Malonyl-coa

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There are no associated biomedical information in the current reference collection.

Current reference collection contains 3249 references associated with Malonyl-coa in LipidPedia. Due to lack of full text of references or no associated biomedical terms are recognized in our current text-mining method, we cannot extract any biomedical terms related to diseases, pathways, locations, functions, genes, lipids, and animal models from the associated reference collection.

Users can download the reference list at the bottom of this page and read the reference manually to find out biomedical information.

Here are additional resources we collected from PubChem and MeSH for Malonyl-coa

Possible diseases from mapped MeSH terms on references

We collected disease MeSH terms mapped to the references associated with Malonyl-coa

MeSH term MeSH ID Detail
Diabetes Mellitus D003920 90 associated lipids
Adenocarcinoma D000230 166 associated lipids
Diabetes Mellitus, Type 2 D003924 87 associated lipids
Fatty Liver D005234 48 associated lipids
Ketosis D007662 13 associated lipids
Body Weight D001835 333 associated lipids
Prostatic Neoplasms D011471 126 associated lipids
Hypothyroidism D007037 32 associated lipids
Weight Gain D015430 101 associated lipids
Hypoglycemia D007003 13 associated lipids
Starvation D013217 47 associated lipids
Cytomegalovirus Infections D003586 7 associated lipids
Angina Pectoris D000787 27 associated lipids
Hyperinsulinism D006946 27 associated lipids
Placental Insufficiency D010927 6 associated lipids
Insulin Resistance D007333 99 associated lipids
Weight Loss D015431 56 associated lipids
Myocardial Stunning D017682 10 associated lipids
Cleft Lip D002971 8 associated lipids
Mitochondrial Myopathies D017240 13 associated lipids
Per page 10 20 | Total 20

PubChem Biomolecular Interactions and Pathways

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All references with Malonyl-coa

