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Volumn 101, Issue 3, 2013, Pages 195-203

Molecular characterization, Tissue distribution and kinetic analysis of carnitine palmitoyltransferase I in juvenile yellow catfish Pelteobagrus fulvidraco

Author keywords

Carnitine palmitoyltransferase I; Isoforms; Kinetic characteristics; MRNA expression; Pelteobagrus fulvidraco

Indexed keywords

CARNITINE PALMITOYLTRANSFERASE 1 ALPHA 1A; CARNITINE PALMITOYLTRANSFERASE 1 ALPHA 1B; CARNITINE PALMITOYLTRANSFERASE 1 ALPHA 2A; CARNITINE PALMITOYLTRANSFERASE 1 BETA; CARNITINE PALMITOYLTRANSFERASE I; LIPID; MALONYL COENZYME A; MESSENGER RNA; UNCLASSIFIED DRUG;

EID: 84873522667     PISSN: 08887543     EISSN: 10898646     Source Type: Journal    
DOI: 10.1016/j.ygeno.2012.12.002     Document Type: Article
Times cited : (46)

References (50)
  • 1
    • 0031043030 scopus 로고    scopus 로고
    • The mitochondrial carnitine palmitoyltransferase system. From concept to molecular analysis
    • McGarry J.D., Brown N.F. The mitochondrial carnitine palmitoyltransferase system. From concept to molecular analysis. Eur. J. Biochem. 1997, 244:1-14.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 1-14
    • McGarry, J.D.1    Brown, N.F.2
  • 2
    • 0034717940 scopus 로고    scopus 로고
    • Fatty acid import into mitochondria
    • Kerner J., Hoppel C. Fatty acid import into mitochondria. Biochim. Biophys. Acta 2000, 1486:1-17.
    • (2000) Biochim. Biophys. Acta , vol.1486 , pp. 1-17
    • Kerner, J.1    Hoppel, C.2
  • 3
    • 0030865233 scopus 로고    scopus 로고
    • Regulation of mitochondrial outer-membrane carnitine palmitoyltransferase (CPT I): role of membrane-topology
    • Zammit V.A., Fraser F., Orstorphine C.G. Regulation of mitochondrial outer-membrane carnitine palmitoyltransferase (CPT I): role of membrane-topology. Adv. Enzyme Regul. 1997, 37:295-317.
    • (1997) Adv. Enzyme Regul. , vol.37 , pp. 295-317
    • Zammit, V.A.1    Fraser, F.2    Orstorphine, C.G.3
  • 4
    • 0018864840 scopus 로고
    • Regulation of hepatic fatty acid oxidation and ketone body production
    • McGarry J.D., Foster D.W. Regulation of hepatic fatty acid oxidation and ketone body production. Annu. Rev. Biochem. 1980, 49:395-420.
    • (1980) Annu. Rev. Biochem. , vol.49 , pp. 395-420
    • McGarry, J.D.1    Foster, D.W.2
  • 5
    • 43649099634 scopus 로고    scopus 로고
    • Intertissue regulation of carnitine palmitoyltransferase I (CPT I): mitochondrial membrane properties and gene expression in rainbow trout (Oncorhynchus mykiss)
    • Morash A.J., Kajimura M., McClelland G.B. Intertissue regulation of carnitine palmitoyltransferase I (CPT I): mitochondrial membrane properties and gene expression in rainbow trout (Oncorhynchus mykiss). Biochim. Biophys. Acta 2008, 1778:1382-1389.
