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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 1-anthracenecarboxylic acid + CoA
AMP + diphosphate + anthracene-1-carboxyl-CoA
show the reaction diagram
-
2% of the activity with hexanoic acid
-
?
ATP + 1-naphthoic acid + CoA
AMP + diphosphate + 1-naphthoyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + 1-naphthoic acid + CoA
AMP + diphosphate + 1-naphthoyl-CoA
show the reaction diagram
-
3% of the activity with hexanoic acid
-
?
ATP + 1-naphthoic acid + CoA
AMP + diphosphate + 1-naphthoyl-CoA
show the reaction diagram
-
less than 10% of the activity with hexanoic acid
-
?
ATP + 1-naphthylacetic acid + CoA
AMP + diphosphate + 1-naphthyl-acetyl-CoA
show the reaction diagram
-
18% of the activity with hexanoic acid
-
?
ATP + 1-naphthylacetic acid + CoA
AMP + diphosphate + 1-naphthyl-acetyl-CoA
show the reaction diagram
-
about 25% of the activity with hexanoic acid
-
?
ATP + 1-naphthylacetic acid + CoA
AMP + diphosphate + 1-naphthylacetoyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + 2-aminobenzoate + CoA
AMP + diphosphate + 2-aminobenzoyl-CoA
show the reaction diagram
-
1.4% of the activity with dodecanoate
-
?
ATP + 2-anthracenecarboxylic acid + CoA
AMP + diphosphate + anthracene-2-carboxyl-CoA
show the reaction diagram
-
16% of the activity with hexanoic acid
-
?
ATP + 2-naphthylacetic acid + CoA
AMP + diphosphate + 2-naphthyl-acetyl-CoA
show the reaction diagram
-
21% of the activity with hexanoic acid
-
?
ATP + 2-naphthylacetic acid + CoA
AMP + diphosphate + 2-naphthyl-acetyl-CoA
show the reaction diagram
-
about 35% of the activity with hexanoic acid
-
?
ATP + 3,4-methylenedioxycinnamic acid + CoA
AMP + diphosphate + 3,4-methylenedioxy-cinnamoyl-CoA
show the reaction diagram
O74725
high activity
-
-
?
ATP + 3-aminobenzoate + CoA
AMP + diphosphate + 3-aminobenzoyl-CoA
show the reaction diagram
-
29% of the activity with benzoate
-
?
ATP + 3-aminobenzoate + CoA
AMP + diphosphate + 3-aminobenzoyl-CoA
show the reaction diagram
-
5% of the activity with hexanoic acid
-
?
ATP + 3-chlorobenzoate + CoA
AMP + diphosphate + 3-chlorobenzoyl-CoA
show the reaction diagram
-
12% of the activity with hexanoic acid
-
?
ATP + 3-chlorobenzoate + CoA
AMP + diphosphate + 3-chlorobenzoyl-CoA
show the reaction diagram
-
126% of the activity with benzoate
-
?
ATP + 3-ethoxycinnamic acid + CoA
AMP + diphosphate + 3-ethoxy-cinnamoyl-CoA
show the reaction diagram
O74725
high activity
-
-
?
ATP + 3-methoxybenzoate + CoA
AMP + diphosphate + 3-methoxybenzoyl-CoA
show the reaction diagram
-
48% of the activity with hexanoic acid
-
?
ATP + 3-methoxybenzoate + CoA
AMP + diphosphate + 3-methoxybenzoyl-CoA
show the reaction diagram
-
54% of the activity with benzoate
-
?
ATP + 3-methoxycinnamic acid + CoA
AMP + diphosphate + 3-methoxy-cinnamoyl-CoA
show the reaction diagram
O74725
high activity
-
-
?
ATP + 3-methylbenzoate + CoA
AMP + diphosphate + 3-methylbenzoyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + 3-methylbenzoate + CoA
AMP + diphosphate + 3-methylbenzoyl-CoA
show the reaction diagram
-
138% of the activity with benzoate
-
?
ATP + 3-methylbenzoate + CoA
AMP + diphosphate + 3-methylbenzoyl-CoA
show the reaction diagram
-
23% of the activity with hexanoic acid
-
?
