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Information on EC 6.2.1.2 - medium-chain acyl-CoA ligase and Organism(s) Mus musculus
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6.2.1.2 medium-chain acyl-CoA ligaseIUBMB Comments
Acts on fatty acids from C4 to C11 and on the corresponding 3-hydroxy and 2,3- or 3,4-unsaturated acids. The enzyme from the bacterium Pseudomonas putida also acts on 4-oxo and 4-hydroxy derivatives.
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Word Map
- 6.2.1.2
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desaturase
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polyunsaturated
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pufas
-
docosahexaenoic
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arachidonic
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monounsaturated
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eicosapentaenoic
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linoleic
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desaturation
- elovl5
- unsaturated
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lc-pufas
- acyl-coas
-
oleic
- stearoyl-coa
-
very-long-chain
-
vlcfas
-
palmitoleic
-
delta6
-
stearic
-
alpha-linolenic
-
linseed
-
gamma-linolenic
- alpina
- stargardt
- mortierella
- isochrysis
- 3-ketoacyl-coa
-
erucic
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cis-vaccenic
-
vaccenic
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dihomo-gamma-linolenic
- medicine
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stearidonic
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
elongase, macs2, mig protein, medium chain acyl-coa synthetase, butyryl-coa synthetase, xm-ligase, short-chain acyl-coa synthetase, xenobiotic/medium-chain fatty acid:coa ligase, medium chain acyl-coenzyme a synthetase, butyryl-coenzyme a synthetase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Acyl-activating enzyme
-
-
-
-
butanoate:CoA ligase (AMP-forming)
-
-
-
-
butyrate-CoA ligase
-
-
-
-
Butyryl-CoA synthetase
-
-
-
-
Butyryl-coenzyme A synthetase
-
-
-
-
Fatty acid thiokinase (medium chain)
-
-
-
-
L-(+)-3-Hydroxybutyryl CoA ligase
-
-
-
-
Medium chain acyl-coenzyme A synthetase
-
-
-
-
Short-chain acyl-CoA synthetase
-
-
-
-
Synthetase, butyryl conzyme A
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acid-thiol ligation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
medium-chain fatty acid:CoA ligase (AMP-forming)
Acts on fatty acids from C4 to C11 and on the corresponding 3-hydroxy and 2,3- or 3,4-unsaturated acids. The enzyme from the bacterium Pseudomonas putida also acts on 4-oxo and 4-hydroxy derivatives.
CAS REGISTRY NUMBER
COMMENTARY
9080-51-7
-
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
ATP + 1-naphthylacetic acid + CoA
AMP + diphosphate + 1-naphthyl-acetyl-CoA
-
about 25% of the activity with hexanoic acid
-
?
ATP + 1-naphthylacetic acid + CoA
AMP + diphosphate + 1-naphthylacetoyl-CoA
-
-
-
-
?
ATP + 2-naphthylacetic acid + CoA
AMP + diphosphate + 2-naphthyl-acetyl-CoA
-
about 35% of the activity with hexanoic acid
-
?
ATP + 3-aminobenzoate + CoA
AMP + diphosphate + 3-aminobenzoyl-CoA
-
29% of the activity with benzoate
-
?
ATP + 3-chlorobenzoate + CoA
AMP + diphosphate + 3-chlorobenzoyl-CoA
-
126% of the activity with benzoate
-
?
ATP + 3-methoxybenzoate + CoA
AMP + diphosphate + 3-methoxybenzoyl-CoA
-
54% of the activity with benzoate
-
?
ATP + 3-nitrobenzoate + CoA
AMP + diphosphate + 3-nitrobenzoyl-CoA
-
28% of the activity with benzoate
-
?
ATP + 4-aminobenzoate + CoA
AMP + diphosphate + 4-aminobenzoyl-CoA
-
19% of the activity with benzoate
-
?
ATP + 4-chlorobenzoate + CoA
AMP + diphosphate + 4-chlorobenzoyl-CoA
-
96% of the activity with benzoate
-
?
ATP + 4-methoxybenzoate + CoA
AMP + diphosphate + 4-methoxybenzoyl-CoA
-
43% of the activity with benzoate
-
?
ATP + 4-nitrobenzoate + CoA
AMP + diphosphate + 4-nitrobenzoyl-CoA
-
29% of the activity with benzoate
-
?
ATP + indomethacin + CoA
AMP + diphosphate + ?
-
less than 5% of the activity with hexanoic acid
-
?
ATP + m-methoxybenzoate + CoA
AMP + diphosphate + m-methoxybenzoyl-CoA
-
-
-
-
?
