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
Hyperinsulinism D006946 27 associated lipids
Hypertension D006973 115 associated lipids
Hypoglycemia D007003 13 associated lipids
Hypothyroidism D007037 32 associated lipids
Insulin Resistance D007333 99 associated lipids
Ketosis D007662 13 associated lipids
Medulloblastoma D008527 22 associated lipids
Mercury Poisoning D008630 4 associated lipids
Placental Insufficiency D010927 6 associated lipids
Prostatic Neoplasms D011471 126 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
Swanson ST et al. 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. 1998 Biochem. J. pmid:9794789
Jackson VN et al. Sequencing and functional expression of the malonyl-CoA-sensitive carnitine palmitoyltransferase from Drosophila melanogaster. 1999 Biochem. J. pmid:10417309
Zammit VA The malonyl-CoA-long-chain acyl-CoA axis in the maintenance of mammalian cell function. 1999 Biochem. J. pmid:10527927
Niot I et al. Involvement of microsomal vesicles in part of the sensitivity of carnitine palmitoyltransferase I to malonyl-CoA inhibition in mitochondrial fractions of rat liver. 1994 Biochem. J. pmid:7998995
Roughan G A semi-preparative enzymic synthesis of malonyl-CoA from [14C]acetate and 14CO2: labelling in the 1, 2 or 3 position. 1994 Biochem. J. pmid:8002939
Guzman M et al. Evidence against direct involvement of phosphorylation in the activation of carnitine palmitoyltransferase by okadaic acid in rat hepatocytes. 1994 Biochem. J. pmid:8010950
Zammit VA et al. Target size analysis by radiation inactivation of carnitine palmitoyltransferase activity and malonyl-CoA binding in outer membranes from rat liver mitochondria. 1989 Biochem. J. pmid:2604707
Derrick JP and Ramsay RR L-carnitine acyltransferase in intact peroxisomes is inhibited by malonyl-CoA. 1989 Biochem. J. pmid:2590167
Baquet A et al. Comparison of the effects of various amino acids on glycogen synthesis, lipogenesis and ketogenesis in isolated rat hepatocytes. 1991 Biochem. J. pmid:1989589
Leadlay PF and Fuller JQ Proton transfer in methylmalonyl-CoA epimerase from Propionibacterium shermanii. Studies with specifically tritiated (2R)-methylmalonyl-CoA as substrate. 1983 Biochem. J. pmid:6311169
Fuller JQ and Leadlay PF Proton transfer in methylmalonyl-CoA epimerase from Propionibacterium shermanii. The reaction of (2R)-methylmalonyl-CoA in tritiated water. 1983 Biochem. J. pmid:6311170
Saggerson ED and Carpenter CA Sensitivity of brown-adipose-tissue carnitine palmitoyltransferase to inhibition by malonyl-CoA. 1982 Biochem. J. pmid:7115330
Zierz S and Engel AG Different sites of inhibition of carnitine palmitoyltransferase by malonyl-CoA, and by acetyl-CoA and CoA, in human skeletal muscle. 1987 Biochem. J. pmid:3663146
Guzmán M et al. Flexibility of zonation of fatty acid oxidation in rat liver. 1995 Biochem. J. pmid:7487941
Walker KA et al. Fluazifop, a grass-selective herbicide which inhibits acetyl-CoA carboxylase in sensitive plant species. 1988 Biochem. J. pmid:2902848
Park EA et al. Insulin regulates enzyme activity, malonyl-CoA sensitivity and mRNA abundance of hepatic carnitine palmitoyltransferase-I. 1995 Biochem. J. pmid:7575418
Broadway NM and Saggerson ED Solubilization and separation of two distinct carnitine acyltransferases from hepatic microsomes: characterization of the malonyl-CoA-sensitive enzyme. 1995 Biochem. J. pmid:7575437
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
Drynan L et al. The role of changes in the sensitivity of hepatic mitochondrial overt carnitine palmitoyltransferase in determining the onset of the ketosis of starvation in the rat. 1996 Biochem. J. pmid:8836117
Fraser F et al. Topology of carnitine palmitoyltransferase I in the mitochondrial outer membrane. 1997 Biochem. J. pmid:9169604