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Information on EC 7.2.4.5 - glutaconyl-CoA decarboxylase
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7.2.4.5 glutaconyl-CoA decarboxylaseIUBMB Comments
The enzyme from the bacterium Acidaminococcus fermentans is a biotinyl-protein, requires Na+, and acts as a sodium pump. Prior to the Na+-dependent decarboxylation, the carboxylate is transferred to biotin in a Na+-independent manner. The conserved lysine, to which biotin forms an amide bond, is located 34 amino acids before the C-terminus, flanked on both sides by two methionine residues, which are conserved in every biotin-dependent enzyme.
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Word Map
- 7.2.4.5
- acetyl-coa
- biotin
- carboxylases
-
biotin-dependent
- malonyl-coa
- propionyl-coa
- fermentans
-
acidaminococcus
- crotonyl-coa
- carboxybiotin
- symbiosum
-
avidin-sepharose
- accases
-
biotin-containing
-
6.4.1.2
- transcarboxylase
- haloxyfop
The enzyme appears in viruses and cellular organisms
Synonyms
carboxyltransferase, glutaconyl-coa decarboxylase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
carboxyltransferase
-
-
-
-
decarboxylase, glutaconyl coenzyme A
-
-
-
-
EC 4.1.1.70
-
-
formerly
-
GCD
pent-2-enoyl-CoA carboxy-lyase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(2E)-4-carboxybut-2-enoyl-CoA + Na+[side 1] = (2E)-but-2-enoyl-CoA + CO2 + Na+[side 2]
stereochemistry
-
(2E)-4-carboxybut-2-enoyl-CoA + Na+[side 1] = (2E)-but-2-enoyl-CoA + CO2 + Na+[side 2]
mechanism of carboxy-transfer
(2E)-4-carboxybut-2-enoyl-CoA + Na+[side 1] = (2E)-but-2-enoyl-CoA + CO2 + Na+[side 2]
energetics
-
(2E)-4-carboxybut-2-enoyl-CoA + Na+[side 1] = (2E)-but-2-enoyl-CoA + CO2 + Na+[side 2]
mechanism, interaction of subunits
-
(2E)-4-carboxybut-2-enoyl-CoA + Na+[side 1] = (2E)-but-2-enoyl-CoA + CO2 + Na+[side 2]
the enzyme from Acidaminococcus fermentans is a biotinyl-protein, requires Na+, and acts as a sodium pump. Prior to the Na+-dependent decarboxylation, the carboxlate is transferred to biotin in a Na+-independent manner. The conserved lysine, to which biotin forms an amine bond, is located 34 amino acids before the C-terminus, flanked on both sides by two methionine residues, which are conserved in every biotin-dependent enzyme
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
(2E)-4-carboxybut-2-enoyl-CoA carboxy-lyase [(2E)-but-2-enoyl-CoA-forming]
The enzyme from the bacterium Acidaminococcus fermentans is a biotinyl-protein, requires Na+, and acts as a sodium pump. Prior to the Na+-dependent decarboxylation, the carboxylate is transferred to biotin in a Na+-independent manner. The conserved lysine, to which biotin forms an amide bond, is located 34 amino acids before the C-terminus, flanked on both sides by two methionine residues, which are conserved in every biotin-dependent enzyme.
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CAS REGISTRY NUMBER
COMMENTARY
84399-93-9
-
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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
glutaconyal-CoA + Na+[side 1]
crotonyl-CoA + CO2 + Na+[side 2]
-
-
-
-
?
(2E)-4-carboxybut-2-enoyl-CoA + Na+[side 1]
(2E)-but-2-enoyl-CoA + CO2 + Na+[side 2]
-
-
-
-
?
(2E)-4-carboxybut-2-enoyl-CoA + Na+[side 1]
(2E)-but-2-enoyl-CoA + CO2 + Na+[side 2]
-
-
-
-
?
4-carboxybut-2-enoyl-CoA + Na+[side 1]
but-2-enoyl-CoA + CO2 + Na+[side 2]
-
-
-
-
?
4-carboxybut-2-enoyl-CoA + Na+[side 1]
but-2-enoyl-CoA + CO2 + Na+[side 2]
-
-
-
-
?
4-carboxybut-2-enoyl-CoA + Na+[side 1]
but-2-enoyl-CoA + CO2 + Na+[side 2]
-
-
-
-
?
