PMID:6833298

Citation	Rodriguez, A, Riendeau, D and Meighen, E (1983) Purification of the acyl coenzyme A reductase component from a complex responsible for the reduction of fatty acids in bioluminescent bacteria. Properties and acyltransferase activity. J. Biol. Chem. 258:5233-7
Abstract	The acyl-CoA reductase component of the fatty acid reductase complex responsible for synthesis of long chain aldehydes for the bioluminescent reaction in bacteria has been purified to homogeneity. The enzyme copurified as part of the complex through the initial steps and was then resolved and further purified to give a single band on sodium dodecyl sulfate-gel electrophoresis of molecular weight 58,000. The molecular weight of the native enzyme was 2 x 10(5), indicating it was an oligomeric enzyme containing identical subunits. The acyl-CoA reductase had a high specificity for NADPH with a Km value of 5 microM at optimal concentrations of tetradecanoyl-CoA (5-10 microM). The purified enzyme was discovered to have a high, intrinsic acyltransferase activity forming thioesters with a number of different thiol compounds (mercaptoethanol, dithiothreitol, 2-mercaptoethyl ether). The rates of the acyltransferase and acyl-CoA reductase reactions were similar to the rate of turnover of the fatty acid reductase complex suggesting that fatty acid reduction and not activation controls the rate of conversion of fatty acids to aldehydes.
Links	PubMed
Keywords	Aldehyde Oxidoreductases/isolation & purification; Aldehyde Oxidoreductases/metabolism; Bacteria/enzymology; Chromatography, Thin Layer; Electrophoresis, Polyacrylamide Gel; Fatty Acids/metabolism; Luminescent Measurements
edit table

Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
PHOPO:LUXC		GO:0050062: long-chain-fatty-acyl-CoA reductase activity	ECO:0000314:		F		Figure 2C - Thin layer chromatography. Shows that when the protein of interest is incubated with radiolabeled tetradecanoyl-CoA (an intermediate in fatty acid metabolism) and NADPH, an aldehyde product is produced and low amounts of free fatty acids are detected. This indicates that the Acyl-CoA reductase reduces the tetradecanoyl-CoA intermediate to the aldehyde substrate.	complete CACAO 9579
PHOPO:LUXC	enables	GO:0050062: long-chain-fatty-acyl-CoA reductase activity	ECO:0000314: direct assay evidence used in manual assertion		F		Seeded From UniProt	complete

References

See Help:References for how to manage references in GONUTS.