can be substituted by Mg2+, Ca2+
Mn2+
-
inhibitory above 1 mM
Mn2+
-
or Mg2+, absolutely required, Km-value 0.02 mM, inhibitory above 0.46 mM
Mn2+
-
dependent on, maximal activity in presence of 10 mM Mn2+
Mn2+
Q82YW6
the enzyme is dependent on divalent metal ions with 100% activity at 20 mM Mn2+
Na+
-
Km: 1 mM
Na+
-
Km: 1.5 mM
Na+
-
Km: 0.78 mM
Na+
-
protects against proteolysis and alcohol inactivation
Na+
-
stoichiometry with decarboxylation, Na+ transport directly depends on biotin carboxylation/decarboxylation
Na+
-
two ions per enzyme required for maximum activity, cooperative binding
Na+
-
two ions per enzyme required for maximum activity, cooperative binding, 20-50 mM protects against tryptic digestion
Na+
-
protects against tryptic digestion
Na+
Q6A1F5, Q6A1F6, Q6A1F7, Q6A1G0, Q9KUH0, Q9KUH1
dependent on
Ni2+
-
activates
Ni2+
-
activates
Zn2+
-
gamma-subunit, involved in carboxytransfer, 0.96 mol/mol enzyme
Zn2+
-
0.61-0.99 mol/mol enzyme
Zn2+
-
binds to the gamma subunit, can not be removed with EDTA or 1,10-phenanthroline
Zn2+
-
binds to the gamma subunit
Zn2+
-
active site metal ion, 2 mol Zn2+ per mol enzyme
Zn2+
-
subunit Oad-gamma contains a Zn(II)-bound metal
Zn2+
-
the gamma subunit contains zinc
Zn2+
-
bound at the gamma-subunit, coordinated by several residues at the hydrophilic C-terminus
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-oxoglutarate
-
2 mM inhibitor in presence of 10 mM Mn2+, 11% inhibition
2-Oxomalonate
-
Ki: 0.06 mM
2-Oxomalonate
-
-
3,3-difluoroxaloacetate
Q9HUU1
-
5,5'-dithiobis(2-nitrobenzoate)
-
-
acetate
-
competitive for oxaloacetate, Ki: 12 mM
acetic acid
-
noncompetitive
Acetopyruvate
Q9HUU1
-
ADP
-
Ki: 1.5 mM
ADP
-
Ki: 1.2 mM
ADP
-
competitive
ADP
Q82YW6
78% residual activity at 0.25 mM
alpha-ketovalerate
Q9HUU1
-
ATP
-
carboxylation competitively inhibited, decarboxylation non-competitively, Ki: 2.2 mM, possibly involved in regulation
ATP
-
Ki: 1.5 mM
ATP
-
complete inhibition at 8-9 mM
ATP
Q82YW6
37% residual activity at 1 mM
Avidin
-
not
-
azide
-
2 mM, 20% inhibition
Ca2+
-
2 mM inhibitor in presence of 1 mM Mn2+, 30% inhibition
citrate
-
50% inhibition of mitochondrial enzyme at 4.5 mM
citrate
-
-
citrate
-
0.5 mM inhibitor or 2 mM inhibitor in presence of 10 mM Mn2+, 24% inhibition
citrate
Q82YW6
74% residual activity at 2 mM
coenzyme A
-
50% inhibition of mitochondrial enzyme at 0.05 mM
coenzyme A
-
Ki: 2.4 mM
Cu2+
-
-
Cu2+
-
Ki: 0.2 mM
Cu2+
-
2 mM, 45% inhibition
Cu2+
-
0.5 mM inhibitor in presence of 1 mM Mn2+, complete inhibition
diethylstilbestrol
-
95% inhibition at 50 mM
EDTA
-
inhibition of residual activity without divalent metal ions
EDTA
-
-
EDTA
-
2 mM, 100% inhibition
EDTA
-
10 mM, complete inhibition
EDTA
Q82YW6
complete inhibition at 2 mM
fumarate
-
2 mM inhibitor in presence of 10 mM Mn2+, 21% inhibition
Glycine-NaOH
-
-
glyoxylate
-
Ki: 0.04 mM
Hg2+
-
-
Hg2+
-
complete inactivation at 1 mM, buffer-dependend, interaction with alpha-subunit
hydrogencarbonate
-
-
KSCN
-
95% inhibition at 50 mM, completely reversible
L-Malate
-
competitive for oxaloacetate, Ki: 4.5 mM
malate
-
2 mM inhibitor in presence of 10 mM Mn2+, 54% inhibition
malate
Q82YW6
65% residual activity at 2 mM
malic acid
-
competitive
malonate
-
-
malonate
-
0.5 mM inhibitor in presence of 10 mM Mn2+, 84% inhibition
malonate
Q82YW6
26% residual activity at 2 mM
Mn2+
-
at concentrations higher than 0.4 mM
N-ethylmaleimide
-
-
N-ethylmaleimide
-
2 mM, 14% inhibition
NaCl
-
almost complete inhibition at 0.4 M
NaCl
-
OAD tertiary structure is sensitive to the presence of NaCl
NAD+
-
2 mM inhibitor in presence of 10 mM Mn2+, complete inhibition
NAD+
Q82YW6
40% residual activity at 0.25 mM
NADH
-
2 mM inhibitor in presence of 10 mM Mn2+, complete inhibition
NADH
Q82YW6
53% residual activity at 0.25 mM
Ni2+
-
2 mM inhibitor in presence of 1 mM Mn2+, 40% inhibition
oxalate
-
competitive for oxaloacetate, Ki: 0.0038 mM
oxalate
-
Ki: 0.0035
oxalate
-
Ki: 0.005 mM
oxalate
-
-
oxalate
Q6A1F5, Q6A1F6, Q6A1F7, Q6A1G0, Q9KUH0, Q9KUH1
half-maximal inhibition at 0.01 mM
oxalate
-
0.5 mM inhibitor in presence of 10 mM Mn2+, 80% inhibition
oxalate
Q9HUU1
-
oxalate
Q82YW6
14% residual activity at 2 mM