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1382-1389
    • Morash, A.J.1    Kajimura, M.2    McClelland, G.B.3
  • 6
    • 0028904122 scopus 로고
    • Human liver mitochondrial carnitine palmitoyltransferase I: characterization of its cDNA and chromosomal localization and partial analysis of the gene
    • Britton C.H., Schultz R.A., Zhang B., Esser V., Foster D.W., McGarry J.D. Human liver mitochondrial carnitine palmitoyltransferase I: characterization of its cDNA and chromosomal localization and partial analysis of the gene. Proc. Natl. Acad. Sci. U. S. A. 1995, 92:1984-1988.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 1984-1988
    • Britton, C.H.1    Schultz, R.A.2    Zhang, B.3    Esser, V.4    Foster, D.W.5    McGarry, J.D.6
  • 7
    • 0029954776 scopus 로고    scopus 로고
    • Isolation and characterization of cDNA and genomic clones encoding human muscle type carnitine palmitoyltransferase I
    • Yamazaki N., Shinohara Y., Shima A., Yamanaka Y., Terada H. Isolation and characterization of cDNA and genomic clones encoding human muscle type carnitine palmitoyltransferase I. Biochim. Biophys. Acta 1996, 1307:157-161.
    • (1996) Biochim. Biophys. Acta , vol.1307 , pp. 157-161
    • Yamazaki, N.1    Shinohara, Y.2    Shima, A.3    Yamanaka, Y.4    Terada, H.5
  • 10
    • 0037683658 scopus 로고    scopus 로고
    • Cloning and tissue distribution of a carnitine palmitoyltransferase I gene in rainbow trout (Oncorhynchus mykiss)
    • Gutieres S., Damon M., Panserat S., Kaushik S., Medale F. Cloning and tissue distribution of a carnitine palmitoyltransferase I gene in rainbow trout (Oncorhynchus mykiss). Comp. Biochem. Physiol. 2003, 135B:139-151.
    • (2003) Comp. Biochem. Physiol. , vol.135 B , pp. 139-151
    • Gutieres, S.1    Damon, M.2    Panserat, S.3    Kaushik, S.4    Medale, F.5
  • 11
    • 77954864428 scopus 로고    scopus 로고
    • Molecular regulation of lipid metabolism in liver and muscle of rainbow trout subjected to acute and chronic insulin treatments
    • Polakof S., Medale F., Skiba-Cassy S., Corraze G., Panserat S. Molecular regulation of lipid metabolism in liver and muscle of rainbow trout subjected to acute and chronic insulin treatments. Domest. Anim. Endocrinol. 2010, 39:26-33.
    • (2010) Domest. Anim. Endocrinol. , vol.39 , pp. 26-33
    • Polakof, S.1    Medale, F.2    Skiba-Cassy, S.3    Corraze, G.4    Panserat, S.5
  • 12
    • 84861850750 scopus 로고    scopus 로고
    • Link between lipid metabolism and voluntary food intake in rainbow trout fed coconut oil rich in medium-chain TAG
    • Figueiredo-Silva A.C., Kaushik S., Terrier F., Schrama J.W., Medale F., Geurden I. Link between lipid metabolism and voluntary food intake in rainbow trout fed coconut oil rich in medium-chain TAG. Br. J. Nutr. 2012, 10.1017/S0007114511004739.
    • (2012) Br. J. Nutr.
    • Figueiredo-Silva, A.C.1    Kaushik, S.2    Terrier, F.3    Schrama, J.W.4    Medale, F.5    Geurden, I.6
  • 13
    • 77955092147 scopus 로고    scopus 로고
    • Molecular characterization of a gilthead sea bream (Sparus aurata) muscle tissue cDNA for carnitine palmitoyltransferase 1B (CPT1B)
    • Boukouvala E., Leaver M.J., Favre-Krey L., Theodoridou M., Krey G. Molecular characterization of a gilthead sea bream (Sparus aurata) muscle tissue cDNA for carnitine palmitoyltransferase 1B (CPT1B). Comp. Biochem. Physiol. 2010, 157B:189-197.
    • (2010) Comp. Biochem. Physiol. , vol.157 B , pp. 189-197
    • Boukouvala, E.1    Leaver, M.J.2    Favre-Krey, L.3    Theodoridou, M.4    Krey, G.5
  • 14
    • 17344392308 scopus 로고    scopus 로고
    • A new mathematical model for relative quantification in real-time RT-PCR
    • Pfaffl M.W. A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res. 2001, 29:2003-2007.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 2003-2007
    • Pfaffl, M.W.1
  • 15
    • 0011464758 scopus 로고
    • Preparation and properties of rainbow trout liver mitochondria
    • Suarez R.K., Hochachka P.W. Preparation and properties of rainbow trout liver mitochondria. J. Comp. Physiol. 1981, 143B:269-273.
