Information on EC 4.1.1.70 - glutaconyl-CoA decarboxylase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY hide
4.1.1.70
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RECOMMENDED NAME
GeneOntology No.
glutaconyl-CoA decarboxylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4-carboxybut-2-enoyl-CoA = but-2-enoyl-CoA + CO2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Benzoate degradation
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Butanoate metabolism
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crotonate fermentation (to acetate and cyclohexane carboxylate)
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glutamate and glutamine metabolism
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glutaryl-CoA degradation
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L-glutamate degradation V (via hydroxyglutarate)
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Microbial metabolism in diverse environments
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tryptophan metabolism
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SYSTEMATIC NAME
IUBMB Comments
4-carboxybut-2-enoyl-CoA carboxy-lyase (but-2-enoyl-CoA-forming)
The enzyme from 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.
CAS REGISTRY NUMBER
COMMENTARY hide
84399-93-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
subunit A; strain HB25
UniProt
Manually annotated by BRENDA team
enzyme also decarboxylates glutaryl-CoA
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-carboxybut-2-enoyl-CoA
but-2-enoyl-CoA + CO2
show the reaction diagram
glutaconyl-CoA
but-2-enoyl-CoA + CO2
show the reaction diagram
glutaryl-CoA
butyryl-CoA + CO2
show the reaction diagram
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-
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
glutaconyl-CoA
but-2-enoyl-CoA + CO2
show the reaction diagram
additional information
?
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pathway of fermentative benzoate degradation
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
biotin
FAD
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1.1 mol of FAD per subunit, Km: 0.00025 mM
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Avidin
deoxycholate
ethanol
glutaryl-CoA
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competitive to glutaconyl-CoA
N-Alkanols
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concentration required for complete inactivation decreases N-dodecyl-N-dimethylaminoxide at 20-30C
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N-ethylmaleimide
Triton X-114
additional information
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with increasing chain length, sodium ions prevent inactivation, Li+ is ten times less effective than Na+
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
biotin
Brij 35
Phospholipid
Triton X-100
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6 - 11
glutaconyl-CoA
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28C, pH 7.5
3 - 5
glutaryl-CoA
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28C, pH 7.5
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0074
glutaryl-CoA
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48
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cell free extract, pH 7.2, 22C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
170000
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gel filtration
232000
gel filtration
additional information
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in sucrose density gradient centrifugation the activity is recovered in 2 peaks: MW 470000, possibly dimer and MW 250000, possibly monomer
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterotetramer
tetramer
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4 * 41000, SDS-PAGE
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
requires Na+ for stability
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sodium ions specifically protect the gamma chain from tryptic digestion
unstable in the presence of buffers containing potassium
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1-butanol
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, little loss of activity after 1 year
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-80C, 24 h, 100 mM Na+, stable
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4C, 24 h, 100 mM Na+, 50% loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Strep-Tactin Sepharose column chromatography, Ni-NTA affinity chromatography, and avidin-biotin affinity chromatography
subsp. nucleatum
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli Rosetta (DE3) cells
four different subunits
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Show AA Sequence (469 entries)
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