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
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
Rainwater DL and Kolattukudy PE Fatty acid biosynthesis in Mycobacterium tuberculosis var. bovis Bacillus Calmette-Guérin. Purification and characterization of a novel fatty acid synthase, mycocerosic acid synthase, which elongates n-fatty acyl-CoA with methylmalonyl-CoA. 1985 J. Biol. Chem. pmid:3880746
Anderson GJ and Kolattukudy PE Fatty acid chain elongation by microsomal enzymes from the bovine meibomian gland. 1985 Arch. Biochem. Biophys. pmid:3918501
Mikkelsen J et al. Amino acid sequence around the active-site serine residue in the acyltransferase domain of goat mammary fatty acid synthetase. 1985 Biochem. J. pmid:3922356
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
Decaux JF et al. [Development of hepatic fatty acid metabolism in the rat during weaning]. 1985 Reprod Nutr Dev pmid:3992000
Bourre JM and Dumont O Changes in fatty acid elongation in developing mouse brain by mercury--comparison with other metals. 1985 Toxicol. Lett. pmid:3992602
Anderson VE and Hammes GG Distribution of reaction intermediates on chicken liver fatty acid synthase. 1985 Biochemistry pmid:3995008
Mikkelsen J et al. Evidence that the medium-chain acyltransferase of lactating-goat mammary-gland fatty acid synthetase is identical with the acetyl/malonyltransferase. 1985 Biochem. J. pmid:4004809
Bird MI et al. Carnitine acyltransferase activities in rat brain mitochondria. Bimodal distribution, kinetic constants, regulation by malonyl-CoA and developmental pattern. 1985 Biochem. J. pmid:3977877
Clouet P et al. High sensitivity of carnitine acyltransferase I to malonyl-CoA inhibition in liver of obese Zucker rats. 1985 FEBS Lett. pmid:3979557
Zammit VA and Corstorphine CG Altered release of carnitine palmitoyltransferase activity by digitonin from liver mitochondria of rats in different physiological states. 1985 Biochem. J. pmid:4052052
Zammit VA and Corstorphine CG Effects of incubation at physiological temperatures on the concentration-dependence of [2-14C]malonyl-CoA binding to rat liver mitochondria. 1985 Biochem. J. pmid:4062901
Scholte HR et al. The source of malonyl-CoA in rat heart. The calcium paradox releases acetyl-CoA carboxylase and not propionyl-CoA carboxylase. 1986 FEBS Lett. pmid:2869975
Wölfle K et al. On the mechanism of action of methylmalonyl-CoA mutase. Change of the steric course on isotope substitution. 1986 Eur. J. Biochem. pmid:2870921
De Spiegeleer B et al. Direct assay for phosphotransacetylase and acetyl-coenzyme A carboxylase by high-performance liquid chromatography. 1986 Anal. Biochem. pmid:2879484
Wakil SJ The relationship between structure and function for and the regulation of the enzymes of fatty acid synthesis. 1986 Ann. N. Y. Acad. Sci. pmid:2879500
Hinderer W and Seitz HU In vitro inhibition of carrot chalcone synthase by 3'-nucleotidase: the role of the 3'-phosphate group of malonyl-coenzyme A in flavonoid biosynthesis. 1986 Arch. Biochem. Biophys. pmid:3008651
Bergseth S et al. Is carnitine palmitoyltransferase inhibited by a malonyl-CoA-binding unit in the mitochondria? 1986 Biochem. Soc. Trans. pmid:3743880
Cook GA and Cox KA Hysteretic behaviour of carnitine palmitoyltransferase. The effect of preincubation with malonyl-CoA. 1986 Biochem. J. pmid:3790097
Jackowski S and Rock CO Consequences of reduced intracellular coenzyme A content in Escherichia coli. 1986 J. Bacteriol. pmid:3519582