    • (1981) J. Comp. Physiol. , vol.143 B , pp. 269-273
    • Suarez, R.K.1    Hochachka, P.W.2
  • 16
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 17
    • 0020624753 scopus 로고
    • Observations on the affinity for carnitine, and malonyl-CoA sensitivity, of carnitine palmitoyltransferase I in animal and human tissues. Demonstration of the presence of malonyl-CoA in non-hepatic tissues of the rat
    • McGarry J.D., Mills S.E., Long C.S., Foster D.W. Observations on the affinity for carnitine, and malonyl-CoA sensitivity, of carnitine palmitoyltransferase I in animal and human tissues. Demonstration of the presence of malonyl-CoA in non-hepatic tissues of the rat. Biochem. J. 1983, 214:21-28.
    • (1983) Biochem. J. , vol.214 , pp. 21-28
    • McGarry, J.D.1    Mills, S.E.2    Long, C.S.3    Foster, D.W.4
  • 18
    • 0022559002 scopus 로고
    • Purification and assay of carnitine acyltransferases
    • Bieber L.L., Fiol C. Purification and assay of carnitine acyltransferases. Methods Enzymol. 1986, 123:276-284.
    • (1986) Methods Enzymol. , vol.123 , pp. 276-284
    • Bieber, L.L.1    Fiol, C.2
  • 19
    • 0034927508 scopus 로고    scopus 로고
    • Inhibition of mitochondrial carnitine palmitoyltransferase-1 by a trimetazidine derivative, S-15176
    • Hamdan M., Urien S., Le Louet H., Tillement J.P., Morin D. Inhibition of mitochondrial carnitine palmitoyltransferase-1 by a trimetazidine derivative, S-15176. Pharmacol. Res. 2001, 44:99-104.
    • (2001) Pharmacol. Res. , vol.44 , pp. 99-104
    • Hamdan, M.1    Urien, S.2    Le Louet, H.3    Tillement, J.P.4    Morin, D.5
  • 20
    • 5844225066 scopus 로고
    • On the evaluation of the constants Vm and KM in enzyme reactions
    • Hofstee B. On the evaluation of the constants Vm and KM in enzyme reactions. Science 1952, 116:329-331.
    • (1952) Science , vol.116 , pp. 329-331
    • Hofstee, B.1
  • 21
    • 33751330608 scopus 로고
    • The determination of enzyme dissociation constants
    • Lineweaver H., Burk D. The determination of enzyme dissociation constants. J. Am. Chem. Soc. 1934, 56:658-666.
    • (1934) J. Am. Chem. Soc. , vol.56 , pp. 658-666
    • Lineweaver, H.1    Burk, D.2
  • 22
    • 0035064946 scopus 로고    scopus 로고
    • Evolutionary rates of duplicate genes in fish and mammals
    • Robinson-Rechavi M., Laudet V. Evolutionary rates of duplicate genes in fish and mammals. Mol. Biol. Evol. 2001, 18:681-683.
    • (2001) Mol. Biol. Evol. , vol.18 , pp. 681-683
    • Robinson-Rechavi, M.1    Laudet, V.2
  • 23
    • 57649142833 scopus 로고    scopus 로고
    • A characteristic Glu17 residue of pig carnitine palmitoyltransferase 1 is responsible for the low Km for carnitine and the low sensitivity to malonyl-CoA inhibition of the enzyme
    • Relat J., Pujol-Vidal M., Haro D., Marrero P.F. A characteristic Glu17 residue of pig carnitine palmitoyltransferase 1 is responsible for the low Km for carnitine and the low sensitivity to malonyl-CoA inhibition of the enzyme. FEBS J. 2009, 276:210-218.
