BRENDA - Enzyme Database
show all sequences of 4.1.1.112

Functionally diverse biotin-dependent enzymes with oxaloacetate decarboxylase activity

Lietzan, A.D.; St Maurice, M.; Arch. Biochem. Biophys. 544, 75-86 (2014)

Data extracted from this reference:

Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
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
Klebsiella aerogenes
16020
-
membrane
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
Vibrio cholerae
16020
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Zn2+
bound at the gamma-subunit, coordinated by several residues at the hydrophilic C-terminus
Klebsiella aerogenes
Zn2+
bound at the gamma-subunit, coordinated by several residues at the hydrophilic C-terminus
Vibrio cholerae
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Klebsiella aerogenes
decarboxylation and sodium transport by the biotin-dependent oxaloacetate decarboxylase complex, overview
?
-
-
-
additional information
Vibrio cholerae
decarboxylation and sodium transport by the biotin-dependent oxaloacetate decarboxylase complex, overview
?
-
-
-
Oxaloacetate
Klebsiella aerogenes
-
Pyruvate + CO2
-
-
?
Oxaloacetate
Vibrio cholerae
-
Pyruvate + CO2
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Klebsiella aerogenes
-
-
-
Vibrio cholerae
-
-
-
Reaction
Reaction
Commentary
Organism
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
Klebsiella aerogenes
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
Vibrio cholerae
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
decarboxylation and sodium transport by the biotin-dependent oxaloacetate decarboxylase complex, overview
726821
Klebsiella aerogenes
?
-
-
-
-
additional information
decarboxylation and sodium transport by the biotin-dependent oxaloacetate decarboxylase complex, overview
726821
Vibrio cholerae
?
-
-
-
-
Oxaloacetate
-
726821
Klebsiella aerogenes
Pyruvate + CO2
-
-
-
?
Oxaloacetate
-
726821
Vibrio cholerae
Pyruvate + CO2
-
-
-
?
Subunits
Subunits
Commentary
Organism
dimer
in the absence of beta- or alpha-subunits, the gamma-subunit forms a homodimer through a dimerization interface in the carboxyltransferase domain
Klebsiella aerogenes
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
Klebsiella aerogenes
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
Vibrio cholerae
Cofactor
Cofactor
Commentary
Organism
Structure
biotin
dependent on, the enzyme utilizes a carboxyltransferase domain to catalyze the biotin-dependent decarboxylation of oxaloacetate
Klebsiella aerogenes
biotin
dependent on, the enzyme utilizes a carboxyltransferase domain to catalyze the biotin-dependent decarboxylation of oxaloacetate
Vibrio cholerae
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
biotin
dependent on, the enzyme utilizes a carboxyltransferase domain to catalyze the biotin-dependent decarboxylation of oxaloacetate
Klebsiella aerogenes
biotin
dependent on, the enzyme utilizes a carboxyltransferase domain to catalyze the biotin-dependent decarboxylation of oxaloacetate
Vibrio cholerae
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
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
Klebsiella aerogenes
16020
-
membrane
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
Vibrio cholerae
16020
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Zn2+
bound at the gamma-subunit, coordinated by several residues at the hydrophilic C-terminus
Klebsiella aerogenes
Zn2+
bound at the gamma-subunit, coordinated by several residues at the hydrophilic C-terminus
Vibrio cholerae
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Klebsiella aerogenes
decarboxylation and sodium transport by the biotin-dependent oxaloacetate decarboxylase complex, overview
?
-
-
-
additional information
Vibrio cholerae
decarboxylation and sodium transport by the biotin-dependent oxaloacetate decarboxylase complex, overview
?
-
-
-
Oxaloacetate
Klebsiella aerogenes
-
Pyruvate + CO2
-
-
?
Oxaloacetate
Vibrio cholerae
-
Pyruvate + CO2
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
decarboxylation and sodium transport by the biotin-dependent oxaloacetate decarboxylase complex, overview
726821
Klebsiella aerogenes
?
-
-
-
-
additional information
decarboxylation and sodium transport by the biotin-dependent oxaloacetate decarboxylase complex, overview
726821
Vibrio cholerae
?
-
-
-
-
Oxaloacetate
-
726821
Klebsiella aerogenes
Pyruvate + CO2
-
-
-
?
Oxaloacetate
-
726821
Vibrio cholerae
Pyruvate + CO2
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
in the absence of beta- or alpha-subunits, the gamma-subunit forms a homodimer through a dimerization interface in the carboxyltransferase domain
Klebsiella aerogenes
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
Klebsiella aerogenes
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
Vibrio cholerae
General Information
General Information
Commentary
Organism
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
Klebsiella aerogenes
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
Vibrio cholerae
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
Klebsiella aerogenes
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
Vibrio cholerae
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
Klebsiella aerogenes
General Information (protein specific)
General Information
Commentary
Organism
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
Klebsiella aerogenes
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
Vibrio cholerae
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
Klebsiella aerogenes
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
Vibrio cholerae
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
Klebsiella aerogenes
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
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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726821
Lietzan
Functionally diverse biotin-de ...
Klebsiella aerogenes, Vibrio cholerae
Arch. Biochem. Biophys.
544
75-86
2014
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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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713674
Ran
Expression, purification, crys ...
Corynebacterium glutamicum
Acta Crystallogr. Sect. F
67
968-970
2011
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714979
Espariz
Identification of malic and so ...
Enterococcus faecalis
FEBS J.
278
2140-2151
2011
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715662
Balsera
Quaternary structure of the ox ...
Vibrio cholerae
J. Biol. Chem.
286
9457-9467
2011
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704327
Klaffl
Genetic and functional analysi ...
Corynebacterium glutamicum
J. Bacteriol.
192
2604-2612
2010
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716673
Granjon
Structure-function relations i ...
Vibrio cholerae
PLoS ONE
5
e10935
2010
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678331
Narayanan
Structure and function of PA48 ...
Pseudomonas aeruginosa
Biochemistry
47
167-182
2008
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