Mutagenesis of rat acyl-CoA synthetase 4 indicates amino acids that contribute to fatty acid binding

Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids

Volumn 1771, Issue 1, 2007, Pages 119-125

  Stinnett, Lori ^a   Lewin, Tal M ^a   Coleman, Rosalind A ^a  

^a The University of North Carolina at Chapel Hill   (United States)

Author keywords

Acyl CoA synthetase; Arachidonic acid; Fatty acid binding; Kinetics; Mutagenesis; Polyunsaturated fatty acid

Indexed keywords

ADENOSINE TRIPHOSPHATE; AMINO ACID; FATTY ACID; LONG CHAIN FATTY ACID COENZYME A LIGASE;

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; BINDING AFFINITY; ENZYME ACTIVITY; ESCHERICHIA COLI; HYDROPHOBICITY; MUTAGENESIS; MUTATION; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN BINDING; RAT; THERMUS THERMOPHILUS;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; BINDING SITES; COENZYME A LIGASES; ENZYME ACTIVATION; ESCHERICHIA COLI; FATTY ACIDS, UNSATURATED; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MUTATION, MISSENSE; PROTEIN BINDING; RATS; SEQUENCE ALIGNMENT; THERMUS THERMOPHILUS;

ESCHERICHIA COLI; MAMMALIA; RATTUS; THERMUS THERMOPHILUS;

EID: 33846057897     PISSN: 13881981     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbalip.2006.09.016     Document Type: Article

References (17)

1. Coleman R.A., Lewin T.M., Van Horn C.G., and Gonzalez-Baró M.R. Do acyl-CoA synthetases regulate fatty acid entry into synthetic versus degradative pathways?. J. Nutr. 132 (2002) 2123-2126
2. Coleman R.A., Van Horn C.G., Gonzalez-Baró M.R., and Lewin T.M. In: Haldar D., and Das S.K. (Eds). Lipids: Glycerolipid Metabolizing Enzymes, Research Signpost, Trivandrum (2002) 1-15
3. Corkey B.E., Deeney J.T., Yaney G.C., Tornheim K., and Prentki M. The role of long-chain fatty acyl-CoA esters in beta-cell signal transduction. J. Nutr. 130 (2000) 299S-304S
4. Hertz R., Magenheim J., Berman I., and Bar-Tana J. Fatty acyl-CoA thioesters are ligands of hepatic nuclear factor-4alpha. Nature 392 (1998) 512-516
5. Hertz R., Kalderon B., Byk T., Berman I., Za'tara G., Mayer R., and Bar-Tana J. Thioesterase activity and acyl-CoA/fatty acid cross-talk of hepatocyte nuclear factor-4a. J. Biol. Chem. 280 (2005) 24451-24461
6. Steinberg S.J., Morgenthaler J., Heinzer A.K., Smith K.D., and Watkins P.A. Very long-chain acyl-CoA synthetases: human "bubblegum" represents a new family of proteins capable of activating very long-chain fatty acids. J. Biol. Chem. 275 (2000) 35162-35169
7. Mashek D.G., Bornfeldt K.E., Coleman R.A., Berger J., Bernlohr D.A., Black P., DiRusso C.C., Farber S.A., Guo W., Hashimoto N., Khodiyar V.K., Kuypers F.A., Maltais L.J., Nebert D.W., Renieri A., Schaffer J.E., Stahl A., Watkins P.A., Vasiliou V., and Yamamoto T.T. Revised nomenclature for the mammalian long chain acyl-CoA synthetase gene family. J. Lipid Res. 45 (2004) 1958-1961
8. Lewin T.M., Van Horn C.G., Krisans S.K., and Coleman R.A. Rat liver acyl-CoA synthetase 4 is a peripheral-membrane protein located in two distinct subcellular organelles, peroxisomes and mitochondrial associated membrane. Arch. Biochem. Biophys. 404 (2002) 263-270
9. Kang M.-J., Fujino T., Sasano H., Minekura H., Yabuki N., Nagura H., Iijima H., and Yamamoto T.T. A novel arachidonate-preferring acyl-CoA synthetase is present in steroidogenic cells of the rat adrenal, ovary, and testis. Proc. Natl. Acad. Sci. 94 (1997) 2880-2884
10. Longo I., Frints S.G., Fryns J.P., Meloni I., Pescucci C., Ariani F., Borghgraef M., Raynaud M., Marynen P., Schwartz C., Renieri A., and Froyen G. A third MRX family (MRX68) is the result of mutation in the long chain fatty acid-CoA ligase 4 (FACL4) gene: proposal of a rapid enzymatic assay for screening mentally retarded patients. J. Med. Genet. 40 (2003) 11-17
11. Meloni I., Muscettola M., Raynaud M., Longo I., Bruttini M., Moizard M.P., Gomot M., Chelly J., des Portes V., Fryns J.P., Ropers H.H., Magi B., Bellan C., Volpi N., Yntema H.G., Lewis S.E., Schaffer J.E., and Renieri A. FACL4, encoding fatty acid-CoA ligase 4, is mutated in nonspecific X-linked mental retardation. Nat. Genet. 30 (2002) 436-440
12. Van Horn C.G., Caviglia J.M., Li L.O., Wang S., Granger D.A., and Coleman R.A. Characterization of recombinant long-chain rat acyl-CoA synthetase isoforms 3 and 6: identification of a novel variant of isoform 6. Biochemistry 44 (2005) 1635-1642
13. Hisanaga Y., Ago H., Nakagawa N., Hamada K., Ida K., Yamamoto M., Hori T., Arii Y., Sugahara M., Kuramitsu S., Yokoyama S., and Miyano M. Structural basis of the substrate-specific two-step catalysis of long chain fatty acyl-CoA synthetase dimer. J. Biol. Chem. 279 (2004) 31717-31726
14. Black P.N., Zhang Q., Weimar J.D., and DiRusso C.C. Mutational analysis of a fatty acyl-coenzyme A synthetase signature motif identifies seven amino acid residues that modulate fatty acid substrate specificity. J. Biol. Chem. 272 (1997) 4896-4903
15. Kim J.-H., Lewin T.M., and Coleman R.A. Expression and characterization of recombinant rat acyl-CoA synthetases 1, 4, and 5: selective inhibition by triacsin C and thiazolidinediones. J. Biol. Chem. 276 (2001) 24667-24673
16. Segel I.H. Enzyme kinetics. Behavior and analysis of rapid equilibrium and steady-state enzyme systems (1975), John Wiley & Sons, Inc., New York
17. Notredame C., Higgins D., and Heringa J. T-Coffee: a novel method for multiple sequence alignments. J. Mol. Biol. 302 (2000) 205-217