    • (2009) FEBS J. , vol.276 , pp. 210-218
    • Relat, J.1    Pujol-Vidal, M.2    Haro, D.3    Marrero, P.F.4
  • 24
    • 0022237772 scopus 로고
    • Phosphorylation of carnitine palmitoyltransferase and activation by glucagon in isolated rat hepatocytes
    • Harano Y., Kashiwagi A., Kojima H., Suzuki M., Hashimoto T., Shigeta Y. Phosphorylation of carnitine palmitoyltransferase and activation by glucagon in isolated rat hepatocytes. FEBS Lett. 1985, 188:267-272.
    • (1985) FEBS Lett. , vol.188 , pp. 267-272
    • Harano, Y.1    Kashiwagi, A.2    Kojima, H.3    Suzuki, M.4    Hashimoto, T.5    Shigeta, Y.6
  • 26
    • 34247634168 scopus 로고    scopus 로고
    • Post-translational modifications of rat liver mitochondrial outer membrane proteins identified by mass spectrometry
    • Distler A.M., Kerner J., Hoppel C.L. Post-translational modifications of rat liver mitochondrial outer membrane proteins identified by mass spectrometry. Biochim. Biophys. Acta 2007, 1774:628-636.
    • (2007) Biochim. Biophys. Acta , vol.1774 , pp. 628-636
    • Distler, A.M.1    Kerner, J.2    Hoppel, C.L.3
  • 27
    • 0035895945 scopus 로고    scopus 로고
    • The N-terminal domain of rat liver carnitine palmitoyltransferase 1 contains an internal mitochondrial import signal and residues essential for folding of its C-terminal catalytic domain
    • Cohen I., Guillerault F., Girard J., Prip-Buus C. The N-terminal domain of rat liver carnitine palmitoyltransferase 1 contains an internal mitochondrial import signal and residues essential for folding of its C-terminal catalytic domain. J. Biol. Chem. 2001, 276:5403-5411.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5403-5411
    • Cohen, I.1    Guillerault, F.2    Girard, J.3    Prip-Buus, C.4
  • 28
    • 0037436271 scopus 로고    scopus 로고
    • Leucine-764 near the extreme C-terminal end of carnitine palmitoyltransferase I is important for activity
    • Dai J., Zhu H., Woldegiorgis G. Leucine-764 near the extreme C-terminal end of carnitine palmitoyltransferase I is important for activity. Biochem. Biophys. Res. Commun. 2003, 301:758-763.
    • (2003) Biochem. Biophys. Res. Commun. , vol.301 , pp. 758-763
    • Dai, J.1    Zhu, H.2    Woldegiorgis, G.3
  • 29
    • 0032491604 scopus 로고    scopus 로고
    • The N-terminal domain of rat liver carnitine palmitoyltransferase 1 mediates import into the outer mitochondrial membrane and is essential for activity and malonyl-CoA sensitivity
    • Cohen I., Kohl C., McGarry J.D., Girard J., Prip-Buus C. The N-terminal domain of rat liver carnitine palmitoyltransferase 1 mediates import into the outer mitochondrial membrane and is essential for activity and malonyl-CoA sensitivity. J. Biol. Chem. 1998, 273:29896-29904.
    • (1998) J. Biol. Chem. , vol.273 , pp. 29896-29904
    • Cohen, I.1    Kohl, C.2    McGarry, J.D.3    Girard, J.4    Prip-Buus, C.5
  • 30
    • 0032511158 scopus 로고    scopus 로고
    • Topological and functional analysis of the rat liver carnitine palmitoyltransferase 1 expressed in Saccharomyces cerevisiae
    • Prip-Buus C., Cohen I., Kohl C., Esser V., McGarry J.D., Girard J. Topological and functional analysis of the rat liver carnitine palmitoyltransferase 1 expressed in Saccharomyces cerevisiae. FEBS Lett. 1998, 429:173-178.
