Enzyme

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     6. Ligases
        6.2 Forming carbon-sulfur bonds
            6.2.1 Acid-thiol ligases
ID:6.2.1.3
Description:Long-chain-fatty-acid--CoA ligase.
Alternative Name: Lignoceroyl-CoA synthase.
Fatty acid thiokinase (long chain).
Acyl-CoA synthetase.
Acyl-activating enzyme.
Prosite: PDOC00427;
PDB:
PDBScop
Cath: 3.30.300.30; 3.30.300.310; 3.40.50.12780;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 6.2.1.3
BRENDA Enzyme Link: BRENDA 6.2.1.3
KEGG Enzyme Link: KEGG6.2.1.3
BioCyc Enzyme Link: BioCyc 6.2.1.3
ExPASy Enzyme Link: ExPASy6.2.1.3
EC2PDB Enzyme Link: EC2PDB 6.2.1.3
ExplorEnz Enzyme Link: ExplorEnz 6.2.1.3
PRIAM enzyme-specific profiles Link: PRIAM 6.2.1.3
IntEnz Enzyme Link: IntEnz 6.2.1.3
MEDLINE Enzyme Link: MEDLINE 6.2.1.3
MSA:

6.2.1.3;

Phylogenetic Tree:

6.2.1.3;

Uniprot:
M-CSA:
RHEA:15421 a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-CoA + AMP + diphosphate
RULE(radius=1) [*:1]-[C;H0;+0:2](=[*:3])-[OH;+0:4].[*:5]-[P;H0;+0:6](=[*:7])(-[*:8])-[O;H0;+0:9]-[*:10].[*:11]-[SH;+0:12]>>[*:10]-[OH;+0:9].[*:5]-[P;H0;+0:6](=[*:7])(-[*:8])-[OH;+0:4].[*:11]-[S;H0;+0:12]-[C;H0;+0:2](-[*:1])=[*:3]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Purification and properties of long-chain acyl-coenzyme-A synthetase from rat liver.Tanaka T, Hosaka K, Hoshimaru M, Numa S1979 Jul467438
Lignoceroyl-coenzyme A synthetase from developing rat brain: partial purification, characterization and comparison with palmitoyl-coenzyme A synthetase activity and liver enzyme.Nagamatsu K, Soeda S, Mori M, Kishimoto Y1985 Aug 223161545
Identical subcellular distribution of palmitoyl-CoA and arachidonoyl-CoA synthetase activities in human blood platelets.Bakken AM, Farstad M1989 Jul 12528345
Acyl-coenzyme-A synthetase I from Candida lipolytica. Purification, properties and immunochemical studies.Hosaka K, Mishina M, Tanaka T, Kamiryo T, Numa S1979 Jan 2108099