| Long-chain-fatty-acid—luciferin-component ligase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 6.2.1.19 | ||||||||
| CAS no. | 82657-98-5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a long-chain-fatty-acid—luciferin-component ligase (EC 6.2.1.19) is an enzyme that catalyzes the chemical reaction
- ATP + an acid + protein AMP + diphosphate + an acyl-protein thioester
The 3 substrates of this enzyme are ATP, acid, and protein, whereas its 3 products are AMP, diphosphate, and acyl-protein thioester.
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is long-chain-fatty-acid:protein ligase (AMP-forming). This enzyme is also called acyl-protein synthetase.
References
- Riendeau D, Rodriguez A, Meighen E (1982). "Resolution of the fatty acid reductase from Photobacterium phosphoreum into acyl protein synthetase and acyl-CoA reductase activities. Evidence for an enzyme complex". J. Biol. Chem. 257 (12): 6908–15. doi:10.1016/S0021-9258(18)34515-0. PMID 7085612.
- Wall L; Meighen EA (1986). "Subunit structure of the fatty-acid reductase complex from Photobacterium phosphoreum". Biochemistry. 25 (15): 4315–4321. doi:10.1021/bi00363a021.
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