3-Ketosphinganine

3-Ketosphinganine is a lipid of Sphingolipids (SP) class. The involved functions are known as Anabolism and establishment and maintenance of localization. 3-ketosphinganine often locates in Membrane and membrane raft.

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Introduction

To understand associated biological information of 3-Ketosphinganine, 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 3-Ketosphinganine?

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

No disease MeSH terms mapped to the current reference collection.

PubChem Associated disorders and diseases

What pathways are associated with 3-Ketosphinganine

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 3-Ketosphinganine?

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What functions are associated with 3-Ketosphinganine?


Related references are published most in these journals:

Function Cross reference Weighted score Related literatures

What lipids are associated with 3-Ketosphinganine?

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

What genes are associated with 3-Ketosphinganine?

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

What common seen animal models are associated with 3-Ketosphinganine?

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

NCBI Entrez Crosslinks

All references with 3-Ketosphinganine

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Authors Title Published Journal PubMed Link
pmid:
Dickson RC et al. Serine palmitoyltransferase. 2000 Meth. Enzymol. pmid:10563304
Gable K et al. Tsc3p is an 80-amino acid protein associated with serine palmitoyltransferase and required for optimal enzyme activity. 2000 J. Biol. Chem. pmid:10713067
Hanada K et al. Purification of the serine palmitoyltransferase complex responsible for sphingoid base synthesis by using affinity peptide chromatography techniques. 2000 J. Biol. Chem. pmid:10722674
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Fornarotto M et al. Sphingolipid biosynthesis in pathogenic fungi: identification and characterization of the 3-ketosphinganine reductase activity of Candida albicans and Aspergillus fumigatus. 2006 Biochim. Biophys. Acta pmid:16431155
Ikushiro H et al. Molecular characterization of membrane-associated soluble serine palmitoyltransferases from Sphingobacterium multivorum and Bdellovibrio stolpii. 2007 J. Bacteriol. pmid:17557831
Pruett ST et al. Biodiversity of sphingoid bases ("sphingosines") and related amino alcohols. 2008 J. Lipid Res. pmid:18499644
Gupta SD et al. Tsc10p and FVT1: topologically distinct short-chain reductases required for long-chain base synthesis in yeast and mammals. 2009 J. Lipid Res. pmid:19141869
Song WQ et al. Characterization of two cotton cDNAs encoding trans-2-enoyl-CoA reductase reveals a putative novel NADPH-binding motif. 2009 J. Exp. Bot. pmid:19286916
Ikushiro H et al. Structural insights into the enzymatic mechanism of serine palmitoyltransferase from Sphingobacterium multivorum. 2009 J. Biochem. pmid:19564159
Seamen E et al. P-type ATPase TAT-2 negatively regulates monomethyl branched-chain fatty acid mediated function in post-embryonic growth and development in C. elegans. 2009 PLoS Genet. pmid:19662161