ATP + 3-nitrobenzoate + CoA
AMP + diphosphate + 3-nitrobenzoyl-CoA
show the reaction diagram
-
28% of the activity with benzoate
-
?
ATP + 4-aminobenzoate + CoA
AMP + diphosphate + 4-aminobenzoyl-CoA
show the reaction diagram
-
19% of the activity with benzoate
-
?
ATP + 4-aminobenzoate + CoA
AMP + diphosphate + 4-aminobenzoyl-CoA
show the reaction diagram
-
3% of the activity with hexanoic acid
-
?
ATP + 4-chlorobenzoate + CoA
AMP + diphosphate + 4-chlorobenzoyl-CoA
show the reaction diagram
-
17% of the activity with hexanoic acid
-
?
ATP + 4-chlorobenzoate + CoA
AMP + diphosphate + 4-chlorobenzoyl-CoA
show the reaction diagram
-
96% of the activity with benzoate
-
?
ATP + 4-heptylbenzoate + CoA
AMP + diphosphate + 4-heptylbenzoyl-CoA
show the reaction diagram
-
66% of the activity with hexanoic acid
-
?
ATP + 4-methoxybenzoate + CoA
AMP + diphosphate + 4-methoxybenzoyl-CoA
show the reaction diagram
-
43% of the activity with benzoate
-
?
ATP + 4-methoxybenzoate + CoA
AMP + diphosphate + 4-methoxybenzoyl-CoA
show the reaction diagram
-
47% of the activity with hexanoic acid
-
?
ATP + 4-methylbenzoate + CoA
AMP + diphosphate + 4-methylbenzoyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + 4-methylbenzoate + CoA
AMP + diphosphate + 4-methylbenzoyl-CoA
show the reaction diagram
-
114% of the activity with benzoate
-
?
ATP + 4-methylbenzoate + CoA
AMP + diphosphate + 4-methylbenzoyl-CoA
show the reaction diagram
-
59% of the activity with hexanoic acid
-
?
ATP + 4-nitrobenzoate + CoA
AMP + diphosphate + 4-nitrobenzoyl-CoA
show the reaction diagram
-
29% of the activity with benzoate
-
?
ATP + a medium chain fatty acid or an aromatic acid or an arylacetic acid + CoA
?
show the reaction diagram
-
the enzyme catalyzes the first reaction of glycine conjugation, which is an important route of detoxification of many xenobiotic and endogenous carboxylic acids
-
-
-
ATP + arachidonic acid + CoA
AMP + diphosphate + arachidonoyl-CoA
show the reaction diagram
-
5.2% of the activity with dodecanoate
-
?
ATP + benzoate + CoA
AMP + diphosphate + benzoyl-CoA
show the reaction diagram
-
-
-
?
ATP + benzoate + CoA
AMP + diphosphate + benzoyl-CoA
show the reaction diagram
-
0.3% of the activity with octanoate
-
?
ATP + benzoate + CoA
AMP + diphosphate + benzoyl-CoA
show the reaction diagram
-
19% of the activity with hexanoic acid
-
?
ATP + benzoate + CoA
AMP + diphosphate + benzoyl-CoA
show the reaction diagram
-
2.3% of the activity with dodecanoate
-
?
ATP + benzoate + CoA
AMP + diphosphate + benzoyl-CoA
show the reaction diagram
-
about 30% of the activity with hexanoic acid
-
?
ATP + benzoate + CoA
AMP + diphosphate + benzoyl-CoA
show the reaction diagram
-
bi uni uni bi ping pong mechanism with ATP binding first, followed in order by benzoate binding, diphosphate release, CoA binding, benzoyl-CoA release and AMP release
-
?
ATP + benzoate + CoA
AMP + diphosphate + benzoyl-CoA
show the reaction diagram
-
high activities are obtained with benzoate having methyl, pentyl, and methoxy groups in the para- or meta-positions of the benzene ring
-
-
?