oxalic acid
-
competitive
oxomalonate
Q6A1F5, Q6A1F6, Q6A1F7, Q6A1G0, Q9KUH0, Q9KUH1
half-maximal inhibition at 0.2 mM
oxomalonate
-
competitive inhibitor of OAD with respect to oxaloacetate
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
50% inhibition at 0.5 mM
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
2 mM, 62% inhibition
p-hydroxymercuribenzoate
-
70% inhibition at 5 mM
p-hydroxymercuribenzoate
-
complete inactivation after preincubation at 0.2 mM
p-hydroxymercuribenzoate
-
partly prevented by NADP+
phosphoenolpyruvate
-
50% inhibition of mitochondrial enzyme at 28 mM
phosphoenolpyruvate
-
competitive
Phosphonopyruvate
Q9HUU1
-
pyruvate
-
product inhibition competitive for oxaloacetate, Ki: 1.3 mM, noncompetitive inhibition for Na+, Ki: 2 mM
pyruvate
-
2 mM inhibitor in presence of 10 mM Mn2+, 8% inhibition
pyruvate
Q9HUU1
-
succinate
-
2 mM inhibitor in presence of 10 mM Mn2+, 23% inhibition
Zn2+
-
54% inhibition at 1.5 mM
Zn2+
-
Ki: 0.8 mM
Zn2+
-
0.5 mM inhibitor in presence of 1 mM Mn2+, complete inhibition
Mn2+
-
inhibitory above 0.46 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)
-
additional information
Q82YW6
not inhibited by succinate
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
citrate
-
expression is induced by citrate
EDTA
-
activating below 5 mM
NaCl
-
highest activity with 1-1.4 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.63
3-methyloxaloacetate
Q9HUU1
wild type enzyme, in 0.2 mM NADH, 5 mM MgCl2 and 50 mM K+HEPES (pH 7.5), at 25C
0.0003
oxaloacetate
-
wild-type, Vmax = 4 micromol/min/mg; Y235A mutant, Vmax = 0.2 micromol/min/mg. In the presence of GDP; Y235F mutant, Vmax = 2 micromol/min/mg; 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; Y235F mutant, Vmax = 3 micromol/min/mg. In the presence of GDP
0.03
oxaloacetate
-
pH 7.1
0.06
oxaloacetate
-
-
0.087
oxaloacetate
Q9HUU1
mutant enzyme Y212F, in 0.2 mM NADH, 5 mM MgCl2 and 50 mM K+HEPES (pH 7.5), at 25C
0.15
oxaloacetate
-
-
0.15
oxaloacetate
-
-
0.22
oxaloacetate
-
-
0.23
oxaloacetate
-
mitochondrial enzyme
0.52
oxaloacetate
-
-
0.55
oxaloacetate
-
-
0.62
oxaloacetate
Q82YW6
calculated value at pH 4.5, temperature not specified in the publication
1.02
oxaloacetate
Q9HUU1
mutant enzyme H235A, in 0.2 mM NADH, 5 mM MgCl2 and 50 mM K+HEPES (pH 7.5), at 25C
1.39
oxaloacetate
-
in 100 mM Tris-HCl (pH 7.3), 10 mM MgCl2, 2.5 mM EDTA, at 30C
1.7
oxaloacetate
-
-
2.1
oxaloacetate
-
-
2.1
oxaloacetate
-
pH 8.0, 25C
2.2
oxaloacetate
Q9HUU1
wild type enzyme, in 0.2 mM NADH, 5 mM MgCl2 and 50 mM K+HEPES (pH 7.5), at 25C
2.5
oxaloacetate
Q9HUU1
mutant enzyme H235Q, in 0.2 mM NADH, 5 mM MgCl2 and 50 mM K+HEPES (pH 7.5), at 25C
4.3
oxaloacetate
-
-
3.3
pyruvate
-
-
additional information
additional information
-
kinetic data; positive cooperativity for oxaloacetate
-
additional information
additional information
-
kinetic data
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
250
3-methyloxaloacetate
Q9HUU1
in 0.2 mM NADH, 5 mM MgCl2 and 50 mM K+HEPES (pH 7.5), at 25C
3.5
oxaloacetate
-
-
11.2
oxaloacetate
Q82YW6
calculated value at pH 4.5, temperature not specified in the publication
20.26
oxaloacetate
-
-
104
oxaloacetate
-
in 100 mM Tris-HCl (pH 7.3), 10 mM MgCl2, 2.5 mM EDTA, at 30C
7500
oxaloacetate
Q9HUU1
in 0.2 mM NADH, 5 mM MgCl2 and 50 mM K+HEPES (pH 7.5), at 25C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
22.3
oxaloacetate
Q82YW6
calculated value at pH 4.5, temperature not specified in the publication
57
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.06
2-Oxomalonate
-
-
0.45
3,3-difluoroxaloacetate
Q9HUU1
-
18.4
acetic acid
-
pH 8.0, 25C
1.09
Acetopyruvate
Q9HUU1
-
1.5
ADP
-
-
5.1
ADP
-
pH 8.0, 25C
6.7
alpha-ketovalerate
Q9HUU1
-
1.5
ATP
-
-
2.4
coenzyme A
-
-
0.04
glyoxylate
-
-
2.2
hydrogencarbonate
-
pH 8.0, 25C
21.4
malic acid
-
pH 8.0, 25C
198
NaCl
-
wild type enzyme, pH 6.9
0.0035
oxalate
-
-
0.005
oxalate
-
-
0.043
oxalate
Q9HUU1
-
0.6
oxalic acid
-
pH 8.0, 25C
0.5
p-chloromercuribenzoate
-
-
7.8
phosphoenolpyruvate
-
pH 8.0, 25C
28
phosphoenolpyruvate
-
mitochondrial enzyme
3
Phosphonopyruvate
Q9HUU1
-
1.3
pyruvate
-
product inhibition competitive for oxaloacetate
