메뉴 건너뛰기




Volumn 1771, Issue 9, 2007, Pages 1246-1253

Mechanistic studies of the long chain acyl-CoA synthetase Faa1p from Saccharomyces cerevisiae

Author keywords

Fatty acid transport; Long chain acyl CoA synthetase; Mechanistic enzymology

Indexed keywords

ADENOSINE TRIPHOSPHATE; COENZYME A; HISTIDINE; LONG CHAIN FATTY ACID COENZYME A LIGASE; MALTOSE; PROTEIN FAA1P; UNCLASSIFIED DRUG;

EID: 34548602373     PISSN: 13881981     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbalip.2007.05.009     Document Type: Article
Times cited : (19)

References (30)
  • 1
    • 33644616729 scopus 로고    scopus 로고
    • Fatty acid transport by vectorial acylation in mammals: roles played by different isoforms of rat long-chain acyl-CoA synthetases
    • Tong F., Black P.N., Coleman R.A., and DiRusso C.C. Fatty acid transport by vectorial acylation in mammals: roles played by different isoforms of rat long-chain acyl-CoA synthetases. Arch. Biochem. Biophys. 447 (2006) 46-52
    • (2006) Arch. Biochem. Biophys. , vol.447 , pp. 46-52
    • Tong, F.1    Black, P.N.2    Coleman, R.A.3    DiRusso, C.C.4
  • 2
    • 33644861799 scopus 로고    scopus 로고
    • Rat long chain acyl-CoA synthetase 5 increases fatty acid uptake and partitioning to cellular triacylglycerol in McArdle-RH7777 cells
    • Mashek D.G., McKenzie M.A., Van Horn C.G., and Coleman R.A. Rat long chain acyl-CoA synthetase 5 increases fatty acid uptake and partitioning to cellular triacylglycerol in McArdle-RH7777 cells. J. Biol. Chem. 281 (2006) 945-950
    • (2006) J. Biol. Chem. , vol.281 , pp. 945-950
    • Mashek, D.G.1    McKenzie, M.A.2    Van Horn, C.G.3    Coleman, R.A.4
  • 3
    • 0035813196 scopus 로고    scopus 로고
    • The Acyl-CoA synthetases encoded within FAA1 and FAA4 in Saccharomyces cerevisiae function as components of the fatty acid transport system linking import, activation, and intracellular Utilization
    • Faergeman N.J., Black P.N., Zhao X.D., Knudsen J., and DiRusso C.C. The Acyl-CoA synthetases encoded within FAA1 and FAA4 in Saccharomyces cerevisiae function as components of the fatty acid transport system linking import, activation, and intracellular Utilization. J. Biol. Chem. 276 (2001) 37051-37059
    • (2001) J. Biol. Chem. , vol.276 , pp. 37051-37059
    • Faergeman, N.J.1    Black, P.N.2    Zhao, X.D.3    Knudsen, J.4    DiRusso, C.C.5
  • 4
    • 0030897513 scopus 로고    scopus 로고
    • Role of long-chain fatty acyl-CoA esters in the regulation of metabolism and in cell signalling
    • Faergeman N.J., and Knudsen J. Role of long-chain fatty acyl-CoA esters in the regulation of metabolism and in cell signalling. Biochem. J. 323 (1997) 1-12
    • (1997) Biochem. J. , vol.323 , pp. 1-12
    • Faergeman, N.J.1    Knudsen, J.2
  • 6
    • 0027984281 scopus 로고
    • Saccharomyces cerevisiae contains four fatty acid activation (FAA) genes: an assessment of their role in regulating protein N-myristoylation and cellular lipid metabolism
    • Johnson D.R., Knoll L.J., Levin D.E., and Gordon J.I. Saccharomyces cerevisiae contains four fatty acid activation (FAA) genes: an assessment of their role in regulating protein N-myristoylation and cellular lipid metabolism. J. Cell Biol. 127 (1994) 751-762
    • (1994) J. Cell Biol. , vol.127 , pp. 751-762
    • Johnson, D.R.1    Knoll, L.J.2    Levin, D.E.3    Gordon, J.I.4
  • 7
    • 0028206276 scopus 로고
