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Information on EC 6.2.1.2 - medium-chain acyl-CoA ligase

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EC Tree
     6 Ligases
         6.2 Forming carbon-sulfur bonds
             6.2.1 Acid-thiol ligases
                6.2.1.2 medium-chain acyl-CoA ligase
IUBMB 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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This record set is specific for:
UNIPROT: Q8TLW1
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
elongase, macs2, mig protein, medium chain acyl-coa synthetase, butyryl-coa synthetase, xenobiotic/medium-chain fatty acid:coa ligase, xm-ligase, short-chain acyl-coa synthetase, medium chain acyl-coenzyme a synthetase, butyryl-coenzyme a synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medium-chain acyl coenzyme A synthetase
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Acyl-activating enzyme
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butanoate:CoA ligase (AMP-forming)
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-
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butyrate-CoA ligase
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-
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Butyryl-CoA synthetase
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-
-
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Butyryl-coenzyme A synthetase
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-
-
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Fatty acid thiokinase (medium chain)
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-
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L-(+)-3-Hydroxybutyryl CoA ligase
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Medium chain acyl-coenzyme A synthetase
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-
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Short-chain acyl-CoA synthetase
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Synthetase, butyryl conzyme A
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acid-thiol ligation
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PATHWAY SOURCE
PATHWAYS
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-, -, -, -, -, -, -, -, -, -
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 hide
9080-51-7
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 2-methylbutyrate + CoA
AMP + diphosphate + 2-methylbutyryl-CoA
show the reaction diagram
when propionate or other less favorable acyl substrates, such as butyrate, 2-methylpropionate, or 2-methylvalerate, are utilized, the acyl-CoA is not produced or is produced at reduced levels. Instead, acyl-AMP and diphosphate are released in the absence of CoA, whereas in the presence of CoA, the intermediate is broken down into AMP and the acyl substrate, which are released along with diphosphate. These results suggest that although acyl-CoA synthetases may have the ability to utilize a broad range of substrates for the acyl-adenylate-forming first step of the reaction, the intermediate may not be suitable for the thioester-forming second step
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?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.92
2-methylbutyrate
pH 7.5, 55°C
4.21
ATP
pH 7.5, 55°C
4.09
CoA
pH 7.5, 55°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.58
2-methylbutyrate
pH 7.5, 55°C
1.94
ATP
pH 7.5, 55°C
2.15
CoA
pH 7.5, 55°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.18
2-methylbutyrate
pH 7.5, 55°C
0.46
ATP
pH 7.5, 55°C
0.53
CoA
pH 7.5, 55°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q8TLW1_METAC
Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
560
0
63751
TrEMBL
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
heterologous production in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Meng, Y.; Ingram-Smith, C.; Cooper, L.L.; Smith, K.S.
Characterization of an archaeal medium-chain acyl coenzyme A synthetase from Methanosarcina acetivorans
J. Bacteriol.
192
5982-5990
2010
Methanosarcina acetivorans (Q8TLW1), Methanosarcina acetivorans, Methanosarcina acetivorans DSM 2834 (Q8TLW1)
Manually annotated by BRENDA team