ATP + benzoic acid + CoA
AMP + diphosphate + benzoyl-CoA
show the reaction diagram
-
also active with several benzoic acids substituted at position 2, 3 or 4
-
-
-
ATP + butyrate + CoA
AMP + diphosphate + butyryl-CoA
show the reaction diagram
-
-
-
-
-
ATP + butyrate + CoA
AMP + diphosphate + butyryl-CoA
show the reaction diagram
-
-
-
-
ATP + butyrate + CoA
AMP + diphosphate + butyryl-CoA
show the reaction diagram
-
-
-
-
ATP + butyrate + CoA
AMP + diphosphate + butyryl-CoA
show the reaction diagram
-
-
-
-
-
ATP + butyrate + CoA
AMP + diphosphate + butyryl-CoA
show the reaction diagram
-
-
-
-
ATP + butyrate + CoA
AMP + diphosphate + butyryl-CoA
show the reaction diagram
-
-
-
-
-
ATP + butyrate + CoA
AMP + diphosphate + butyryl-CoA
show the reaction diagram
-
-
-
?
ATP + butyrate + CoA
AMP + diphosphate + butyryl-CoA
show the reaction diagram
-
-
-
-
ATP + butyrate + CoA
AMP + diphosphate + butyryl-CoA
show the reaction diagram
-
-
-
-
ATP + butyrate + CoA
AMP + diphosphate + butyryl-CoA
show the reaction diagram
-
-
-
-
-
ATP + butyrate + CoA
AMP + diphosphate + butyryl-CoA
show the reaction diagram
-
no activity with GTP
-
-
-
ATP + butyrate + CoA
AMP + diphosphate + butyryl-CoA
show the reaction diagram
-
46% of the activity with octanoate
-
?
ATP + butyrate + CoA
AMP + diphosphate + butyryl-CoA
show the reaction diagram
Paecilomyces variotii AHU 9417
-
-
-
-
ATP + caproic acid + CoA
AMP + diphosphate + caproyl-CoA
show the reaction diagram
O74725
-
-
-
?
ATP + crotonate + CoA
AMP + diphosphate + crotonyl-CoA
show the reaction diagram
-
i.e. E-2-butenoate, 20% of the activity relative to butyrate
-
-
-
ATP + cyclohexanoic acid + CoA
AMP + diphosphate + cyclohexanoyl-CoA
show the reaction diagram
-
41% of the activity with hexanoic acid
-
?
ATP + decanoate + CoA
AMP + diphosphate + decanoyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + decanoate + CoA
AMP + diphosphate + decanoyl-CoA
show the reaction diagram
-
48% of the activity with octanoate
-
?
ATP + decanoate + CoA
AMP + diphosphate + decanoyl-CoA
show the reaction diagram
-
substrate with the highest activity
-
?
ATP + dodecanoate + CoA
AMP + diphosphate + dodecanoyl-CoA
show the reaction diagram
-
-
-
-
-
ATP + dodecanoate + CoA
AMP + diphosphate + dodecanoyl-CoA
show the reaction diagram
-
31% of the activity with dodecanoate
-
?
ATP + dodecanoate + CoA
AMP + diphosphate + dodecanoyl-CoA
show the reaction diagram
-
39% of the activity with hexanoic acid
-
?
ATP + heptanoate + CoA
AMP + diphosphate + heptanoyl-CoA
show the reaction diagram
-
-
-
-
-
ATP + heptanoate + CoA
AMP + diphosphate + heptanoyl-CoA
show the reaction diagram
-
34% of the activity with dodecanoate
-
?
ATP + hexanoate + CoA
AMP + diphosphate + hexanoyl-CoA
show the reaction diagram
-
-
-
?
ATP + hexanoate + CoA
AMP + diphosphate + hexanoyl-CoA
show the reaction diagram
-
-
-
-
-
ATP + hexanoate + CoA
AMP + diphosphate + hexanoyl-CoA
show the reaction diagram
-
-
-
?
ATP + hexanoate + CoA
AMP + diphosphate + hexanoyl-CoA
show the reaction diagram
-
highest activity
-
-
-
ATP + hexanoate + CoA
AMP + diphosphate + hexanoyl-CoA
show the reaction diagram
-
15% of the activity with octanoate
-
?