2.1
pyruvate
-
pH 8.0, 25C
7.2
pyruvate
Q9HUU1
-
2.5
Mn2+
-
pH 8.0, 25C
additional information
additional information
-
Ki-values given for inhibition with NaCl for all mutant enzymes at 3-4 different pH
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.54
-
-
3.15
-
purified enzyme, pH 7.1
9
-
alpha-chain, independent of Na+
45
-
wild type enzyme
319
-
pH 8.0, 25C
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
activity of reconstituted enzyme and isolated subunits
additional information
-
strain-dependend
additional information
-
specific activity for all mutant enzymes
additional information
Q6A1F5, Q6A1F6, Q6A1F7, Q6A1G0, Q9KUH0, Q9KUH1
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5
-
cytoplasmic enzyme
5.5
-
Q192L and Y209A mutants
6
-
enzyme assay at
6.25 - 6.75
-
wild type enzyme
6.5 - 7
-
wild type enzyme
6.5 - 7.5
-
-
6.5 - 7.5
-
-
6.5 - 7.5
-
wild type enzyme
7
-
enzyme assay at
7
-
pH optimum at about pH 7 for all mutant enzymes except R389A
7.1
-
-
8.5
-
pH-optima above 8.5 found for N373L, R389A, R389L mutant enzymes
9.2
-
R389A mutant
9.5
-
mitochondrial enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5 - 5
Q82YW6
-
3.5 - 5.5
-
pH 3.5: about 55% of maximal activity, pH 5.5: about 40% of maximal activity
6 - 8
-
-
6 - 8.5
-
-
7 - 10
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
-
enzyme assay at
25
-
enzyme assay at
30
-
enzyme assay at
30
-
enzyme assay at
37
-
enzyme assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
58
-
no activity above
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Q6A1F5, Q6A1F6, Q6A1F7, Q6A1G0, Q9KUH0, Q9KUH1
upon anaerobic growth of Vibrio cholerae on citrate, exclusivle the oad-2 gene is expressed
Manually annotated by BRENDA team
Vibrio cholerae O395-N1
-
upon anaerobic growth of Vibrio cholerae on citrate, exclusivle the oad-2 gene is expressed
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
83% of activity
Manually annotated by BRENDA team
-
isolated alpha-subunits or reconstituted alpha-beta-complexes expressed in Escherichia coli
Manually annotated by BRENDA team
-
differs from mitochondrial enzyme
Manually annotated by BRENDA team
-
subunits Ef-A, Ef-D, and Ef-H form a cytoplasmic soluble complex, Ef-AHD, which is also associated with the membrane
Manually annotated by BRENDA team
-
subunits Ef-A, Ef-D, and Ef-H form a cytoplasmic soluble complex, Ef-AHD, which is also associated with the membrane
-
Manually annotated by BRENDA team
-
alpha-subunit is peripheral membrane protein, beta- and gamma-subunits are integral membrane proteins, spatial model
Manually annotated by BRENDA team
-
reconstituted gamma-alpha-subunits or whole enzyme expressed in Escherichia coli
Manually annotated by BRENDA team
-
beta and gamma subunits are integral membrane proteins, alpha subunit is attached to the gamma subunit
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
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
-
Manually annotated by BRENDA team
-
differs from cytoplasmic enzyme
Manually annotated by BRENDA team
-
14% of activity
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
32000
-
monomer, SDS-PAGE
704327
58000
-
gel filtration
653877
62100
-
native enzyme, gel filtration
704327
63000
-
gel filtration
654328
63600
-
alpha-subunit, calculated from amino acid sequence
4258
80000
-
gel filtration
4268
98300
-
static light scattering
681424
102000
-
gel filtration
681424
105000
-
gel filtration
4283
118000
-
gel filtration
4276
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
715662
570000
Q6A1F5, Q6A1F6, Q6A1F7, Q6A1G0, Q9KUH0, Q9KUH1
oxaloacetate decarboxylase OAD-2, gel filtration
663796
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
2 * 49000, SDS-PAGE
dimer
Q9HUU1
dimer of dimers, X-ray crystallography
dimer
-
in the absence of beta- or alpha-subunits, the gamma-subunit forms a homodimer through a dimerization interface in the carboxyltransferase domain
heterotrimer
-
-
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
homodimer
-
2 * 51000, gel filtration
homodimer
-
2 * 29000, gel filtration
tetramer
-
4 * 31700, SDS-PAGE
tetramer
Q6A1F5, Q6A1F6, Q6A1F7, Q6A1G0, Q9KUH0, Q9KUH1