4-carboxybut-2-enoyl-CoA + Na+[side 1]
but-2-enoyl-CoA + CO2 + Na+[side 2]
-
-
-
-
?
4-carboxybut-2-enoyl-CoA + Na+[side 1]
but-2-enoyl-CoA + CO2 + Na+[side 2]
-
-
-
-
?
4-carboxybut-2-enoyl-CoA + Na+[side 1]
but-2-enoyl-CoA + CO2 + Na+[side 2]
-
i.e. glutaconyl-CoA
i.e. crotonyl-CoA
?
4-carboxybut-2-enoyl-CoA + Na+[side 1]
but-2-enoyl-CoA + CO2 + Na+[side 2]
-
-
-
-
?
glutaconyl-CoA + Na+[side 1]
but-2-enoyl-CoA + CO2 + Na+[side 2]
-
-
-
-
?
glutaconyl-CoA + Na+[side 1]
but-2-enoyl-CoA + CO2 + Na+[side 2]
-
-
-
-
?
glutaconyl-CoA + Na+[side 1]
but-2-enoyl-CoA + CO2 + Na+[side 2]
-
-
-
-
?
glutaconyl-CoA + Na+[side 1]
but-2-enoyl-CoA + CO2 + Na+[side 2]
-
-
-
-
?
glutaconyl-CoA + Na+[side 1]
but-2-enoyl-CoA + CO2 + Na+[side 2]
-
i.e. glutaconyl-CoA
i.e. crotonyl-CoA
?
glutaconyl-CoA + Na+[side 1]
but-2-enoyl-CoA + CO2 + Na+[side 2]
-
-
-
-
?
additional information
?
-
-
enzyme catalyzes a 3H exchange of [2,4,4-3H]glutaconate with water when acetyl-CoA is present
-
-
?
additional information
?
-
-
not: 3-methylglutaconyl-CoA
-
-
?
additional information
?
-
-
pathway of fermentative benzoate degradation
-
-
?
additional information
?
-
-
glutaconyl-CoA, i.e. (2E)-4-carboxybut-2-enoyl-CoA is decarboxylated to crotonyl-CoA by a sodium-ion-dependent membrane-bound glutaconyl-CoA decarboxylase
-
-
?
additional information
?
-
-
glutaconyl-CoA, i.e. (2E)-4-carboxybut-2-enoyl-CoA is decarboxylated to crotonyl-CoA by a sodium-ion-dependent membrane-bound glutaconyl-CoA decarboxylase
-
-
?
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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
glutaconyal-CoA + Na+[side 1]
crotonyl-CoA + CO2 + Na+[side 2]
-
-
-
-
?
additional information
?
-
-
pathway of fermentative benzoate degradation
-
-
?
glutaconyl-CoA + Na+[side 1]
but-2-enoyl-CoA + CO2 + Na+[side 2]
-
-
-
-
?
glutaconyl-CoA + Na+[side 1]
but-2-enoyl-CoA + CO2 + Na+[side 2]
-
-
-
-
?
glutaconyl-CoA + Na+[side 1]
but-2-enoyl-CoA + CO2 + Na+[side 2]
-
-
-
-
?
glutaconyl-CoA + Na+[side 1]
but-2-enoyl-CoA + CO2 + Na+[side 2]
-
-
-
-
?
glutaconyl-CoA + Na+[side 1]
but-2-enoyl-CoA + CO2 + Na+[side 2]
-
i.e. glutaconyl-CoA
i.e. crotonyl-CoA
?
glutaconyl-CoA + Na+[side 1]
but-2-enoyl-CoA + CO2 + Na+[side 2]
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Biocytin
may substitute for biotin, Km value 13 mM
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Li+
Na+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
N-Alkanols
-
concentration required for complete inactivation decreases N-dodecyl-N-dimethylaminoxide at 20-30°C
-
additional information
-
with increasing chain length, sodium ions prevent inactivation, Li+ is ten times less effective than Na+
-
N-ethylmaleimide
Gcd holoenzyme loses half of its activity within 6 min, whereas the expressed GcdA requires 21 min
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Brij 35
-
only Triton X-100 and Brij 35 are able to keep the enzyme in an active state at 20-30°C
Brij 35
-
only Triton X-100 and Brij 35 are able to keep the enzyme in an active state at 20-30°C
Brij 35
-
only Triton X-100 and Brij 35 are able to keep the enzyme in an active state at 20-30°C
Brij 35
-
only Triton X-100 and Brij 35 are able to keep the enzyme in an active state at 20-30°C
Triton X-100
-
only Triton X-100 and Brij 35 are able to keep the enzyme in an active state at 20-30°C
Triton X-100
-
only Triton X-100 and Brij 35 are able to keep the enzyme in an active state at 20-30°C
Triton X-100
-
only Triton X-100 and Brij 35 are able to keep the enzyme in an active state at 20-30°C
Triton X-100
-
only Triton X-100 and Brij 35 are able to keep the enzyme in an active state at 20-30°C
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
The Structure of the Carboxyltransferase Component of Acetyl-CoA Carboxylase Reveals a Zinc-Binding Motif Unique to the Bacterial Enzyme(,).