ATP + hexanoate + CoA
AMP + diphosphate + hexanoyl-CoA
show the reaction diagram
-
15% of the activity with octanoate
-
?
ATP + hexanoate + CoA
AMP + diphosphate + hexanoyl-CoA
show the reaction diagram
-
35% of the activity with dodecanoate
-
?
ATP + hexanoate + CoA
AMP + diphosphate + hexanoyl-CoA
show the reaction diagram
-
maximal activity on hexanoate
-
-
?
ATP + indomethacin + CoA
AMP + diphosphate + ?
show the reaction diagram
-
6% of the activity with hexanoic acid
-
?
ATP + indomethacin + CoA
AMP + diphosphate + ?
show the reaction diagram
-
less than 5% of the activity with hexanoic acid
-
?
ATP + isobutyrate + CoA
AMP + diphosphate + isobutyryl-CoA
show the reaction diagram
-
-
-
-
-
ATP + isobutyrate + CoA
AMP + diphosphate + isobutyryl-CoA
show the reaction diagram
-
20% of the activity relative to butyrate
-
-
-
ATP + isopentanoate
AMP + diphosphate + isopentanoyl-CoA
show the reaction diagram
-
-
-
-
-
ATP + ketoprofen + CoA
ADP + diphosphate + ?
show the reaction diagram
-
less active on ketoprofen
-
-
?
ATP + L-(+)-3-hydroxybutyrate + CoA
AMP + diphosphate + L-(+)-3-hydroxybutyryl-CoA
show the reaction diagram
-
-
-
-
ATP + L-(+)-3-hydroxybutyrate + CoA
?
show the reaction diagram
-
enzyme reesterifies CoA and L-(+)-3-hydroxybutyrate. It is required for the production of L-(+)-3-hydroxybutyrate in rat liver
-
-
-
ATP + laurate + CoA
AMP + diphosphate + lauroyl-CoA
show the reaction diagram
-
12.6% of the activity with octanoate
-
?
ATP + linolenic acid + CoA
AMP + diphosphate + linolenoyl-CoA
show the reaction diagram
-
8.3% of the activity with dodecanoate
-
?
ATP + m-hydroxybenzoate + CoA
AMP + diphosphate + m-hydroxybenzoyl-CoA
show the reaction diagram
-
0.8% of the activity with dodecanoate
-
?
ATP + m-methoxybenzoate + CoA
AMP + diphosphate + m-methoxybenzoyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + m-pentylbenzoate + CoA
AMP + diphosphate + m-pentylbenzoyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + myristic acid + CoA
AMP + diphosphate + myristoyl-CoA
show the reaction diagram
O74725
-
-
-
?
ATP + octanoate + CoA
AMP + diphosphate + octanoyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + octanoate + CoA
AMP + diphosphate + octanoyl-CoA
show the reaction diagram
-
-
-
?
ATP + octanoate + CoA
AMP + diphosphate + octanoyl-CoA
show the reaction diagram
-
-
-
-
-
ATP + octanoate + CoA
AMP + diphosphate + octanoyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + octanoate + CoA
AMP + diphosphate + octanoyl-CoA
show the reaction diagram
-
31% of the activity with dodecanoate
-
?
ATP + octanoate + CoA
AMP + diphosphate + octanoyl-CoA
show the reaction diagram
-
about 50% of the activity with hexanoic acid
-
?
ATP + p-methoxybenzoate + CoA
AMP + diphosphate + p-methoxybenzoyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + p-pentylbenzoate + CoA
AMP + diphosphate + p-pentylbenzoyl-CoA
show the reaction diagram
-
-
-
-
?
ATP + pentanoate + CoA
AMP + diphosphate + pentanoyl-CoA
show the reaction diagram
-
-
-
-
-
ATP + pentanoate + CoA
AMP + diphosphate + pentanoyl-CoA
show the reaction diagram
-
1.6% of the activity with dodecanoate
-
?
