Information on EC 6.2.1.2 - butyrate-CoA ligase

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

EC NUMBER
COMMENTARY
6.2.1.2
-
RECOMMENDED NAME
GeneOntology No.
butyrate-CoA ligase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ATP + a carboxylate + CoA = AMP + diphosphate + an acyl-CoA
show the reaction diagram
-
-
-
-
ATP + a carboxylate + CoA = AMP + diphosphate + an acyl-CoA
show the reaction diagram
bi uni uni bi ping-pong mechanism, in which the order of addition and evolution of substrates and products is ATP, butyrate, diphosphate, CoA, butyryl-CoA or AMP, and AMP or butyryl-CoA. Butyryl-CoA and AMP are evolved at random or at the same time
-
ATP + a carboxylate + CoA = AMP + diphosphate + an acyl-CoA
show the reaction diagram
bi uni uni bi ping-pong mechanism, in which the order of addition and evolution of substrates and products is ATP, butyrate, diphosphate, CoA, butyryl-CoA or AMP, and AMP or butyryl-CoA. Butyryl-CoA and AMP are evolved at random or at the same time
Paecilomyces variotii AHU 9417
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Acid-thiol ligation
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Butanoate metabolism
-
Metabolic pathways
-
methyl ketone biosynthesis
-
SYSTEMATIC NAME
IUBMB Comments
butanoate:CoA ligase (AMP-forming)
Acts on acids from C4 to C11 and on the corresponding 3-hydroxy- and 2,3- or 3,4-unsaturated acids.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Acyl-activating enzyme
-
-
-
-
Butyryl-CoA synthetase
-
-
-
-
Butyryl-coenzyme A synthetase
-
-
-
-
EloA
Dictyostelium discoideum AX3
Q54CJ4
-
-
elongase
Q54CJ4
-
elongase
Dictyostelium discoideum AX3
Q54CJ4
-
-
Fatty acid thiokinase (medium chain)
-
-
-
-
L-(+)-3-Hydroxybutyryl CoA ligase
-
-
-
-
MACS2
-
-
medium chain acyl-CoA synthase
-
-
medium chain acyl-CoA synthetase
-
-
Medium chain acyl-coenzyme A synthetase
-
-
-
-
medium-chain acyl-CoA synthetase 2
-
-
Short-chain acyl-CoA synthetase
-
-
-
-
Synthetase, butyryl conzyme A
-
-
-
-
xenobiotic/medium-chain fatty acid:CoA ligase
-
-
xenobiotic/medium-chain fatty acid:CoA ligase
-
-
XM-ligase
-
-
Mig protein
-
-
additional information
Q54CJ4
the Dictyostelium genome possesses members of both the ELO and KCS fatty acid elongase families
additional information
Dictyostelium discoideum AX3
Q54CJ4
the Dictyostelium genome possesses members of both the ELO and KCS fatty acid elongase families
-
additional information
O74725
cf. 6.2.1.30
CAS REGISTRY NUMBER
COMMENTARY
9080-51-7
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
axenic strain, AX3, gene eloA
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain AHU 9417
-
-
Manually annotated by BRENDA team
Paecilomyces variotii AHU 9417
strain AHU 9417
-
-
Manually annotated by BRENDA team
gene phl or pclA; gene phl
UniProt
Manually annotated by BRENDA team
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
ATP
O74725
dependent on
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Bovine serum albumin
-
activates 5fold to 6fold
-
Bovine serum albumin
-
-
-
iodoacetate
-
activates up to 80% by low concentrations, in a 1:1 molar ratio with the 40000 MW species of the enzyme
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.7
-
ATP
O74725
pH 8.5, 30C, recombinant enzyme, with phenylacetic acid
42.9
-
ATP
O74725
pH 8.5, 30C, recombinant enzyme, with trans-cinnamic acid
1.5
-
CoA
O74725
pH 8.5, 30C, recombinant enzyme, with phenylacetic acid
60.5
-
CoA
O74725
pH 8.5, 30C, recombinant enzyme, with trans-cinnamic acid
12
-
Phenoxyacetate
O74725
pH 8.5, 30C, recombinant enzyme
1.3
1.9
phenylacetate
O74725
pH 8.5, 30C, recombinant enzyme
41.2
-
trans-Cinnamic acid
O74725
pH 8.5, 30C, recombinant enzyme
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
presence of 200 mM NaCl is essential for the stability of the enzyme and storage or conversions in buffer lacking NaCl resulted in rapid loss of activity
O74725
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, purified recobnant protein in TANG buffer, several months without significant loss of activity
O74725
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
F307A
O74725
site-directed mutagenesis, the mutant shows an increased Km for phenoxyacetic acid compared to the wild-type enzyme
V270A
O74725
site-directed mutagenesis, the mutant activity is similar to the wild-type enzyme
V370A
O74725
site-directed mutagenesis, the mutant activity is similar to the wild-type enzyme
Y267A
O74725
site-directed mutagenesis, the mutant shows an increased Km for phenoxyacetic acid compared to the wild-type enzyme
F335A
O74725
site-directed mutagenesis, the mutant shows an increased Km for phenoxyacetic acid compared to the wild-type enzyme
additional information
O74725
construction of mutants with substrate binding pocket residues exchanged for alanine, the mutants show altered kinetics, overview