Obesity
Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase.
Tuberculosis
AccD6, a key carboxyltransferase essential for mycolic acid synthesis in Mycobacterium tuberculosis, is dispensable in a nonpathogenic strain.
Tuberculosis
AccD6, a member of the Fas II locus, is a functional carboxyltransferase subunit of the acyl-coenzyme A carboxylase in Mycobacterium tuberculosis.
Tuberculosis
Structure, activity, and inhibition of the Carboxyltransferase ?-subunit of acetyl coenzyme A carboxylase (AccD6) from Mycobacterium tuberculosis.
Tuberculosis
Structure-based inhibitor design of AccD5, an essential acyl-CoA carboxylase carboxyltransferase domain of Mycobacterium tuberculosis.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
48
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Q06700 i.e. subunit GcdA, Q9ZAA6 .e. subunit GcdB, Q9ZAA7 .e. subunit GcdC, Q9ZAA8 .e. subunit GcdD
UniProt
brenda
Q06700 i.e. subunit GcdA, Q9ZAA6 .e. subunit GcdB, Q9ZAA7 .e. subunit GcdC, Q9ZAA8 .e. subunit GcdD
UniProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
Gcd couples the biotin-dependent decarboxylation of glutaconyl-CoA with the generation of an electrochemical Na+ gradient
physiological function
Acidaminococcus fermentans is able to ferment glutamate to ammonia, CO2, acetate, butyrate, and H2. H2 formation is dependent on Na+ in washed cells. According to the model, electrons, generated by NADH oxidation inside of the cytoplasmic membrane, reduce protons outside of the cytoplasmic membrane. The entire process can be driven by decarboxylation of glutaconyl-CoA, which consumes the protons released by NADH oxidation inside the cell. Hydrogen production commences exactly at those Na+ concentrations at which the electrogenic H+/Na+-antiporter glutaconyl-CoA decarboxylase is converted into a Na+/Na+ exchanger
physiological function
-
decarboxylation of glutaconyl-CoA to crotonyl-CoA is catalysed by a membrane-bound, biotin-dependent enzyme which requires Na+ for activity. The enzyme is able to convert the free energy of decarboxylation into a Na+ gradient
physiological function
sodium-ion pump glutaconyl-CoA decarboxylase is composed of four subunits: GcdA, the carboxytransferase (65 kDa), GcdB, the carboxylyase (36 kDa), GcdC, the biotin carrier (24 kDa) and GcdD (14 kDa) of unknown function. The GcdA subunit catalyzes the biotin-dependent formation of crotonyl-CoA from glutaconyl-CoA
physiological function
-
Gcd couples the biotin-dependent decarboxylation of glutaconyl-CoA with the generation of an electrochemical Na+ gradient
-
physiological function
-
Acidaminococcus fermentans is able to ferment glutamate to ammonia, CO2, acetate, butyrate, and H2. H2 formation is dependent on Na+ in washed cells. According to the model, electrons, generated by NADH oxidation inside of the cytoplasmic membrane, reduce protons outside of the cytoplasmic membrane. The entire process can be driven by decarboxylation of glutaconyl-CoA, which consumes the protons released by NADH oxidation inside the cell. Hydrogen production commences exactly at those Na+ concentrations at which the electrogenic H+/Na+-antiporter glutaconyl-CoA decarboxylase is converted into a Na+/Na+ exchanger
-
physiological function
-
sodium-ion pump glutaconyl-CoA decarboxylase is composed of four subunits: GcdA, the carboxytransferase (65 kDa), GcdB, the carboxylyase (36 kDa), GcdC, the biotin carrier (24 kDa) and GcdD (14 kDa) of unknown function. The GcdA subunit catalyzes the biotin-dependent formation of crotonyl-CoA from glutaconyl-CoA