ATP + pentanoate + CoA
AMP + diphosphate + pentanoyl-CoA
show the reaction diagram
Paecilomyces variotii AHU 9417
-
-
-
-
-
ATP + phenoxyacetate + CoA
AMP + diphosphate + phenoxyacetyl-CoA
show the reaction diagram
O74725
i.e. POA, low activity
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
show the reaction diagram
-
-
-
?
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
show the reaction diagram
O74725
enzymatic activation of phenylacetic acid to phenylacetyl-CoA is an important step in the biosynthesis of the beta-lactam antibiotic penicillin G by the fungus Penicillium chrysogenum, CoA esters of PAA and phenoxyacetic acid act as acyl donor in the exchange of the aminoadipyl side chain of isopenicillin N to produce penicillin G or penicillin V, i.e. PAA
-
-
?
ATP + propionate + CoA
AMP + diphosphate + propionyl-CoA
show the reaction diagram
-
-
-
-
-
ATP + propionate + CoA
AMP + diphosphate + propionyl-CoA
show the reaction diagram
-
2% of the activity with octanoate
-
?
ATP + propionate + CoA
AMP + diphosphate + propionyl-CoA
show the reaction diagram
Paecilomyces variotii AHU 9417
-
-
-
-
-
ATP + propionic acid + CoA
AMP + diphosphate + propioyl-CoA
show the reaction diagram
O74725
low activity
-
-
?
ATP + tetradecanoate + CoA
AMP + diphosphate + tetradecanoyl-CoA
show the reaction diagram
-
3.9% of the activity with dodecanoate
-
?
ATP + tranexamic acid + CoA
AMP + diphosphate + tranexoyl-CoA
show the reaction diagram
-
7% of the activity with hexanoic acid
-
?
ATP + tranexamic acid + CoA
AMP + diphosphate + tranexoyl-CoA
show the reaction diagram
-
less than 10% of the activity with hexanoic acid
-
?
ATP + trans-4-coumaric acid + CoA
AMP + diphosphate + trans-4-coumaroyl-CoA
show the reaction diagram
O74725
-
-
-
?
ATP + trans-cinnamic acid + CoA
AMP + diphosphate + trans-cinnamoyl-CoA
show the reaction diagram
O74725
1000fold higher activity compared to PAA
-
-
?
ATP + tridecanoate + CoA
AMP + diphosphate + tridecanoyl-CoA
show the reaction diagram
-
15% of the activity with dodecanoate
-
?
ATP + valerate + CoA
AMP + diphosphate + valeryl-CoA
show the reaction diagram
-
9.9% of the activity with octanoate
-
?
ATP + valproate + CoA
ADP + diphosphate + valproyl-CoA
show the reaction diagram
-
less active on valproate
-
-
?
ATP + valproic acid + CoA
AMP + diphosphate + valproyl-CoA
show the reaction diagram
-
i.e. 2-n-propylpentanoic acid
-
-
-
ATP + valproic acid + CoA
AMP + diphosphate + valproyl-CoA
show the reaction diagram
-
less than 10% of the activity with hexanoic acid
-
?
CTP + butyrate + CoA
CMP + diphosphate + butyryl-CoA
show the reaction diagram
-
slight activity
-
-
-
ITP + butyrate + CoA
IMP + diphosphate + butyryl-CoA
show the reaction diagram
-
slight activity
-
-
-
additional information
?
-
-
no activity with hexanoate
-
-
-
additional information
?
-
-
no activity with formate and heptanoate, straight chain acids having 3, 5 or 6 carbons are less active as substrates than butyrate, no activity with acetate and octanoate
-
-
-
additional information
?
-
-
no activity with acetate and octanoate
-
-
-
additional information
?
-
-
major enzyme for glycine conjugation of benzoic acids with electron-donating groups in bovine liver mitochondria
-
-
-
additional information
?
-
-
the enzyme catalyzes the first reaction of glycine conjugation
-
?
additional information
?
-
-
the enzyme is involved in the metabolism of fatty acid during mycobacterial survival in macrophages
-
?
additional information
?
-
-
the enzyme is responsible for glycine conjugation
-
?
additional information
?
