HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Byers, D. Articles by Meighen, E. Search for Related Content PubMed PubMed Citation Articles by Byers, D. Articles by Meighen, E. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 259, Issue 11, 7109-7114, 06, 1984

Vibrio harveyi aldehyde dehydrogenase. Partial reversal of aldehyde oxidation and its possible role in the reduction of fatty acids for the bioluminescence reaction

D Byers and E Meighen

Vibrio harveyi aldehyde dehydrogenase, which catalyzes the oxidation of long chain aliphatic aldehydes to acids, has been discovered to have both acyl-CoA reductase and thioesterase activities. Tetradecanoyl-CoA was reduced to tetradecanal in the presence of NAD(P)H, as monitored by the stimulation of luciferase activity by the aldehyde product (acyl- CoA reductase). In the absence of NADPH, [3H]tetradecanoyl-CoA was hydrolyzed to the hexane-soluble fatty acid (thioesterase). Inhibition data with N-ethylmaleimide suggest that a single active site on aldehyde dehydrogenase is responsible for all three enzymatic activities. The acyl-CoA reductase activity was maximal at low NADPH concentration (about 1 microM), whereas much higher concentrations of NADH (greater than 100-fold) were required for optimal activity. Further increases in NADPH or NADH concentrations inhibited both the acyl-CoA reductase and thioesterase reactions. On the basis of the specificity of aldehyde dehydrogenase for NADP(H), an improved purification procedure employing affinity chromatography on 2', 5'-ADP- Sepharose is described. Although fatty acid reductase activity could not be reconstituted, aldehyde dehydrogenase specifically stimulated the rate of acylation of the acyl protein synthetase component from the Photobacterium phosphoreum fatty acid reductase system. This observation, combined with the partial reversal of aldehyde oxidation described above, suggests a possible role for aldehyde dehydrogenase in aldehyde biosynthesis for the luminescent reaction in V. harveyi.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				E. J. Nelson, H. S. Tunsjo, P. M. Fidopiastis, H. Sorum, and E. G. Ruby A Novel lux Operon in the Cryptically Bioluminescent Fish Pathogen Vibrio salmonicida Is Associated with Virulence Appl. Envir. Microbiol., March 15, 2007; 73(6): 1825 - 1833. [Abstract] [Full Text] [PDF]