-
Show AA Sequence and Transmembrane Helices (1234 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
12000
120000
14000
16000
-
x * 65000 alpha, carboxytransferase + x * 33000, beta, carboxylyase + x * 19000, gamma, biotin carrier + x * 16000, probably carboxylyase, SDS-PAGE
19000
-
x * 65000 alpha, carboxytransferase + x * 33000, beta, carboxylyase + x * 19000, gamma, biotin carrier + x * 16000, probably carboxylyase, SDS-PAGE
30000
33000
-
x * 65000 alpha, carboxytransferase + x * 33000, beta, carboxylyase + x * 19000, gamma, biotin carrier + x * 16000, probably carboxylyase, SDS-PAGE
35000
39000
-
x * 65000, alpha, carboxytransferase, + x * 39000, beta, decarboxylase, + x * 14000, gamma, biotin carrier, + x * 12000, delta, membrane anchor, deduced from gene sequence, expression and purification of alpha leads to a homotrimer, SDS-PAGE
60000
65000
additional information
-
in sucrose density gradient centrifugation the activity is recovered in 2 peaks: MW 470000, possibly dimer and MW 250000, possibly monomer
12000
-
x * 65000, alpha, carboxytransferase, + x * 39000, beta, decarboxylase, + x * 14000, gamma, biotin carrier, + x * 12000, delta, membrane anchor, deduced from gene sequence, expression and purification of alpha leads to a homotrimer, SDS-PAGE
12000
1 * 65000 + 1 * 35000 + 1 * 14000 + 1 * 12000, X-ray crystallography
120000
-
x * 120000, alpha, biotin carrier + x * 60000, beta, carboxytransferase, carboxylase + x * 30000, gamma, sodium pump, SDS-PAGE
120000
-
x * 120000, alpha, biotin carrier + x * 60000, beta, transferase + x * 30000, gamma, sodium-dependent carboxybiotin decarboxylase, SDS-PAGE
14000
-
x * 65000, alpha, carboxytransferase, + x * 39000, beta, decarboxylase, + x * 14000, gamma, biotin carrier, + x * 12000, delta, membrane anchor, deduced from gene sequence, expression and purification of alpha leads to a homotrimer, SDS-PAGE
14000
1 * 65000 + 1 * 35000 + 1 * 14000 + 1 * 12000, X-ray crystallography
30000
-
x * 120000, alpha, biotin carrier + x * 60000, beta, carboxytransferase, carboxylase + x * 30000, gamma, sodium pump, SDS-PAGE
30000
-
x * 120000, alpha, biotin carrier + x * 60000, beta, transferase + x * 30000, gamma, sodium-dependent carboxybiotin decarboxylase, SDS-PAGE
35000
-
1 * 120000-140000, alpha, contains biotin + 1 * 60000, beta, + 1 * 35000, gamma, hydrophobic, SDS-PAGE
35000
1 * 65000 + 1 * 35000 + 1 * 14000 + 1 * 12000, X-ray crystallography
60000
-
1 * 120000-140000, alpha, contains biotin + 1 * 60000, beta, + 1 * 35000, gamma, hydrophobic, SDS-PAGE
60000
-
x * 120000, alpha, biotin carrier + x * 60000, beta, carboxytransferase, carboxylase + x * 30000, gamma, sodium pump, SDS-PAGE
60000
-
x * 120000, alpha, biotin carrier + x * 60000, beta, transferase + x * 30000, gamma, sodium-dependent carboxybiotin decarboxylase, SDS-PAGE
65000
-
x * 65000, alpha, carboxytransferase, + x * 39000, beta, decarboxylase, + x * 14000, gamma, biotin carrier, + x * 12000, delta, membrane anchor, deduced from gene sequence, expression and purification of alpha leads to a homotrimer, SDS-PAGE
65000
-
x * 65000 alpha, carboxytransferase + x * 33000, beta, carboxylyase + x * 19000, gamma, biotin carrier + x * 16000, probably carboxylyase, SDS-PAGE
65000
1 * 65000 + 1 * 35000 + 1 * 14000 + 1 * 12000, X-ray crystallography
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterotetramer
?