-
O74725
the enzyme also belongs to EC 6.2.1.30, substrate specificity, the more substituted compounds ferulic acid, caffeic acid and sinapic acid, which are substrates for most 4-coumarate CoA ligases, are very poor substrates for the enzyme. With the exception of acetic acid, all short and medium chain fatty acids tested are converted by the enzyme, the enzyme is able to activate all the side chains of these naturally occurring lactam side products, overview. Residues H265, I266, Y267, V270, F307, F335, G337, A338, G361, T369, V370, and K557 are involved in substrate binding
-
-
-
additional information
?
-
Paecilomyces variotii AHU 9417
-
no activity with hexanoate, no activity with acetate and octanoate
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + a medium chain fatty acid or an aromatic acid or an arylacetic acid + CoA
?
show the reaction diagram
-
the enzyme catalyzes the first reaction of glycine conjugation, which is an important route of detoxification of many xenobiotic and endogenous carboxylic acids
-
-
-
ATP + L-(+)-3-hydroxybutyrate + CoA
?
show the reaction diagram
-
enzyme reesterifies CoA and L-(+)-3-hydroxybutyrate. It is required for the production of L-(+)-3-hydroxybutyrate in rat liver
-
-
-
ATP + phenylacetate + CoA
AMP + diphosphate + phenylacetyl-CoA
show the reaction diagram
O74725
enzymatic activation of phenylacetic acid to phenylacetyl-CoA is an important step in the biosynthesis of the beta-lactam antibiotic penicillin G by the fungus Penicillium chrysogenum, CoA esters of PAA and phenoxyacetic acid act as acyl donor in the exchange of the aminoadipyl side chain of isopenicillin N to produce penicillin G or penicillin V
-
-
?
additional information
?
-
-
major enzyme for glycine conjugation of benzoic acids with electron-donating groups in bovine liver mitochondria
-
-
-
additional information
?
-
-
the enzyme catalyzes the first reaction of glycine conjugation
-
?
additional information
?
-
-
the enzyme is involved in the metabolism of fatty acid during mycobacterial survival in macrophages
-
?
additional information
?
-
-
the enzyme is responsible for glycine conjugation
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
ATP
O74725
dependent on
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
can replace Mg2+ in activation with 47% of the efficiency, Km: 0.14 mM
K+
-
increases activity 10fold
K+
-
requires both Mg2+ and K+, Km: 2.4 mM
Mg2+
-
activates
Mg2+
-
absolute requirement
Mg2+
-
requires both Mg2+ and K+
Mg2+
-
Km: 1.8 mM; required
Mg2+
O74725
dependent on, optimal at 5 mM
Mn2+
-
can replace Mg2+ in activation; with 128% of the activation compared to Mg2+, Km: 0.14 mM
NaCl
O74725
stabilizes at 200 mM
Rb+
-
can replace K+ in activation with 81% efficiency, Km: 2.4 mM
Mn2+
-
can replace Mg2+ in activation
additional information
-
no differential response to monovalent cations
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(NH4)2SO4
-
-
2-hydroxydodecanoic acid
-
-
2-hydroxydodecanoic acid
-
competitive; potent
2-hydroxydodecanoic acid
-
-
2-hydroxydodecanoic acid
-
0.04 mM, 48% inhibition
2-Hydroxynaphthoic acid
-
competitive; potent
2-Hydroxynaphthoic acid
-
competitive with respect to hexanoate
2-Hydroxyoctanoic acid
-
competitive with respect to hexanoate
2-hydroxyphenylacetic acid
-
-
4-methylsalicylic acid
-
competitive with respect to hexanoate
5,5'-dithiobis(2-nitrobenzoate)
-
-
AMP
-
product inhibitor
AMP
-
competitive for ATP
Benzoate
-
competitive inhibitor of butyrate
benzoyl-CoA
-
product inhibitor
Butyrate
-
competitive inhibitor of benzoate
Butyryl-CoA
-
competitive inhibitor with respect to both butyrate and benzoate
Butyryl-CoA