    • (1998) FEBS Lett. , vol.429 , pp. 173-178
    • Prip-Buus, C.1    Cohen, I.2    Kohl, C.3    Esser, V.4    McGarry, J.D.5    Girard, J.6
  • 31
    • 33845964421 scopus 로고    scopus 로고
    • The mitochondrial intermembrane loop region of rat carnitine palmitoyltransferase 1A is a major determinant of its malonyl-CoA sensitivity
    • Borthwick K., Jackson V.N., Price N.T., Zammit V.A. The mitochondrial intermembrane loop region of rat carnitine palmitoyltransferase 1A is a major determinant of its malonyl-CoA sensitivity. J. Biol. Chem. 2006, 281:32946-32952.
    • (2006) J. Biol. Chem. , vol.281 , pp. 32946-32952
    • Borthwick, K.1    Jackson, V.N.2    Price, N.T.3    Zammit, V.A.4
  • 32
    • 56949093657 scopus 로고    scopus 로고
    • Effects of dietary fatty acid composition on the regulation of carnitine palmitoyltransferase (CPT) I in rainbow trout (Oncorhynchus mykiss)
    • Morash A.J., Bureau D.P., McClelland G.B. Effects of dietary fatty acid composition on the regulation of carnitine palmitoyltransferase (CPT) I in rainbow trout (Oncorhynchus mykiss). Comp. Biochem. Physiol. 2009, 152B:85-93.
    • (2009) Comp. Biochem. Physiol. , vol.152 B , pp. 85-93
    • Morash, A.J.1    Bureau, D.P.2    McClelland, G.B.3
  • 33
    • 41749119661 scopus 로고    scopus 로고
    • Liver and muscle metabolic changes induced by dietary energy content and genetic selection in rainbow trout (Oncorhynchus mykiss)
    • Kolditz C., Borthaire M., Richard N., Corraze G., Panserat S., Vachot C., Lefevre F., Medale F. Liver and muscle metabolic changes induced by dietary energy content and genetic selection in rainbow trout (Oncorhynchus mykiss). Am. J. Physiol. 2008, 294:R1154-R1164.
    • (2008) Am. J. Physiol. , vol.294
    • Kolditz, C.1    Borthaire, M.2    Richard, N.3    Corraze, G.4    Panserat, S.5    Vachot, C.6    Lefevre, F.7    Medale, F.8
  • 34
    • 0033515467 scopus 로고    scopus 로고
    • A single amino acid change (substitution of glutamate 3 with alanine) in the N-terminal region of rat liver carnitine palmitoyltransferase I abolishes malonyl-CoA inhibition and high affinity binding
    • Shi J., Zhu H., Arvidson D.N., Woldegiorgis G. A single amino acid change (substitution of glutamate 3 with alanine) in the N-terminal region of rat liver carnitine palmitoyltransferase I abolishes malonyl-CoA inhibition and high affinity binding. J. Biol. Chem. 1999, 274:9421-9426.
    • (1999) J. Biol. Chem. , vol.274 , pp. 9421-9426
    • Shi, J.1    Zhu, H.2    Arvidson, D.N.3    Woldegiorgis, G.4
  • 35
    • 0034624069 scopus 로고    scopus 로고
    • Identification of positive and negative determinants of malonyl-CoA sensitivity and carnitine affinity within the amino termini of rat liver- and muscle-type carnitine palmitoyltransferase I
    • Jackson V.N., Zammit V.A., Pric N.T. Identification of positive and negative determinants of malonyl-CoA sensitivity and carnitine affinity within the amino termini of rat liver- and muscle-type carnitine palmitoyltransferase I. J. Biol. Chem. 2000, 275:38410-38416.
    • (2000) J. Biol. Chem. , vol.275 , pp. 38410-38416
    • Jackson, V.N.1    Zammit, V.A.2    Pric, N.T.3
  • 36
    • 0035807927 scopus 로고    scopus 로고
    • Specificity of the interactions between Glu-3, Ser-24, and Gln-30 within the N-terminal segment of rat liver mitochondrial overt carnitine palmitoyltransferase (L-CPT I) in determining the malonyl-CoA sensitivity of the enzyme
    • Jackson V.N., Price N.T., Zammit V.A. Specificity of the interactions between Glu-3, Ser-24, and Gln-30 within the N-terminal segment of rat liver mitochondrial overt carnitine palmitoyltransferase (L-CPT I) in determining the malonyl-CoA sensitivity of the enzyme. Biochemistry 2001, 40:14629-14634.