-
1 * 120000-140000, alpha, contains biotin + 1 * 60000, beta, + 1 * 35000, gamma, hydrophobic, SDS-PAGE
?
-
x * 120000, alpha, biotin carrier + x * 60000, beta, carboxytransferase, carboxylase + x * 30000, gamma, sodium pump, SDS-PAGE
?
-
x * 120000, alpha, biotin carrier + x * 60000, beta, transferase + x * 30000, gamma, sodium-dependent carboxybiotin decarboxylase, SDS-PAGE
?
-
x * 65000, alpha, carboxytransferase, + x * 39000, beta, decarboxylase, + x * 14000, gamma, biotin carrier, + x * 12000, delta, membrane anchor, deduced from gene sequence, expression and purification of alpha leads to a homotrimer, SDS-PAGE
?
enzyme is composed of subunits GcdA (65 kDa), GcdB (36 kDa), GcdC (24 kDa) and GcdD (14 kDa), calculated from sequence
?
-
enzyme is composed of subunits GcdA (65 kDa), GcdB (36 kDa), GcdC (24 kDa) and GcdD (14 kDa), calculated from sequence
-
?
-
x * 65000 alpha, carboxytransferase + x * 33000, beta, carboxylyase + x * 19000, gamma, biotin carrier + x * 16000, probably carboxylyase, SDS-PAGE
heterotetramer
1 * 65000 + 1 * 35000 + 1 * 14000 + 1 * 12000, X-ray crystallography
heterotetramer
-
1 * 65000 + 1 * 35000 + 1 * 14000 + 1 * 12000, X-ray crystallography
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
subunit alpha, decarboxylase, in complex with glutaconyl-CoA, dimer
co-crystallization of the decarboxylase subunit GcdA with the substrate glutaconyl-CoA, the product crotonyl-CoA, and the substrate analogue glutaryl-CoA, sitting drop vapor diffusion method, using in 0.1 M sodium citrate, pH 5.6-6.5, 1 M ammonium phosphate, 27.5% (v/v) glycerol
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
37
-
200 mM KCl: 50% loss of activity after 4 min, 200 mM NaCl: 10% loss of activity after 15 min
37
-
200 mM KCl: 50% loss of activity after 4 min, 200 mM NaCl: 10% loss of activity after 15 min
37
-
200 mM KCl: 50% loss of activity after 4 min, 200 mM NaCl: 10% loss of activity after 15 min
37
-
200 mM KCl: 50% loss of activity after 4 min, 200 mM NaCl: 10% loss of activity after 15 min
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
sodium ions specifically protect the gamma chain from tryptic digestion
sodium ions specifically protect the gamma chain from tryptic digestion
-
sodium ions specifically protect the gamma chain from tryptic digestion
-
sodium ions specifically protect the gamma chain from tryptic digestion
-
sodium ions specifically protect the gamma chain from tryptic digestion
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1-butanol
1-butanol
-
concentration 1%, 50% loss of activity after 1 min in presence of 200 mM KCl, 50% loss of activity after 3 min in presence of 200 mM NaCl
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Strep-Tactin Sepharose column chromatography, Ni-NTA affinity chromatography, and avidin-biotin affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Haertel, U.; Eckel, E.; Koch, J.; Fuchs, G.; Linder, D.; Buckel, W.
Purification of glutaryl-CoA dehydrogenase from Pseudomonas sp., an enzyme involved in the anaerobic degradation of benzoate
Arch. Microbiol.
159
174-181
1993
Pseudomonas sp.
brenda
Buckel, W.; Semmler, R.
Purification, characterisation and reconstitution of glutaconyl-CoA decarboxylase, a biotin-dependent sodium pump from anaerobic bacteria
Eur. J. Biochem.
136
427-434
1983
Acidaminococcus fermentans, [Clostridium] symbiosum, Clostridium tetanomorphum, Peptoniphilus asaccharolyticus
brenda
Wohlfarth, G.; Buckel, P.; Buckel, W.
On the structure and function of glutaconyl-CoA, a biotin dependent sodium pump from anaerobic bacteria
Prog. Biotechnol.
2
111-116
1986
Acidaminococcus fermentans, Peptoniphilus asaccharolyticus
-
brenda
Beatrix, B.; Bendrat, K.; Rospert, S.; Buckel, W.
