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Genomes and Genes | Nigel PriceSummaryAffiliation: Rowett Research Institute Country: UK Publications
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Publications
A novel brain-expressed protein related to carnitine palmitoyltransferase INigel Price
Hannah Research Institute, Ayr, KA6 5HL, UK
Genomics 80:433-42. 2002..Thus this new CPT I related protein may be specialized for the metabolism of a distinct class of fatty acids involved in brain function...
Cloning and expression of the liver and muscle isoforms of ovine carnitine palmitoyltransferase 1: residues within the N-terminus of the muscle isoform influence the kinetic properties of the enzymeNigel T Price
Hannah Research Institute, Ayr KA6 5HL, UK
Biochem J 372:871-9. 2003..The ovine N-terminal segment influences the kinetics of the enzyme for both its substrates, such that the K (m) for palmitoyl-CoA is decreased and that for carnitine is increased for the chimaera, relative to the parental ovine M-CPT 1...- Structural and functional genomics of the CPT1B gene for muscle-type carnitine palmitoyltransferase I in mammalsFeike R van der Leij
Department of Pediatrics, Groningen University Institute for Drug Exploration, University of Groningen and Beatrix Children s Hospital, Groningen 9700RB, The Netherlands
J Biol Chem 277:26994-7005. 2002..Therefore, the involvement of splice variation of M-CPT I in the modulation of malonyl-CoA inhibition of fatty acid oxidation may be less relevant than hitherto assumed... - The mitochondrial intermembrane loop region of rat carnitine palmitoyltransferase 1A is a major determinant of its malonyl-CoA sensitivityKaren Borthwick
Clinical Sciences Research Institute, Warwick Medical School, University of Warwick, University Hospital Coventry and Warwick Campus, Coventry CV2 2DX, UK
J Biol Chem 281:32946-52. 2006..The data suggest that the sequence spanning the loop-TM2 boundary determines the disposition of this TM in the membrane so as to alter the conformation of the C-terminal segment and thus affect its interaction with malonyl-CoA... - Characterisation of an N-terminal variant of acetyl-CoA carboxylase-alpha: expression in human tissues and evolutionary aspectsMaureen T Travers
Cell Biochemistry Group, Hannah Research Institute, Hannah Research Park, Ayr, Scotland KA6 5HL, UK
Biochim Biophys Acta 1634:97-106. 2003.... - Localization of messenger RNAs encoding enzymes associated with malonyl-CoA metabolism in mouse brainAnnette Sorensen
Hannah Research Institute, Ayr KA6 5HL, UK
Brain Res Gene Expr Patterns 1:167-73. 2002..Localization of transcripts encoding enzymes involved in fatty acid synthesis and beta-oxidation in distinct nuclei of the hypothalamus supports a role for malonyl-CoA as a potential effector of satiety... - Demonstration of N- and C-terminal domain intramolecular interactions in rat liver carnitine palmitoyltransferase 1 that determine its degree of malonyl-CoA sensitivityAudrey Faye
, Institut Cochin, INSERM U567, , , 24 rue du Faubourg Saint-Jacques, 75014 Paris, France
Biochem J 387:67-76. 2005.... - Structure and regulation of acetyl-CoA carboxylase genes of metazoaMichael C Barber
Hannah Research Institute, Ayr, KA6 5HL, Scotland, United Kingdom
Biochim Biophys Acta 1733:1-28. 2005..This review focuses on the structure of ACC genes and the putative individual roles of their gene products in fatty acid metabolism, taking an evolutionary viewpoint provided by data in genome databases... - Mutation of surface cysteine 374 to alanine in monoamine oxidase A alters substrate turnover and inactivation by cyclopropylaminesAna Paula B Vintém
Centre for Biomolecular Sciences, University of St Andrews, St Andrews, UK
Bioorg Med Chem 13:3487-95. 2005..The data suggest that mutation of Cys374 influences MAO A catalysis, which has implications for MAO susceptibility to redox damage. These results are compared with previous work on the equivalent residue in MAO B, namely, cysteine 365... - Distinct ontogenic patterns of overt and latent DGAT activities of rat liver microsomesIan J Waterman
Hannah Research Institute, Ayr, Scotland, United Kingdom
J Lipid Res 43:1555-62. 2002..We conclude that post-translational modification may play an important role in the overt and latent distribution of DGAT activity in the liver microsomal membrane... - Rat liver carnitine palmitoyltransferase 1 forms an oligomeric complex within the outer mitochondrial membraneAudrey Faye
Institut Cochin, Centre National de la Recherche Scientifique Unite Mixte de Recherche 8104, Universite Paris Descartes, 24 rue du Faubourg Saint Jacques, 75014 Paris, France
J Biol Chem 282:26908-16. 2007..Based on these findings, we proposed that the oligomeric structure of CPT1A would allow the newly formed acylcarnitines to gain direct access into the intermembrane space, hence facilitating substrate channeling...