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Information on EC 6.2.1.2 - medium-chain acyl-CoA ligase and Organism(s) Dictyostelium discoideum and UniProt Accession Q54CJ4

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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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Dictyostelium discoideum
UNIPROT: Q54CJ4
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Word Map
The taxonomic range for the selected organisms is: Dictyostelium discoideum
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl-activating enzyme
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-
-
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butanoate:CoA ligase (AMP-forming)
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-
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butyrate-CoA ligase
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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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-
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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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-
-
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Synthetase, butyryl conzyme A
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-
-
-
additional information
the Dictyostelium genome possesses members of both the ELO and KCS fatty acid elongase families
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acid-thiol ligation
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-
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-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -, -, -
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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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
total lipid composition, profiling of the total fatty acid
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
axenic strain, AX3, gene eloA
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ELOA_DICDI
271
6
32176
Swiss-Prot
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene eloA, phylogenetic analysis, expression of the putative Dictyostelium discoideum eloA cDNA in Saccharomces cerevisiae
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Blacklock, B.J.; Kelley, D.; Patel, S.
A fatty acid elongase ELO with novel activity from Dictyostelium discoideum
Biochem. Biophys. Res. Commun.
374
226-230
2008
Dictyostelium discoideum (Q54CJ4)
Manually annotated by BRENDA team