The biotin-dependent sodium ion pump glutaconyl-CoA decarboxylase from Fusobacterium nucleatum (subsp. nucleatum)
Arch. Microbiol.
154
362-369
1990
Acidaminococcus fermentans, [Clostridium] symbiosum, Fusobacterium nucleatum, Peptoniphilus asaccharolyticus
brenda
Buckel, W.; Liedke, H.
The sodium pump glutaconyl-CoA decarboxylase from Acidaminococcus fermentans. Specific cleavage by n-alkanols
Eur. J. Biochem.
156
251-257
1986
Acidaminococcus fermentans
brenda
Buckel, W.
Substrate stereochemistry of the biotin-dependent sodium pump glutacoynl-CoA decarboxylase from Acidaminococcus fermentans
Eur. J. Biochem.
156
259-263
1986
Acidaminococcus fermentans
brenda
Buckel, W.
Biotin-dependent decarboxylases as bacterial sodium pumps: Purification and reconstitution of glutaconyl-CoA decarboxylase from Acidaminococcus fermentans
Methods Enzymol.
125
547-558
1986
Acidaminococcus fermentans, [Clostridium] symbiosum, Fusobacterium nucleatum, Peptoniphilus asaccharolyticus
-
brenda
Braune, A.; Bendrat, K.; Rospert, S.; Buckel, W.
The sodium ion translocating glutaconyl-CoA decarboxylase from Acidaminococcus fermentans: cloning and function of the genes forming a second operon
Mol. Microbiol.
31
473-487
1999
Acidaminococcus fermentans
brenda
Buckel, W.
Sodium ion-translocating decarboxylases
Biochim. Biophys. Acta
1505
15-27
2001
Acidaminococcus fermentans
brenda
Schocke, L.; Schink, B.
Energetics and biochemistry of fermentative benzoate degradation by Syntrophus gentianae
Arch. Microbiol.
171
331-337
1999
Syntrophus gentianae
-
brenda
Wendt, K.S.; Schall, I.; Huber, R.; Buckel, W.; Jacob, U.
Crystal structure of the carboxyltransferase subunit of the bacterial sodium ion pump glutaconyl-coenzyme A decarboxylase
EMBO J.
22
3493-3502
2003
Acidaminococcus fermentans (Q06700), Acidaminococcus fermentans
brenda
Kress, D.; Bruegel, D.; Schall, I.; Linder, D.; Buckel, W.; Essen, L.O.
An asymmetric model for Na+-translocating glutaconyl-CoA decarboxylases
J. Biol. Chem.
284
28401-28409
2009
[Clostridium] symbiosum (B7TVP1), [Clostridium] symbiosum, [Clostridium] symbiosum HB25 (B7TVP1)
brenda
Haertel, U.; Buckel, W.
Sodium ion-dependent hydrogen production in Acidaminococcus fermentans
Arch. Microbiol.
166
350-356
1996
Acidaminococcus fermentans (Q06700 and Q9ZAA6 and Q9ZAA7 and Q9ZAA8), Acidaminococcus fermentans, Acidaminococcus fermentans DSM 20731 (Q06700 and Q9ZAA6 and Q9ZAA7 and Q9ZAA8)
brenda
Schoecke, L.; Schink, B.
Energetics and biochemistry of fermentative benzoate degradation by Syntrophus gentianae
Arch. Microbiol.
171
331-337
1999
Syntrophus gentianae, Syntrophus gentianae DSM 8423
-
brenda
Bendrat, K.; Buckel, W.
Cloning, sequencing and expression of the gene encoding the carboxytransferase subunit of the biotin-dependent Na+ pump glutaconyl-CoA decarboxylase from Acidaminococcus fermentans in Escherichia coli
Eur. J. Biochem.
211
697-702
1993
Acidaminococcus fermentans (Q06700 and Q9ZAA6 and Q9ZAA7 and Q9ZAA8), Acidaminococcus fermentans, Acidaminococcus fermentans DSM 20731 (Q06700 and Q9ZAA6 and Q9ZAA7 and Q9ZAA8)
brenda
Buckel, W.; Semmler, R.
A biotin-dependent sodium pump glutaconyl-CoA decarboxylase from Acidaminococcus fermentans
FEBS Lett.
148
35-38
1982
Acidaminococcus fermentans
brenda
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EXTERNAL LINKS (specific for EC-Number 7.2.4.5)
Transporter Classification Database (TCDB): 3.B.1.1.3
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