Long-chain-fatty-acid-luciferin-component_ligase

Long-chain-fatty-acid—luciferin-component ligase

Long-chain-fatty-acid—luciferin-component ligase

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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
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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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