Generation of fatty acids by an acyl esterase in the bioluminescent system of Photobacterium phosphoreum
The fatty acid reductase complex from Photobacterium phosphoreum has been discovered to have a long chain ester hydrolase activity associated with the 34K protein component of the complex. This protein has been resolved from the other components (50K and 58K) of the fatty acid reductase complex with a purity of > 95% and found to catalyze the transfer of acyl groups from acyl-CoA primarily to thiol acceptors with a low level of transfer to glycerol and water. Addition of the 50K protein of the complex caused a dramatic change in specificity increasing the transfer to oxygen acceptors. The acyl-CoA hydrolase activity increased almost 10-fold, and hence free fatty acids can be generated by the 34K protein when it is present in the fatty acid reductase complex. Hydrolysis of acyl-S-mercaptoethanol and acyl-1-glycerol and the ATP-dependent reduction of the released fatty acids to aldehyde for the luminescent reaction were also demonstrated for the reconstituted fatty acid reductase complex, raising the possibility that the immediate source of fatty acids for this reaction in vivo could be the membrane lipids and/or the fatty acid synthetase system.
- Research Organization:
- McGill Univ., Montreal, Quebec
- OSTI ID:
- 5332029
- Journal Information:
- J. Biol. Chem.; (United States), Vol. 259:16
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
BACTERIA
ENZYME ACTIVITY
CARBOXYLIC ACIDS
BIOSYNTHESIS
ESTERASES
BIOCHEMISTRY
BIOLUMINESCENCE
CELL MEMBRANES
ELECTROPHORESIS
EXTREME ULTRAVIOLET RADIATION
PHOTOCHEMISTRY
CELL CONSTITUENTS
CHEMISTRY
ELECTROMAGNETIC RADIATION
ENZYMES
HYDROLASES
LUMINESCENCE
MEMBRANES
MICROORGANISMS
ORGANIC ACIDS
ORGANIC COMPOUNDS
RADIATIONS
SYNTHESIS
ULTRAVIOLET RADIATION
550201* - Biochemistry- Tracer Techniques