oxaloacetate decarboxylase OAD-2
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
-
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
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
Vibrio cholerae O395-N1
-
oxaloacetate decarboxylase OAD-2
-
trimer
-
alpha-subunit also necessary for Na+ transport, spatial arrangement and subunit interactions
trimer
-
1 * 63600 + 1 * 34000 + 1 * 12000 alpha,beta,gamma, SDS-PAGE
trimer
-
1 * 65000 + 1 * 34000 + 1 * 12000 alpha,beta,gamma, SDS-PAGE, subunits carry different functions
trimer
-
size and ultrastructure
trimer
-
1 * 63800 + 1 * 34500 + 1 * 10600, alpha,beta,gamma, SDS-PAGE
trimer
-
spatial arrangement of cloned enzyme in Escherichia coli
trimer
-
alpha, beta, gamma
monomer
-
1 * 63000, SDS-PAGE
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
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 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)
Q9HUU1
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
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3
-
-
4273
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
-
5 min
4266
50
-
only if protected by oxalate
4261
55
-
up to
4272
85
-
half life for inacivation, 5 h
4283
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
very instable, protease-sensitive, 50% loss of activity after 4 min at 4C
-
buffer-dependent, mercaptoethanol stabilises
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, Tris-HCl buffer, pH 7.5, 2 month, 40% loss of activity
-
frozen, Tris-HCl buffer, pH 7.5, 1 month, 25% loss of activity
-
-20C, potassium phosphate buffer, pH 7, 50% glycerol, 2 month
-
4C, glycerol, 2 months
-
25C, 50 mM triethanolamine/HCl, pH 7.0, 5 days, almost complete inactivation, presence of 1 mM Mn2+ and 50% v/v glycerol stabilize
-
4C, phosphate buffer or arsenate buffer, pH 7, with mercaptoethanol, N2-atmosphere, 2 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, HiPrep column chromatography, Mono Q column chromatography, and Superdex-200 gel filtration
-
Ni-NTA column chromatography and Superdex G-200 gel filtration
-
alpha- and beta-chain
-
Ni2+-bounded affinity column chromatography
Q82YW6
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
-
recombinant enzyme from Escherichia coli
-
recombinant protein from Escherichia coli
-
recombinant
-
DEAE-cellulose column chromatography, phenyl-Sepharose columnn chromatography, and butyl-Sepharose column chromatography
Q9HUU1
avidin-Sepharose column chromatography
-
enzyme from Vibrio cholerae and heterologously expressed enzyme
Q6A1F5, Q6A1F6, Q6A1F7, Q6A1G0, Q9KUH0, Q9KUH1
Ni2+-NTA-agarose column chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
expressed in Escherichia coli C43 (DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
Q82YW6
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)
-
all subunits, expressed in Escherichia coli, alpha-subunit strongly overexpressed from pT7-7 plasmid
-
alpha-subunit, expressed in Escherichia coli
-
expressed in Escherichia coli
-
expressed in Escherichia coli CC118
-
expressed in Escherichia coli DH5alpha
-
expressed in Escherichia coli DH5alpha/pSK-GAB
-
expression in Escherichia coli, expression of mutant enzymes and domains of the alpha subunit
-
expression in Escherichia coli M15
-
expressed in Escherichia coli BL21 (DE3) cells
Q9HUU1
expressed in Escherichia coli C43(DE3) cells
-
expressed in Escherichia coli Rosetta (C43) cells
-
expressed in Escherichia coli strain C43(DE3)
-
expression in Escherichia coli; expression in Escherichia coli
Q6A1F5, Q6A1F6, Q6A1F7, Q6A1G0, Q9KUH0, Q9KUH1
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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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Y235A
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site-directed mutagenesis
Y235F
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site-directed mutagenesis
Y235S
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site-directed mutagenesis
A383C
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beta subunit, very low activity, low activity after modification with 2-aminoethyl methanethiosulfonate
C291E