-
competitive for ATP
cyclohexane carboxylate
-
-
diflunisal
-
competitive
diflunisal
-
competitive; potent
diflunisal
-
0.002 mM, 55% inhibition
diflunisal
-
0.001 mM, complete inhibition
diphosphate
-
weak product inhibitor, competitive with respect to CoA and mixed inhibitor with respect to benzoate. Mixed type inhibitor with respect to CoA in butyrate:CoA ligase activity
diphosphate
-
competitive for CoA
dithiothreitol
-
-
enoxacin
-
potent, mixed-type inhibition
felbinac
-
inhibits activity with hexanoic acid, IC50: 0.025 mM
iodoacetamide
-
-
Mercury compounds
-
-
-
Nalidixic acid
-
competitive
Nalidixic acid
-
competitive; potent
Nalidixic acid
-
0.001 mM, complete inhibition
Octanoate
-
valproyl-AMP synthesis
ofloxacin
-
potent, mixed-type inhibition
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
butyrate or ATP partially protects
salicylic acid
-
competitive; potent
salicylic acid
-
0.05 mM, 53% inhibition
salicylic acid
-
0.001 mM, complete inhibition
salicylic acid
-
-
salicylic acid
-
competitive with respect to hexanoate
Silver compounds
-
-
-
sulfhydryl reagents
-
-
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
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.08
-
ATP
-
-
0.2
-
ATP
-
-
0.48
-
ATP
O74725
pH 8.5, 30C, recombinant enzyme, with trans-cinnamic acid
0.65
-
ATP
O74725
pH 8.5, 30C, recombinant enzyme, with phenylacetic acid
3
-
ATP
-
-
0.007
-
Benzoate
-
-
0.14
-
Butyrate
-
ATP
0.731
-
Butyrate
-
-
1.5
-
Butyrate
-
-
4.2
-
Butyrate
-
-
0.02
-
CoA
-
-
0.06
-
CoA
-
-
0.12
-
CoA
O74725
pH 8.5, 30C, recombinant enzyme, with phenylacetic acid
0.85
-
CoA
-
-
0.94
-
CoA
O74725
pH 8.5, 30C, recombinant enzyme, with trans-cinnamic acid
1.775
-
Decanoate
-
-
0.02
-
dodecanoate
-
-
1.6
-
Isobutyrate
-
-
0.47
-
Isopentanoate
-
-
4
-
L-(+)-3-hydroxybutyrate
-
-
0.001
-
myristic acid
O74725
below, pH 8.5, 30C, recombinant enzyme
0.108
-
Octanoate
-
-
0.285
-
Octanoate
-
-
0.38
-
pentanoate
-
-
2.1
-
Phenoxyacetate
O74725
pH 8.5, 30C, recombinant enzyme
5.2
6.1
phenylacetate
O74725
pH 8.5, 30C, recombinant enzyme
3.3
-
Propionate
-
-
80
-
Propionic acid
O74725
pH 8.5, 30C, recombinant enzyme
0.19
-
trans-Cinnamic acid
O74725
pH 8.5, 30C, recombinant enzyme
0.97
-
MgATP2-
-
-
additional information
-
additional information
-
the relation between enzyme activity and protein concentration is non-linear
-
additional information
-
additional information
O74725
kinetics with diverse substrates, overview
-
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
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0044
-
2-hydroxydodecanoic acid
-
pH 8.5
0.015
-
2-hydroxydodecanoic acid
-
pH 8.5, 37C
0.0134
-
2-Hydroxynaphthoic acid
-
pH 8.5, 37C
0.37
-
2-hydroxyphenylacetic acid
-
pH 8.5
0.17
-
cyclohexane carboxylate
-
reaction with butyrate as substrate
0.0006
-
diflunisal
-
pH 8.5, 37C
0.0008
-
diflunisal
-
pH 8.5
0.0123
-
Nalidixic acid
-
pH 8.5
0.0124
-
Nalidixic acid
-
pH 8.5, 37C
0.0382
-
ofloxacine
-
-
0.0196
-
salicylic acid
-
pH 8.5, 37C
0.0237
-
enoxacin
-
-
additional information
-
additional information
O74725
inhibition kinetics
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.025
-
felbinac
-
inhibits activity with hexanoic acid, IC50: 0.025 mM
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.02
-
O74725
purified recombinant enzyme
0.023
-
-
cell extract, with 0.001 mM hexanoic acid as a substrate in 0.2 M Tris-HCl buffer (pH 8.5)
3.3
-
-
-
3.718
-
-
-
4.14
-
-
after 180fold purification, with 0.001 mM hexanoic acid as a substrate in 0.2 M Tris-HCl buffer (pH 8.5)
4.15
-
-
-
additional information
-
-
-
additional information
-
-, Q54CJ4