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Per page 10 20 50 100 | Total 927
Authors Title Published Journal PubMed Link
Declercq PE et al. Interaction of malonyl-CoA and 2-tetradecylglycidyl-CoA with mitochondrial carnitine palmitoyltransferase I. 1985 J. Biol. Chem. pmid:3840167
Rangan VS et al. Fatty acid synthase dimers containing catalytically active beta-ketoacyl synthase or malonyl/acetyltransferase domains in only one subunit can support fatty acid synthesis at the acyl carrier protein domains of both subunits. 1998 J. Biol. Chem. pmid:9857025
Beaty NB and Lane MD The polymerization of acetyl-CoA carboxylase. 1983 J. Biol. Chem. pmid:6138356
Shi J et al. 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. 1999 J. Biol. Chem. pmid:10092622
Price NT et al. Alternative exon usage in the single CPT1 gene of Drosophila generates functional diversity in the kinetic properties of the enzyme: differential expression of alternatively spliced variants in Drosophila tissues. 2010 J. Biol. Chem. pmid:20061394
Saddik M et al. Acetyl-CoA carboxylase regulation of fatty acid oxidation in the heart. 1993 J. Biol. Chem. pmid:7902355
Guay C et al. A role for ATP-citrate lyase, malic enzyme, and pyruvate/citrate cycling in glucose-induced insulin secretion. 2007 J. Biol. Chem. pmid:17928289
Kovachy RJ et al. Recognition, isolation, and characterization of rat liver D-methylmalonyl coenzyme A hydrolase. 1983 J. Biol. Chem. pmid:6885824
Murthy MS and Pande SV Malonyl-CoA-sensitive and -insensitive carnitine palmitoyltransferase activities of microsomes are due to different proteins. 1994 J. Biol. Chem. pmid:8034571
López-Viñas E et al. Definition by functional and structural analysis of two malonyl-CoA sites in carnitine palmitoyltransferase 1A. 2007 J. Biol. Chem. pmid:17452323
Kerner J et al. Characterization of the malonyl-CoA-sensitive carnitine palmitoyltransferase (CPTo) of a rat heart mitochondrial particle. Evidence that the catalytic unit is CPTi. 1994 J. Biol. Chem. pmid:8132545
Cook GA et al. Yonetani-Theorell analysis of hepatic carnitine palmitoyltransferase-I inhibition indicates two distinct inhibitory binding sites. 1994 J. Biol. Chem. pmid:8132614
Esser V et al. Cloning, sequencing, and expression of a cDNA encoding rat liver carnitine palmitoyltransferase I. Direct evidence that a single polypeptide is involved in inhibitor interaction and catalytic function. 1993 J. Biol. Chem. pmid:8449948
Thampy KG Formation of malonyl coenzyme A in rat heart. Identification and purification of an isozyme of A carboxylase from rat heart. 1989 J. Biol. Chem. pmid:2572585
Jackowski S et al. Acetoacetyl-acyl carrier protein synthase. A target for the antibiotic thiolactomycin. 1989 J. Biol. Chem. pmid:2651445
Kashiwaya Y et al. A ketone ester diet increases brain malonyl-CoA and Uncoupling proteins 4 and 5 while decreasing food intake in the normal Wistar Rat. 2010 J. Biol. Chem. pmid:20529850
Liu H et al. Cysteine-scanning mutagenesis of muscle carnitine palmitoyltransferase I reveals a single cysteine residue (Cys-305) is important for catalysis. 2005 J. Biol. Chem. pmid:15579906
Rose-Kahn G and Bar-Tana J Inhibition of lipid synthesis by beta beta'-tetramethyl-substituted, C14-C22, alpha, omega-dicarboxylic acids in cultured rat hepatocytes. 1985 J. Biol. Chem. pmid:4008497
Pan Y et al. The extreme C terminus of rat liver carnitine palmitoyltransferase I is not involved in malonyl-CoA sensitivity but in initial protein folding. 2002 J. Biol. Chem. pmid:12351641
Hu Z et al. A role for hypothalamic malonyl-CoA in the control of food intake. 2005 J. Biol. Chem. pmid:16219771
Decaux JF et al. Decreased hepatic fatty acid oxidation at weaning in the rat is not linked to a variation of malonyl-CoA concentration. 1988 J. Biol. Chem. pmid:2893801
Treber M et al. 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. 2003 J. Biol. Chem. pmid:12540837
MENON GK and STERN JR Enzymic synthesis and metabolism of malonyl coenzyme A and glutaryl coenzyme A. 1960 J. Biol. Chem. pmid:13769479
Morillas M et al. Identification of conserved amino acid residues in rat liver carnitine palmitoyltransferase I critical for malonyl-CoA inhibition. Mutation of methionine 593 abolishes malonyl-CoA inhibition. 2003 J. Biol. Chem. pmid:12499375
Miyazawa T et al. Identification of Middle Chain Fatty Acyl-CoA Ligase Responsible for the Biosynthesis of 2-Alkylmalonyl-CoAs for Polyketide Extender Unit. 2015 J. Biol. Chem. pmid:26378232