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beta subunit, unstable in the absence of Na+, dissociates into an alpha-gamma subcomplex and the beta subunit
C87A
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slightly increased activity
C87A/A194C
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no effect on activity
C87A/I198C
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no effect on activity
C87A/L178C
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about 50% of activity
C87A/L7C
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no activity
C87A/P191C
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no activity
C87A/P205C
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no effect on activity, only traces of activity
C87A/S187C
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no effect on activity
C87A/V129C
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strongly increased activity
C87A/Y182C
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slightly increased activity
D203N
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beta subunit, complete loss of activity
D62A
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gamma subunit, Zn2+ content decreased to 35% of the wild type enzyme, roughly 30% of activity
D63A
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gamma subunit, almost no effect on activity
DELTAH76-P83
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gamma subunit, unable to associate to the alpha subunit, no activity
DELTAH78-P83
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gamma subunit, unable to associate to the alpha subunit, no activity
DELTAH82-P83
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gamma subunit, Zn2+ content decreased to 5% of the wild type enzyme, very low activity
G337A
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beta subunit, complete loss of activity
G377A
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beta subunit, complete loss of activity
G377C
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beta subunit, no activity even after modification with 2-aminoethyl methanethiosulfonate
G380A
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beta subunit, about 30% of activity
G380C
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beta subunit, very low activity, low activity after modification with 2-aminoethyl methanethiosulfonate
H76A
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gamma subunit, almost no effect on activity
H77A
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gamma subunit, Zn2+ content decreased to 10% of the wild type enzyme, very low activity
N373D
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beta subunit, no protection against tryptic digestion by Na+
N373L
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beta subunit, almost complete loss of activity
N373L
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beta subunit, very low activity, no protection against tryptic digestion by Na+
N392L
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beta subunit, about 70% of activity
Q192L
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beta subunit, lower pH optimum than wild type enzyme
R389A
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beta subunit, about 10% of activity, significantly decreased Na+ binding
R389A
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beta subunit, significantly increased pH-optimum
R389C
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beta subunit, increased pH-optimum, reduced activity, activity and pH-optimum can be restored to wild type value by modification with 2-aminoethyl methanethiosulfonate
R389D
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beta subunit, almost complete loss of activity
R389D
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beta subunit, very low activity
R389K
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beta subunit, about 80% of activity, significantly decreased Na+ binding
R389L
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beta subunit, about 10% of activity, significantly decreased Na+ binding
S382A
