Page last updated: 2024-08-17

histidine and malonyl coenzyme a

histidine has been researched along with malonyl coenzyme a in 7 studies

Research

Studies (7)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's1 (14.29)18.2507
2000's6 (85.71)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Brown, NF; Foster, DW; McGarry, JD; Swanson, ST1
Ariño, J; Asins, G; Clotet, J; Hegardt, FG; Morillas, M; Rubí, B; Serra, D1
Brown, NF; McGarry, JD1
Fukuma, K; Kagami, J; Sankawa, U; Suh, DY1
Asins, G; Gómez-Puertas, P; Hegardt, FG; Morillas, M; Roca, R; Serra, D; Valencia, A1
Cane, DE; Khosla, C; Lau, J; Liou, GF1
Dawe, JH; Porter, CT; Tabor, AB; Thornton, JM1

Other Studies

7 other study(ies) available for histidine and malonyl coenzyme a

ArticleYear
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.
    The Biochemical journal, 1998, Nov-01, Volume: 335 ( Pt 3)

    Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Carnitine O-Palmitoyltransferase; Conserved Sequence; COS Cells; Epoxy Compounds; Histidine; Isoenzymes; Kinetics; Malonyl Coenzyme A; Mutagenesis, Site-Directed; Peptide Fragments; Point Mutation; Rats; Recombinant Fusion Proteins; Transfection

1998
Identification of the two histidine residues responsible for the inhibition by malonyl-CoA in peroxisomal carnitine octanoyltransferase from rat liver.
    FEBS letters, 2000, Jan-21, Volume: 466, Issue:1

    Topics: Amino Acid Sequence; Animals; Base Sequence; Carnitine Acyltransferases; Catalytic Domain; DNA Primers; DNA, Complementary; Gene Expression; Histidine; Humans; In Vitro Techniques; Kinetics; Liver; Malonyl Coenzyme A; Mutagenesis, Site-Directed; Peroxisomes; Point Mutation; Rats; Recombinant Proteins; Saccharomyces cerevisiae; Sequence Homology, Amino Acid

2000
Reconstitution of purified, active and malonyl-CoA-sensitive rat liver carnitine palmitoyltransferase I: relationship between membrane environment and malonyl-CoA sensitivity.
    The Biochemical journal, 2000, Jul-01, Volume: 349, Issue:Pt 1

    Topics: Animals; Carnitine O-Palmitoyltransferase; Cell Membrane; Dose-Response Relationship, Drug; Food Deprivation; Histidine; Hydrogen-Ion Concentration; Inhibitory Concentration 50; Kinetics; Liver; Malonyl Coenzyme A; Mitochondria, Liver; Pichia; Plasmids; Protein Isoforms; Rats; Rats, Sprague-Dawley; Recombinant Proteins; Temperature

2000
Evidence for catalytic cysteine-histidine dyad in chalcone synthase.
    Biochemical and biophysical research communications, 2000, Sep-07, Volume: 275, Issue:3

    Topics: Acyltransferases; Amino Acid Substitution; Binding Sites; Catalysis; Cysteine; Diethyl Pyrocarbonate; Enzyme Inhibitors; Escherichia coli; Flavanones; Flavonoids; Histidine; Hydrogen-Ion Concentration; Iodoacetamide; Malonyl Coenzyme A; Mutagenesis, Site-Directed; Plants; Recombinant Fusion Proteins; Resveratrol; Stilbenes

2000
Structural model of the catalytic core of carnitine palmitoyltransferase I and carnitine octanoyltransferase (COT): mutation of CPT I histidine 473 and alanine 381 and COT alanine 238 impairs the catalytic activity.
    The Journal of biological chemistry, 2001, Nov-30, Volume: 276, Issue:48

    Topics: Alanine; Amino Acid Sequence; Animals; Binding Sites; Carnitine Acyltransferases; Carnitine O-Palmitoyltransferase; Catalysis; Catalytic Domain; Dose-Response Relationship, Drug; Histidine; Kinetics; Malonyl Coenzyme A; Mice; Models, Molecular; Molecular Sequence Data; Multigene Family; Mutagenesis, Site-Directed; Mutation; Plasmids; Protein Conformation; Protein Isoforms; Protein Structure, Secondary; Protein Structure, Tertiary; Rats; Saccharomyces cerevisiae; Sequence Homology, Amino Acid

2001
Quantitative analysis of loading and extender acyltransferases of modular polyketide synthases.
    Biochemistry, 2003, Jan-14, Volume: 42, Issue:1

    Topics: Acetyl Coenzyme A; Acyl Carrier Protein; Acyl Coenzyme A; Acyltransferases; Cysteamine; Genetic Vectors; Histidine; Kinetics; Malonyl Coenzyme A; Multienzyme Complexes; Mutagenesis, Site-Directed; Protein Structure, Tertiary; Protein Subunits; Quantitative Structure-Activity Relationship; Sirolimus; Substrate Specificity

2003
A template search reveals mechanistic similarities and differences in beta-ketoacyl synthases (KAS) and related enzymes.
    Proteins, 2003, Aug-15, Volume: 52, Issue:3

    Topics: 3-Oxoacyl-(Acyl-Carrier-Protein) Synthase; Binding Sites; Computational Biology; Cysteine; Databases, Protein; Enzymes; Histidine; Isoenzymes; Malonyl Coenzyme A; Molecular Structure

2003