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
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
Carreras CW and Khosla C Purification and in vitro reconstitution of the essential protein components of an aromatic polyketide synthase. 1998 Biochemistry pmid:9518007
Martinez MA et al. A novel role of malonyl-ACP in lipid homeostasis. 2010 Biochemistry pmid:20201588
Reeves CD et al. Alteration of the substrate specificity of a modular polyketide synthase acyltransferase domain through site-specific mutations. 2001 Biochemistry pmid:11747421
Kerner J and Bieber L Isolation of a malonyl-CoA-sensitive CPT/beta-oxidation enzyme complex from heart mitochondria. 1990 Biochemistry pmid:2350540
Prigge ST et al. The initiating steps of a type II fatty acid synthase in Plasmodium falciparum are catalyzed by pfACP, pfMCAT, and pfKASIII. 2003 Biochemistry pmid:12549938
Liou GF et al. Quantitative analysis of loading and extender acyltransferases of modular polyketide synthases. 2003 Biochemistry pmid:12515555
Kumar S and Srinivasan KR Inactivation of chicken liver fatty acid synthetase by malonyl coenzyme A. Effects of acetyl coenzyme A and nicotinamide adenine dinucleotide phosphate. 1981 Biochemistry pmid:7260044
Srinivasan KR and Kumar S Kinetic analysis of the malonyl coenzyme A decarboxylation and the condensation reaction of fatty acid synthesis. Application to the study of malonyl coenzyme A inactivated chicken liver fatty acid synthetase. 1981 Biochemistry pmid:7260045
Mazur MT et al. Site-specific observation of acyl intermediate processing in thiotemplate biosynthesis by fourier transform mass spectrometry: the polyketide module of yersiniabactin synthetase. 2003 Biochemistry pmid:14621984
Spencer JB and Jordan PM Investigation of the mechanism and steric course of the reaction catalyzed by 6-methylsalicylic acid synthase from Penicillium patulum using (R)-[1-13C;2-2H]- and (S)-[1-13C;2-2H]malonates. 1992 Biochemistry pmid:1390697
Chung CH et al. Conferral of malonyl coenzyme A sensitivity to purified rat heart mitochondrial carnitine palmitoyltransferase. 1992 Biochemistry pmid:1390753
Dunn BJ et al. Comparative analysis of the substrate specificity of trans- versus cis-acyltransferases of assembly line polyketide synthases. 2014 Biochemistry pmid:24871074
Sleboda J et al. Short-term regulation of carnitine palmitoyltransferase I in cultured rat hepatocytes: spontaneous inactivation and reactivation by fatty acids. 1999 Biochim. Biophys. Acta pmid:9989283
Ghadiminejad I and Saggerson D A proportion of rat liver mitochondrial carnitine palmitoyltransferase can be made activatable by malonyl-CoA. 1991 Biochim. Biophys. Acta pmid:1911872
Ghadiminejad I and Saggerson D Cholate separates the catalytic and malonyl-CoA-binding components of carnitine palmitoyltransferase from liver outer mitochondrial membranes. 1991 Biochim. Biophys. Acta pmid:2036450
Fiol CJ et al. Effect of malonyl-CoA on the kinetics and substrate cooperativity of membrane-bound carnitine palmitoyltransferase of rat heart mitochondria. 1987 Biochim. Biophys. Acta pmid:3689805
Veerkamp JH and Van Moerkerk HT The effect of malonyl-CoA on fatty acid oxidation in rat muscle and liver mitochondria. 1982 Biochim. Biophys. Acta pmid:7066363
Kashfi K and Cook GA Temperature effects on malonyl-CoA inhibition of carnitine palmitoyltransferase I. 1995 Biochim. Biophys. Acta pmid:7619853
Kerner J and Hoppel C Fatty acid import into mitochondria. 2000 Biochim. Biophys. Acta pmid:10856709
Vandhana S et al. Biochemical changes accompanying apoptotic cell death in retinoblastoma cancer cells treated with lipogenic enzyme inhibitors. 2013 Biochim. Biophys. Acta pmid:23816424