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beta subunit, complete loss of activity
S382A
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beta subunit, no activity below 20 mM Na+, active with 400 mM NaCl, no protection against tryptic digestion by Na+, no Na+ transport
S382C
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beta subunit, complete loss of activity
S382C
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beta subunit, no activity even after modification with 2-aminoethyl methanethiosulfonate
S382D
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beta subunit, about 10% of activity
S382D
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beta subunit, very low activity
S382E
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beta subunit, complete loss of activity
S382N
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beta subunit, complete loss of activity
S382Q
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beta subunit, complete loss of activity
S382T
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beta subunit, about 10% of activity
S382T
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beta subunit, very low activity
Y209A
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beta subunit, lower pH optimum than wild type enzyme
H235A
Q9HUU1
the kcat value for catalysis of oxaloacetate decarboxylation is less than an order of magnitude smaller compared to the wild type enzyme
H235Q
Q9HUU1
the kcat value for catalysis of oxaloacetate decarboxylation is less than an order of magnitude smaller compared to the wild type enzyme
Y212F
Q9HUU1
25fold reduction of the Km value compared to the wild type enzyme
C148A
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74% activity of the wild type enzyme
C148S
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54% activity of the wild type enzyme
D17A
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inactive
H207I
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inactive
H209I
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inactive
K178I
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inactive
K178R
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inactive
M180I
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16% activity of the wild type enzyme
Q20L
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inactive
R16I
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inactive
additional information
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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
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oadA, oadB, and oadD deletion mutants are constructed, while an oadH mutant strain cannot be obtained in spite of using different genetic strategies
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H78A
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gamma subunit, binding to alpha subunit is lost, gamma subunit, unable to associate to the alpha subunit, no activity
additional information
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fusion protein from different domains of the enzyme subunits
additional information
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mutations in the beta subunit do not affect the ability to transfer the carboxyl-group to biotin, but reduce the decarboxylase activity
additional information
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several other mutant with reduced activity
Y229F
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beta subunit, completely inactive
additional information
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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
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
reconstition of isolated alpha-chains and bacterial membranes containing beta- and gamma-chains
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heterologously expressed oxaloacetate decarboxylase OAD-2
Q6A1F5, Q6A1F6, Q6A1F7, Q6A1G0, Q9KUH0, Q9KUH1
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
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optimization of oxaloacetate may increase lysine productivity of commercially used strains