Mulder H et al. Overexpression of a modified human malonyl-CoA decarboxylase blocks the glucose-induced increase in malonyl-CoA level but has no impact on insulin secretion in INS-1-derived (832/13) beta-cells. 2001 J. Biol. Chem. pmid:11113153
Jackson VN et al. 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. 2000 J. Biol. Chem. pmid:10969089
HATCH MD and STUMPF PK Fat metabolism in higher plants. XVI. Acetyl coenzyme A carboxylase and acyl coenzyme A-malonyl coenzyme A transcarboxylase from wheat germ. 1961 J. Biol. Chem. pmid:13905314
Declercq PE et al. Characterization of the mitochondrial carnitine palmitoyltransferase enzyme system. I. Use of inhibitors. 1987 J. Biol. Chem. pmid:3597441
VAGELOS PR and ALBERTS AW Malonyl coenzyme A-carbon dioxide exchange reaction. 1960 J. Biol. Chem. pmid:13779560
VAGELOS PR Propionic acid metabolism. IV. Synthesis of malonyl coenzyme A. 1960 J. Biol. Chem. pmid:13840646
VAGELOS PR and EARL JM Propionic acid metabolism. III. beta-Hydroxypropionyl coenzyme A and malonyl semialdehyde coenzyme A, intermediates in propionate oxidation by Clostridium kluyveri. 1959 J. Biol. Chem. pmid:13840645
Prasad MR et al. Rat hepatic microsomal acetoacetyl-CoA reductase. A beta-ketoacyl-CoA reductase distinct from the long chain beta-ketoacyl-CoA reductase component of the microsomal fatty acid chain elongation system. 1984 J. Biol. Chem. pmid:6376489
Jin Z et al. Compartmentation of Metabolism of the C12-, C9-, and C5-n-dicarboxylates in Rat Liver, Investigated by Mass Isotopomer Analysis: ANAPLEROSIS FROM DODECANEDIOATE. 2015 J. Biol. Chem. pmid:26070565
Gamble MS and Cook GA Alteration of the apparent Ki of carnitine palmitoyltransferase for malonyl-CoA by the diabetic state and reversal by insulin. 1985 J. Biol. Chem. pmid:3894356
BRODIE JD et al. The participation of malonyl coenzyme A in the biosynthesis of mevalonic acid. 1963 J. Biol. Chem. pmid:14015675
Fraser F et al. Distinct kinetics of carnitine palmitoyltransferase i in contact sites and outer membranes of rat liver mitochondria. 2001 J. Biol. Chem. pmid:11274214
Soulié JM et al. Transient kinetic studies of fatty acid synthetase. A kinetic self-editing mechanism for the loading of acetyl and malonyl residues and the role of coenzyme A. 1984 J. Biol. Chem. pmid:6706923
Gokulan K et al. Crystal structure of Mycobacterium tuberculosis polyketide synthase 11 (PKS11) reveals intermediates in the synthesis of methyl-branched alkylpyrones. 2013 J. Biol. Chem. pmid:23615910
Gande R et al. Acyl-CoA carboxylases (accD2 and accD3), together with a unique polyketide synthase (Cg-pks), are key to mycolic acid biosynthesis in Corynebacterianeae such as Corynebacterium glutamicum and Mycobacterium tuberculosis. 2004 J. Biol. Chem. pmid:15308633
Kerner J et al. Phosphorylation of rat liver mitochondrial carnitine palmitoyltransferase-I: effect on the kinetic properties of the enzyme. 2004 J. Biol. Chem. pmid:15247243
Onay-Besikci A et al. gAd-globular head domain of adiponectin increases fatty acid oxidation in newborn rabbit hearts. 2004 J. Biol. Chem. pmid:15269215
Reszko AE et al. Regulation of malonyl-CoA concentration and turnover in the normal heart. 2004 J. Biol. Chem. pmid:15181001
Fernandes ND and Kolattukudy PE A newly identified methyl-branched chain fatty acid synthesizing enzyme from Mycobacterium tuberculosis var. bovis BCG. 1998 J. Biol. Chem. pmid:9446591
Rangan VS and Smith S Expression in Escherichia coli and refolding of the malonyl-/acetyltransferase domain of the multifunctional animal fatty acid synthase. 1996 J. Biol. Chem. pmid:8940200
Bederman IR et al. In vitro modeling of fatty acid synthesis under conditions simulating the zonation of lipogenic [13C]acetyl-CoA enrichment in the liver. 2004 J. Biol. Chem. pmid:15284243
Rangan VS and Smith S Alteration of the substrate specificity of the malonyl-CoA/acetyl-CoA:acyl carrier protein S-acyltransferase domain of the multifunctional fatty acid synthase by mutation of a single arginine residue. 1997 J. Biol. Chem. pmid:9115261
Bortolami S et al. Long chain fatty acyl-CoA modulation of H(2)O (2) release at mitochondrial complex I. 2008 J. Bioenerg. Biomembr. pmid:18214656
Ohashi K et al. Assay of fatty acid synthetase by mass fragmentography using [13C]malonyl-CoA. 1985 J. Biochem. pmid:4019438
Kawaguchi A et al. Substrate control of termination of fatty acid biosynthesis by fatty acid synthetase from Brevibacterium ammoniagenes. 1980 J. Biochem. pmid:7419496