    • (2001) Biochemistry , vol.40 , pp. 14629-14634
    • Jackson, V.N.1    Price, N.T.2    Zammit, V.A.3
  • 37
    • 0037405394 scopus 로고    scopus 로고
    • Substitution of glutamate-3, valine-19, leucine-23, and serine-24 with alanine in the N-terminal region of human heart muscle carnitine palmitoyltransferase I abolishes malonyl CoA inhibition and binding
    • Zhu H., Shi J., Treber M., Dai J., Arvidson D.N., Woldegiorgis G. Substitution of glutamate-3, valine-19, leucine-23, and serine-24 with alanine in the N-terminal region of human heart muscle carnitine palmitoyltransferase I abolishes malonyl CoA inhibition and binding. Arch. Biochem. Biophys. 2003, 413:67-74.
    • (2003) Arch. Biochem. Biophys. , vol.413 , pp. 67-74
    • Zhu, H.1    Shi, J.2    Treber, M.3    Dai, J.4    Arvidson, D.N.5    Woldegiorgis, G.6
  • 38
    • 0032212886 scopus 로고    scopus 로고
    • Roles of the N-and C-terminal domains of carnitine palmitoyltransferase I isoforms in malonyl-CoA sensitivity of the enzymes: insights from expression of chimaeric proteins and mutation of conserved histidine residues
    • Swanson S.T., Foster D.W., McGarry J.D., Brown N.F. Roles of the N-and C-terminal domains of carnitine palmitoyltransferase I isoforms in malonyl-CoA sensitivity of the enzymes: insights from expression of chimaeric proteins and mutation of conserved histidine residues. Biochem. J. 1998, 335:513-519.
    • (1998) Biochem. J. , vol.335 , pp. 513-519
    • Swanson, S.T.1    Foster, D.W.2    McGarry, J.D.3    Brown, N.F.4
  • 41
    • 14244260908 scopus 로고    scopus 로고
    • Cysteine-scanning mutagenesis of muscle carnitine palmitoyltransferase I reveals a single cysteine residue (Cys-305) is important for catalysis
    • Liu H., Zheng G., Treber M., Dai J., Woldegiorgis G. Cysteine-scanning mutagenesis of muscle carnitine palmitoyltransferase I reveals a single cysteine residue (Cys-305) is important for catalysis. J. Biol. Chem. 2005, 280:4524-4531.
    • (2005) J. Biol. Chem. , vol.280 , pp. 4524-4531
    • Liu, H.1    Zheng, G.2    Treber, M.3    Dai, J.4    Woldegiorgis, G.5
  • 42
    • 0242286152 scopus 로고    scopus 로고
    • Mutations of penicillin acylase residue B71 extend substrate specificity by decreasing steric constraints for substrate binding
    • Morillas M., McVey C.E., Brannigan J.A., Ladurner A.G., Forney L.J., Virden R. Mutations of penicillin acylase residue B71 extend substrate specificity by decreasing steric constraints for substrate binding. Biochem. J. 2003, 371:143-150.
    • (2003) Biochem. J. , vol.371 , pp. 143-150
    • Morillas, M.1    McVey, C.E.2    Brannigan, J.A.3    Ladurner, A.G.4    Forney, L.J.5    Virden, R.6
  • 43
    • 0034698039 scopus 로고    scopus 로고
    • Identification by mutagenesis of conserved arginine and tryptophan residues in rat liver carnitine palmitoyltransferase I important for catalytic activity
    • Dai J., Zhu H., Shi J., Woldegiorgis G. Identification by mutagenesis of conserved arginine and tryptophan residues in rat liver carnitine palmitoyltransferase I important for catalytic activity. J. Biol. Chem. 2000, 275:22020-22024.