    • Biochemical studies of three Saccharomyces cerevisiae acyl-CoA synthetases, Faa1p, Faa2p, and Faa3p
    • Knoll L.J., Johnson D.R., and Gordon J.I. Biochemical studies of three Saccharomyces cerevisiae acyl-CoA synthetases, Faa1p, Faa2p, and Faa3p. J. Biol. Chem. 269 (1994) 16348-16356
    • (1994) J. Biol. Chem. , vol.269 , pp. 16348-16356
    • Knoll, L.J.1    Johnson, D.R.2    Gordon, J.I.3
  • 8
    • 0033579432 scopus 로고    scopus 로고
    • The fatty acid transport protein (FATP1) is a very long chain acyl-CoA synthetase
    • Coe N.R., Smith A.J., Frohnert B.I., Watkins P.A., and Bernlohr D.A. The fatty acid transport protein (FATP1) is a very long chain acyl-CoA synthetase. J. Biol. Chem. 274 (1999) 36300-36304
    • (1999) J. Biol. Chem. , vol.274 , pp. 36300-36304
    • Coe, N.R.1    Smith, A.J.2    Frohnert, B.I.3    Watkins, P.A.4    Bernlohr, D.A.5
  • 9
    • 0030746946 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae acetyl-coenzyme A synthetase encoded by the ACS1 gene, but not the ACS2-encoded enzyme, is subject to glucose catabolite inactivation
    • de Jong-Gubbels P., van den Berg M.A., Steensma H.Y., van Dijken J.P., and Pronk J.T. The Saccharomyces cerevisiae acetyl-coenzyme A synthetase encoded by the ACS1 gene, but not the ACS2-encoded enzyme, is subject to glucose catabolite inactivation. FEMS Microbiol. Lett. 153 (1997) 75-81
    • (1997) FEMS Microbiol. Lett. , vol.153 , pp. 75-81
    • de Jong-Gubbels, P.1    van den Berg, M.A.2    Steensma, H.Y.3    van Dijken, J.P.4    Pronk, J.T.5
  • 10
    • 1042276711 scopus 로고    scopus 로고
    • Crystal structure of yeast acetyl-coenzyme A synthetase in complex with AMP
    • Jogl G., and Tong L. Crystal structure of yeast acetyl-coenzyme A synthetase in complex with AMP. Biochemistry 43 (2004) 1425-1431
    • (2004) Biochemistry , vol.43 , pp. 1425-1431
    • Jogl, G.1    Tong, L.2
  • 11
    • 0030889638 scopus 로고    scopus 로고
    • Disruption of the Saccharomyces cerevisiae homologue to the murine fatty acid transport protein impairs uptake and growth on long-chain fatty acids
    • Faergeman N.J., DiRusso C.C., Elberger A., Knudsen J., and Black P.N. Disruption of the Saccharomyces cerevisiae homologue to the murine fatty acid transport protein impairs uptake and growth on long-chain fatty acids. J. Biol. Chem. 272 (1997) 8531-8538
    • (1997) J. Biol. Chem. , vol.272 , pp. 8531-8538
    • Faergeman, N.J.1    DiRusso, C.C.2    Elberger, A.3    Knudsen, J.4    Black, P.N.5
  • 12
    • 0026609190 scopus 로고
    • Isolation of a Saccharomyces cerevisiae long chain fatty acyl:CoA synthetase gene (FAA1) and assessment of its role in protein N-myristoylation
    • Duronio R.J., Knoll L.J., and Gordon J.I. Isolation of a Saccharomyces cerevisiae long chain fatty acyl:CoA synthetase gene (FAA1) and assessment of its role in protein N-myristoylation. J. Cell Biol. 117 (1992) 515-529
    • (1992) J. Cell Biol. , vol.117 , pp. 515-529
    • Duronio, R.J.1    Knoll, L.J.2    Gordon, J.I.3
  • 13
    • 0037507257 scopus 로고    scopus 로고
    • Vectorial acylation in Saccharomyces cerevisiae. Fat1p and fatty acyl-CoA synthetase are interacting components of a fatty acid import complex
    • Zou Z., Tong F., Faergeman N.J., Borsting C., Black P.N., and DiRusso C.C. Vectorial acylation in Saccharomyces cerevisiae. Fat1p and fatty acyl-CoA synthetase are interacting components of a fatty acid import complex. J. Biol. Chem. 278 (2003) 16414-16422
