Lmfa07050031

Lmfa07050031 is a lipid of Fatty Acyls (FA) class. The involved functions are known as Pigment and Polymerization. The related lipids are Propionate.

Cross Reference

Introduction

To understand associated biological information of Lmfa07050031, we collected biological information of abnormalities, associated pathways, cellular/molecular locations, biological functions, related genes/proteins, lipids and common seen animal/experimental models with organized paragraphs from literatures.

What diseases are associated with Lmfa07050031?

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

Possible diseases from mapped MeSH terms on references

We collected disease MeSH terms mapped to the references associated with Lmfa07050031

MeSH term MeSH ID Detail
Diabetes Mellitus D003920 90 associated lipids
Adenocarcinoma D000230 166 associated lipids
Reperfusion Injury D015427 65 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
Heart Failure D006333 36 associated lipids
Prostatic Neoplasms D011471 126 associated lipids
Hypothyroidism D007037 32 associated lipids
Weight Gain D015430 101 associated lipids
Hypoglycemia D007003 13 associated lipids
Alcoholism D000437 27 associated lipids
Starvation D013217 47 associated lipids
Hypertension D006973 115 associated lipids
Cytomegalovirus Infections D003586 7 associated lipids
Protein-Energy Malnutrition D011502 9 associated lipids
Cachexia D002100 21 associated lipids
Hyperinsulinism D006946 27 associated lipids
Placental Insufficiency D010927 6 associated lipids
Per page 10 20 50 | Total 27

PubChem Associated disorders and diseases

What pathways are associated with Lmfa07050031

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

PubChem Biomolecular Interactions and Pathways

Link to PubChem Biomolecular Interactions and Pathways

What cellular locations are associated with Lmfa07050031?

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

What functions are associated with Lmfa07050031?


Related references are published most in these journals:

Function Cross reference Weighted score Related literatures

What lipids are associated with Lmfa07050031?

Related references are published most in these journals:

Lipid concept Cross reference Weighted score Related literatures
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What genes are associated with Lmfa07050031?

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

What common seen animal models are associated with Lmfa07050031?

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

NCBI Entrez Crosslinks

All references with Lmfa07050031

Download all related citations
Per page 10 20 50 100 | Total 787
Authors Title Published Journal PubMed Link
Walker TA et al. Kinetic studies of the fatty acid synthetase multienzyme complex from Euglena gracilis variety bacillaris. 1981 Biochem. J. pmid:6803763
Kolattukudy PE et al. Malonyl-CoA decarboxylase from avian, mammalian, and microbial sources. 1981 Meth. Enzymol. pmid:6792462
Saito K et al. Differential hydrogen exchange during the fatty acid synthetase reaction: deuterium distribution of fatty acids synthesized from [2-2H2]malonyl-CoA. 1982 Biochem. Biophys. Res. Commun. pmid:6758778
Mills SE et al. Effects of pH on the interaction of substrates and malonyl-CoA with mitochondrial carnitine palmitoyltransferase I. 1984 Biochem. J. pmid:6743235
Singh B et al. Determination of malonyl-coenzyme A in rat heart, kidney, and liver: a comparison between acetyl-coenzyme A and butyryl-coenzyme A as fatty acid synthase primers in the assay procedure. 1984 Anal. Biochem. pmid:6731835
Zammit VA Time-dependence of inhibition of carnitine palmitoyltransferase I by malonyl-CoA in mitochondria isolated from livers of fed or starved rats. Evidence for transition of the enzyme between states of low and high affinity for malonyl-CoA. 1984 Biochem. J. pmid:6712621
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
Kaneda T et al. Fatty acid composition and primer specificity of de novo fatty acid synthetase in Bacillus globispores, Bacillus insolitus, and Bacillus psychrophilus. 1983 Can. J. Microbiol. pmid:6673817
Klimov AN et al. [Biosynthesis of mevalonic acid, sterols and bile acids from acetyl-CoA and malonyl-CoA in the human liver]. 1983 Biokhimiia pmid:6661459
McCormick K et al. Inhibition by acetyl-CoA of hepatic carnitine acyltransferase and fatty acid oxidation. 1983 Biochem. J. pmid:6661211
Zammit VA Reversible sensitization and desensitization of carnitine palmitoyltransferase I to inhibition by malonyl-CoA in isolated rat liver mitochondria. Significance for the mechanism of malonyl-CoA-induced sensitization. 1983 Biochem. J. pmid:6626153
Mills SE et al. Interaction of malonyl-CoA and related compounds with mitochondria from different rat tissues. Relationship between ligand binding and inhibition of carnitine palmitoyltransferase I. 1983 Biochem. J. pmid:6615474
McGarry JD et al. Carnitine palmitoyltransferase I. The site of inhibition of hepatic fatty acid oxidation by malonyl-CoA. 1978 J. Biol. Chem. pmid:659409
McCarthy AD and Hardie DG The multifunctional polypeptide chains of rabbit-mammary fatty-acid synthase. Stoichiometry of active sites and active-site mapping using limited proteolysis. 1983 Eur. J. Biochem. pmid:6549986
Trevisan CP et al. Myoglobinuria and carnitine palmityltransferase (CPT) deficiency: studies with malonyl-CoA suggest absence of only CPT-II. 1984 Neurology pmid:6538275
Cook GA Involvement of hysteretic effects in the inhibition of carnitine palmitoyltransferase by malonyl-CoA. 1984 Biochem. J. pmid:6525169
Saggerson ED et al. Cycloheximide blocks changes in rat liver carnitine palmitoyltransferase 1 activity in starvation. 1984 Biochem. J. pmid:6508756
Kollmann-Koch A and Eggerer H Nicotinic acid metabolism. Dimethylmaleate hydratase. 1984 Hoppe-Seyler's Z. Physiol. Chem. pmid:6489933
Cook GA Differences in the sensitivity of carnitine palmitoyltransferase to inhibition by malonyl-CoA are due to differences in Ki values. 1984 J. Biol. Chem. pmid:6480597
Zammit VA et al. Changes in the ability of malonyl-CoA to inhibit carnitine palmitoyltransferase I activity and to bind to rat liver mitochondria during incubation in vitro. Differences in binding at 0 degree C and 37 degrees C with a fixed concentration of malonyl-CoA. 1984 Biochem. J. pmid:6477517