    • (2000) J. Biol. Chem. , vol.275 , pp. 22020-22024
    • Dai, J.1    Zhu, H.2    Shi, J.3    Woldegiorgis, G.4
  • 44
    • 0032145885 scopus 로고    scopus 로고
    • Molecular basis of hepatic carnitine palmitoyltransferase I deficiency
    • IJlst L., Mandel H., Oostheim W., Ruiter J., Gutman A., Wanders R. Molecular basis of hepatic carnitine palmitoyltransferase I deficiency. J. Clin. Invest. 1998, 102(1998):527-531.
    • (1998) J. Clin. Invest. , vol.102 , Issue.1998 , pp. 527-531
    • IJlst, L.1    Mandel, H.2    Oostheim, W.3    Ruiter, J.4    Gutman, A.5    Wanders, R.6
  • 46
    • 0141817917 scopus 로고    scopus 로고
    • A single amino acid change (substitution of the conserved Glu-590 with alanine) in the C-terminal domain of rat liver carnitine palmitoyltransferase I increases its malonyl-CoA sensitivity close to that observed with the muscle isoform of the enzyme
    • Napal L., Dai J., Treber M., Haro D., Marrero P.F., Woldegiorgis G. A single amino acid change (substitution of the conserved Glu-590 with alanine) in the C-terminal domain of rat liver carnitine palmitoyltransferase I increases its malonyl-CoA sensitivity close to that observed with the muscle isoform of the enzyme. J. Biol. Chem. 2003, 278:34084-34089.
    • (2003) J. Biol. Chem. , vol.278 , pp. 34084-34089
    • Napal, L.1    Dai, J.2    Treber, M.3    Haro, D.4    Marrero, P.F.5    Woldegiorgis, G.6
  • 47
    • 0037837797 scopus 로고    scopus 로고
    • Identification by mutagenesis of conserved arginine and glutamate residues in the C-terminal domain of rat liver carnitine palmitoyltransferase I that are important for catalytic activity and malonyl-CoA sensitivity
    • Treber M., Dai J., Woldegiorgis G. Identification by mutagenesis of conserved arginine and glutamate residues in the C-terminal domain of rat liver carnitine palmitoyltransferase I that are important for catalytic activity and malonyl-CoA sensitivity. J. Biol. Chem. 2003, 278:11145-11149.
    • (2003) J. Biol. Chem. , vol.278 , pp. 11145-11149
    • Treber, M.1    Dai, J.2    Woldegiorgis, G.3
  • 48
    • 0032544596 scopus 로고    scopus 로고
    • Redesign of choline acetyltransferase specificity by protein engineering
    • Cronin C.N. Redesign of choline acetyltransferase specificity by protein engineering. J. Biol. Chem. 1998, 273:24465-24469.
    • (1998) J. Biol. Chem. , vol.273 , pp. 24465-24469
    • Cronin, C.N.1
  • 49
    • 0034142251 scopus 로고    scopus 로고
    • The first 28 N-terminal amino acid residues of human heart muscle carnitine palmitoyltransferase I are essential for malonyl CoA sensitivity and high-affinity binding
    • Shi J., Zhu H., Arvidson D.N., Woldegiorgis G. The first 28 N-terminal amino acid residues of human heart muscle carnitine palmitoyltransferase I are essential for malonyl CoA sensitivity and high-affinity binding. Biochemistry 2000, 39:712-717.
    • (2000) Biochemistry , vol.39 , pp. 712-717
    • Shi, J.1    Zhu, H.2    Arvidson, D.N.3    Woldegiorgis, G.4
  • 50
    • 0037033090 scopus 로고    scopus 로고
    • The extreme C terminus of rat liver carnitine palmitoyltransferase I is not involved in malonyl-CoA sensitivity but in initial protein folding
    • Pan Y., Cohen I., Guillerault F., Feve B., Girard J., Prip-Buus C. The extreme C terminus of rat liver carnitine palmitoyltransferase I is not involved in malonyl-CoA sensitivity but in initial protein folding. J. Biol. Chem. 2002, 277:47184-47189.
    • (2002) J. Biol. Chem. , vol.277 , pp. 47184-47189
    • Pan, Y.1    Cohen, I.2    Guillerault, F.3    Feve, B.4    Girard, J.5    Prip-Buus, C.6


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