total lipid composition, profiling of the total fatty acid
additional information
-
O74725
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
-
-
reaction with butyrate as substrate
8
-
-
broad pH-optimum around
8.6
-
-
reaction with octanoate as substrate
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.8
8
-
increase of activity when the pH increases from 6.8 to 8
8.5
10
-
8.5: 53% of maximal activity, 10.0: 80% of maximal activity, a pH-optimum is not observed
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
in vivo the enzyme is linked to a mitochondrial membrane by a bond cleavable by disulfide bond reducing agents
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
41000
-
-
sedimentation equilibrium measurement
41000
-
-
gel filtration
46500
-
-
gel filtration
64000
-
-
monomeric form of enzyme, gel filtration
65000
-
-
SDS-PAGE
130000
-
-
dimeric form of enzyme, gel filtration
142000
-
-
disc gel electrophoresis
145000
-
-
gel filtration
260000
-
-
tetrameric form of enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 38000, SDS-PAGE
?
O74725
x * 62600, recombinant enzyme, SDS-PAGE
dimer
-
2 * 74000, SDS-PAGE
dimer
-
x * 65000, the enzyme exists in monomeric, dimeric and tertameric form, SDS-PAGE
dimer
Paecilomyces variotii AHU 9417
-
2 * 74000, SDS-PAGE
-
tetramer
-
4 * 37000, SDS-PAGE
tetramer
-
x * 65000, the enzyme exists in monomeric, dimeric and tertameric form, SDS-PAGE
monomer
-
1 * 65000, the enzyme exists in monomeric, dimeric and tertameric form, SDS-PAGE
additional information
-, Q54CJ4
EloA membrane topology model where the ELO consensus motifs are located at the cytosolic face of the membrane consistent with their potential role in the catalytic activity of EloA
additional information
O74725
enzyme structure modelling of wild-type and mutant enzymes using the crystal structure of the luciferase from firefly species Luciola cruciata as template, PDB ID 2D1S
additional information
Dictyostelium discoideum AX3
-
EloA membrane topology model where the ELO consensus motifs are located at the cytosolic face of the membrane consistent with their potential role in the catalytic activity of EloA
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
9
-
37C, 15 min, stable
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
pH 4.0-9.0, 15 min, stable
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
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Sephadex G-25 gel filtration, DEAE-Sepharose column chromatography, and hydroxylapatite column chromatography
-
enzyme form HXM-A and HXM-B
-
Sephadex G-25 gel filtration, DEAE-Sepharose column chromatography, and hydroxylapatite column chromatography
-
partial
-
recombinant C-terminally His6-tagged maltose binding protein fusion from Escherichia coli by nickel affinity chromatography, the MBP is cleaved off by factor Xa, imidazole is eliminated by gel filtration, recombinant His-tagged mutants
O74725
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
gene eloA, phylogenetic analysis, expression of the putative Dictyostelium discoideum eloA cDNA in Saccharomces cerevisiae
-, Q54CJ4
expression of HXM-A in COS cells
-
a plasmid with a His-tagged fusion protein is constructed for expression in Escherichia coli
-
gene phl, sequence analysis, functional expression as C-terminally His6-tagged maltose binding protein fusion in Escherichia coli, expression of His-tagged mutants
O74725
expressed in Escherichia coli DH5alpha and BL21(DE) cells
-
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
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
involvement of the MACS2 Leu513Ser polymorphism in the development of the metabolic syndrome