    • (2003) J. Biol. Chem. , vol.278 , pp. 16414-16422
    • Zou, Z.1    Tong, F.2    Faergeman, N.J.3    Borsting, C.4    Black, P.N.5    DiRusso, C.C.6
  • 14
    • 0032693609 scopus 로고    scopus 로고
    • Identification and characterization of major lipid particle proteins of the yeast Saccharomyces cerevisiae
    • Athenstaedt K., Zweytick D., Jandrositz A., Kohlwein S.D., and Daum G. Identification and characterization of major lipid particle proteins of the yeast Saccharomyces cerevisiae. J. Bacteriol. 181 (1999) 6441-6448
    • (1999) J. Bacteriol. , vol.181 , pp. 6441-6448
    • Athenstaedt, K.1    Zweytick, D.2    Jandrositz, A.3    Kohlwein, S.D.4    Daum, G.5
  • 16
    • 18944406929 scopus 로고    scopus 로고
    • The spatial organization of lipid synthesis in the yeast Saccharomyces cerevisiae derived from large scale green fluorescent protein tagging and high resolution microscopy
    • Natter K., Leitner P., Faschinger A., Wolinski H., McCraith S., Fields S., and Kohlwein S.D. The spatial organization of lipid synthesis in the yeast Saccharomyces cerevisiae derived from large scale green fluorescent protein tagging and high resolution microscopy. Mol. Cell Proteomics 4 (2005) 662-672
    • (2005) Mol. Cell Proteomics , vol.4 , pp. 662-672
    • Natter, K.1    Leitner, P.2    Faschinger, A.3    Wolinski, H.4    McCraith, S.5    Fields, S.6    Kohlwein, S.D.7
  • 17
    • 0015038005 scopus 로고
    • The purification and properties of microsomal palmitoyl-coenzyme A synthetase
    • Bar-Tana J., Rose G., and Shapiro B. The purification and properties of microsomal palmitoyl-coenzyme A synthetase. Biochem. J. 122 (1971) 353-362
    • (1971) Biochem. J. , vol.122 , pp. 353-362
    • Bar-Tana, J.1    Rose, G.2    Shapiro, B.3
  • 18
    • 0029093993 scopus 로고
    • Comparison of the reactivity of tetradecenoic acids, a triacsin, and unsaturated oximes with four purified Saccharomyces cerevisiae fatty acid activation proteins
    • Knoll L.J., Schall O.F., Suzuki I., Gokel G.W., and Gordon J.I. Comparison of the reactivity of tetradecenoic acids, a triacsin, and unsaturated oximes with four purified Saccharomyces cerevisiae fatty acid activation proteins. J. Biol. Chem. 270 (1995) 20090-20097
    • (1995) J. Biol. Chem. , vol.270 , pp. 20090-20097
    • Knoll, L.J.1    Schall, O.F.2    Suzuki, I.3    Gokel, G.W.4    Gordon, J.I.5
  • 19
    • 0016888730 scopus 로고
    • Fatty acid activation: specificity, localization, and function
    • Groot P.H., Scholte H.R., and Hulsmann W.C. Fatty acid activation: specificity, localization, and function. Adv. Lipid Res. 14 (1976) 75-126
    • (1976) Adv. Lipid Res. , vol.14 , pp. 75-126
    • Groot, P.H.1    Scholte, H.R.2    Hulsmann, W.C.3
  • 20
    • 0015580995 scopus 로고
    • Palmitoyl-coenzyme A synthetase. Mechanism of reaction
    • Bar-Tana J., Rose G., Brandes R., and Shapiro B. Palmitoyl-coenzyme A synthetase. Mechanism of reaction. Biochem. J. 131 (1973) 199-209
    • (1973) Biochem. J. , vol.131 , pp. 199-209
    • Bar-Tana, J.1    Rose, G.2    Brandes, R.3    Shapiro, B.4
  • 23
    • 0031040894 scopus 로고    scopus 로고
    • Mutational analysis of a fatty acyl-coenzyme A synthetase signature motif identifies seven amino acid residues that modulate fatty acid substrate specificity
    • 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
    • (1997) J. Biol. Chem. , vol.272 , pp. 4896-4903