ATP + p-methoxybenzoate + CoA
AMP + diphosphate + p-methoxybenzoyl-CoA
-
-
-
-
?
ATP + tranexamic acid + CoA
AMP + diphosphate + tranexoyl-CoA
-
less than 10% of the activity with hexanoic acid
-
?
ATP + valproate + CoA
ADP + diphosphate + valproyl-CoA
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less active on valproate
-
-
?
ATP + valproic acid + CoA
AMP + diphosphate + valproyl-CoA
-
less than 10% of the activity with hexanoic acid
-
?
ATP + 1-naphthoic acid + CoA
AMP + diphosphate + 1-naphthoyl-CoA
-
less than 10% of the activity with hexanoic acid
-
?
ATP + 3-methylbenzoate + CoA
AMP + diphosphate + 3-methylbenzoyl-CoA
-
138% of the activity with benzoate
-
?
ATP + 4-methylbenzoate + CoA
AMP + diphosphate + 4-methylbenzoyl-CoA
-
114% of the activity with benzoate
-
?
ATP + benzoate + CoA
AMP + diphosphate + benzoyl-CoA
-
about 30% of the activity with hexanoic acid
-
?
ATP + benzoate + CoA
AMP + diphosphate + benzoyl-CoA
-
high activities are obtained with benzoate having methyl, pentyl, and methoxy groups in the para- or meta-positions of the benzene ring
-
-
?
ATP + hexanoate + CoA
AMP + diphosphate + hexanoyl-CoA
-
15% of the activity with octanoate
-
?
ATP + hexanoate + CoA
AMP + diphosphate + hexanoyl-CoA
-
maximal activity on hexanoate
-
-
?
ATP + octanoate + CoA
AMP + diphosphate + octanoyl-CoA
-
about 50% of the activity with hexanoic acid
-
?
additional information
?
-
-
the enzyme catalyzes the first reaction of glycine conjugation
-
?
additional information
?
-
-
the enzyme is responsible for glycine conjugation
-
?
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
additional information
?
-
-
the enzyme catalyzes the first reaction of glycine conjugation
-
?
additional information
?
-
-
the enzyme is responsible for glycine conjugation
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.023
-
cell extract, with 0.001 mM hexanoic acid as a substrate in 0.2 M Tris-HCl buffer (pH 8.5)
4.14
-
after 180fold purification, with 0.001 mM hexanoic acid as a substrate in 0.2 M Tris-HCl buffer (pH 8.5)
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ACSM4_MOUSE
580
0
65427
Swiss-Prot
Mitochondrion (Reliability: 2)
ACSM5_MOUSE
578
0
64328
Swiss-Prot
Mitochondrion (Reliability: 2)
ACSL3_MOUSE
720
1
80492
Swiss-Prot
Secretory Pathway (Reliability: 3)
ACSM1_MOUSE
573
0
64760
Swiss-Prot
Mitochondrion (Reliability: 2)
ACSM2_MOUSE
575
0
64269
Swiss-Prot
other Location (Reliability: 5)
ACSM3_MOUSE
580
0
65623
Swiss-Prot
Mitochondrion (Reliability: 2)
ACSF2_MOUSE
615
0
67951
Swiss-Prot
Mitochondrion (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Sephadex G-25 gel filtration, DEAE-Sepharose column chromatography, and hydroxylapatite column chromatography
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kasuya, F.; Hiasa, M.; Kawai, Y.; Igarashi, K.; Fukui, M.
Inhibitory effect of quinolone antimicrobial and nonsteroidal anti-inflammatory drugs on a medium chain acyl-CoA synthetase
Biochem. Pharmacol.
62
363-367
2001
Mus musculus
Kasuya, F.; Igarashi, K.; Fukui, M.
Characterization of a renal medium chain acyl-CoA synthetase responsible for glycine conjugation in mouse kidney mitochondria
Chem. Biol. Interact.
118
233-246
1999
Mus musculus
Kasuya, F.; Tatsuki, T.; Ohta, M.; Kawai, Y.; Igarashi, K.
Purification, characterization, and mass spectrometric sequencing of a medium chain acyl-CoA synthetase from mouse liver mitochondria and comparisons with the homologs of rat and bovine
Protein Expr. Purif.
47
405-414
2006
Bos taurus, Mus musculus
EXTERNAL LINKS (specific for EC-Number 6.2.1.2)
Transporter Classification Database (TCDB): 4.C.1.1.3
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Release 2023.1 (January 2023)
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