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J. Lipid Res.
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Originally published In Press as doi:10.1194/jlr.M700378-JLR200 on August 30, 2007

Papers In Press, published online ahead of print December 1, 2007
J. Lipid Res., doi:10.1194/jlr.M700378-JLR200
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Journal of Lipid Research, Vol. 48, 2736-2750, December 2007
Copyright © 2007 by American Society for Biochemistry and Molecular Biology

Evidence for 26 distinct acyl-coenzyme A synthetase genes in the human genomeboxs

Paul A. Watkins1,*,{dagger}, Dony Maiguel*,{dagger}, Zhenzhen Jia* and Jonathan Pevsner*,§

* Kennedy Krieger Institute, Johns Hopkins University School of Medicine, Baltimore, MD 21205
{dagger} Department of Neurology, Johns Hopkins University School of Medicine, Baltimore, MD 21205
§ Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD 21205

boxs The online version of this article (available at http://www.jlr.org) contains supplementary data in the form of 3 Tables.

Published, JLR Papers in Press, August 30, 2007.

2 In our previous publications, motifs were designated by Arabic numerals (Motifs 1 and 2) (11, 61, 62). Because this work has led to the refinement of consensus sequences, motifs are now designated by Roman numerals.

1 To whom correspondence should be addressed. e-mail: watkins{at}kennedykrieger.org

Acyl-coenzyme A synthetases (ACSs) catalyze the fundamental, initial reaction in fatty acid metabolism. "Activation" of fatty acids by thioesterification to CoA allows their participation in both anabolic and catabolic pathways. The availability of the sequenced human genome has facilitated the investigation of the number of ACS genes present. Using two conserved amino acid sequence motifs to probe human DNA databases, 26 ACS family genes/proteins were identified. ACS activity in either humans or rodents was demonstrated previously for 20 proteins, but 6 remain candidate ACSs. For two candidates, cDNA was cloned, protein was expressed in COS-1 cells, and ACS activity was detected. Amino acid sequence similarities were used to assign enzymes into subfamilies, and subfamily assignments were consistent with acyl chain length preference. Four of the 26 proteins did not fit into a subfamily, and bootstrap analysis of phylograms was consistent with evolutionary divergence. Three additional conserved amino acid sequence motifs were identified that likely have functional or structural roles. The existence of many ACSs suggests that each plays a unique role, directing the acyl-CoA product to a specific metabolic fate. Knowing the full complement of ACS genes in the human genome will facilitate future studies to characterize their specific biological functions.

Supplementary key words fatty acid activation • fatty acid metabolism • conserved motifs • bioinformatics • consensus sequence • phylogenetic analysis • structure-function

Abbreviations: ACS, acyl-coenzyme A synthetase; ACSAc, yeast or bacterial acetyl-coenzyme A synthetase; ACSBG, bubblegum ACS; ACSF, ACS family; ACSL, long-chain ACS; ACSM, medium-chain ACS; ACSS, short-chain ACS; ACSVL, very long-chain ACS; BLAST, Basic Local Alignment Search Tool; EST, expressed sequence tag; FATP, fatty acid transport protein; HUGO, Human Genome Organization; LCFA, long-chain fatty acid; NCBI, National Center for Biotechnology Information; ttACS, Thermus thermophilus ACS; VLCFA, very long-chain fatty acid


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