    • Black, P.N.1    Zhang, Q.2    Weimar, J.D.3    DiRusso, C.C.4
  • 24
    • 0018721369 scopus 로고
    • Substrate inhibition methods
    • Cleland W.W. Substrate inhibition methods. Enzymol 63 (1979) 500-513
    • (1979) Enzymol , vol.63 , pp. 500-513
    • Cleland, W.W.1
  • 25
    • 34548641251 scopus 로고
    • The enzyme-substrate complex
    • Frieden E. The enzyme-substrate complex. Sci. Am. 201 (1959) 119-125
    • (1959) Sci. Am. , vol.201 , pp. 119-125
    • Frieden, E.1
  • 26
    • 50549155520 scopus 로고
    • The kinetics of enzyme-catalyzed reactions with two or more substrates or products: III. Prediction of initial velocity and inhibition patterns by inspection
    • Cleland W.W. The kinetics of enzyme-catalyzed reactions with two or more substrates or products: III. Prediction of initial velocity and inhibition patterns by inspection. Biochim. Biophys. Acta 67 (1963) 188-196
    • (1963) Biochim. Biophys. Acta , vol.67 , pp. 188-196
    • Cleland, W.W.1
  • 27
    • 0035663382 scopus 로고    scopus 로고
    • Evaluation of adenosine 5′-hexadecylphosphate as an inhibitor of acyl-CoA synthetase isozyme functional for phospholipid reconstitution in the yeast Saccharomyces cerevisiae
    • Nakayama K., and Tanaka T. Evaluation of adenosine 5′-hexadecylphosphate as an inhibitor of acyl-CoA synthetase isozyme functional for phospholipid reconstitution in the yeast Saccharomyces cerevisiae. J. Biosci. Bioeng. 92 (2001) 475-477
    • (2001) J. Biosci. Bioeng. , vol.92 , pp. 475-477
    • Nakayama, K.1    Tanaka, T.2
  • 28
    • 0036401543 scopus 로고    scopus 로고
    • Irreversible deacylation of plasma membrane phospholipids by the combined action of Mg2+ and a long-chain acyl-CoA synthetase inhibitor in Saccharomyces cerevisiae
    • Nakayama K., Nakamura T., Taniguchi M., and Tanaka T. Irreversible deacylation of plasma membrane phospholipids by the combined action of Mg2+ and a long-chain acyl-CoA synthetase inhibitor in Saccharomyces cerevisiae. J. Biosci. Bioeng. 94 (2002) 258-263
    • (2002) J. Biosci. Bioeng. , vol.94 , pp. 258-263
    • Nakayama, K.1    Nakamura, T.2    Taniguchi, M.3    Tanaka, T.4
  • 29
    • 0016420266 scopus 로고
    • Long-chain fatty acyl-CoA synthetase from rat liver microsomes. EC 6.2.1.3 fatty acyl-CoA ligase (ATP)
    • Bar-Tana J., and Shapiro B. Long-chain fatty acyl-CoA synthetase from rat liver microsomes. EC 6.2.1.3 fatty acyl-CoA ligase (ATP). Methods Enzymol. 35 (1975) 17-22
    • (1975) Methods Enzymol. , vol.35 , pp. 17-22
    • Bar-Tana, J.1    Shapiro, B.2
  • 30
    • 0037119475 scopus 로고    scopus 로고
    • Functional role of fatty acyl-coenzyme A synthetase in the transmembrane movement and activation of exogenous long-chain fatty acids. Amino acid residues within the ATP/AMP signature motif of Escherichia coli FadD are required for enzyme activity and fatty acid transport
    • Weimar J.D., DiRusso C.C., Delio R., and Black P.N. Functional role of fatty acyl-coenzyme A synthetase in the transmembrane movement and activation of exogenous long-chain fatty acids. Amino acid residues within the ATP/AMP signature motif of Escherichia coli FadD are required for enzyme activity and fatty acid transport. J. Biol. Chem. 277 (2002) 29369-29376
    • (2002) J. Biol. Chem. , vol.277 , pp. 29369-29376
    • Weimar, J.D.1    DiRusso, C.C.2    Delio, R.3    Black, P.N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.