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Literature summary for 2.3.1.24 extracted from

  • Megyeri, M.; Prasad, R.; Volpert, G.; Sliwa-Gonzalez, A.; Haribowo, A.; Aguilera-Romero, A.; Riezman, H.; Barral, Y.; Futerman, A.; Schuldiner, M.
    Yeast ceramide synthases, Lag1 and Lac1, have distinct substrate specificity (2019), J. Cell Sci., 132, jcs228411 .
    View publication on PubMedView publication on EuropePMC
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Localization

Localization Comment Organism GeneOntology No. Textmining
nucleus Lag1 is uniquely required for the establishment of a lateral diffusion barrier in the nuclear envelope, which depends on phytoceramide Saccharomyces cerevisiae 5634
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Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
a fatty acyl-CoA + phytosphingosine
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 Saccharomyces cerevisiae CoA + an N-acylphytosphingosine
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 ?
fatty acyl-CoA + dihydrosphingosine
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 Saccharomyces cerevisiae CoA + an N-acyldihydrosphingosine
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 ?
additional information Lag1 preferentially synthesizes phytosphingolipids Saccharomyces cerevisiae ?
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Synonyms

Synonyms Comment Organism
LAC1
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 Saccharomyces cerevisiae
LAG1
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 Saccharomyces cerevisiae

General Information

General Information Comment Organism
physiological function a Lag1 deletion mutant does not have a reduction in total sphingolipid levels. Additional deletion of C4 hydroxylase Sur2 causes a reduction in levels of all phytosphingolipids Saccharomyces cerevisiae
physiological function a Lag1 deletion mutant does not have a reduction in total sphingolipid levels. Additional deletion of C4 hydroxylase Sur2 causes a reduction in levels of all phytosphingolipids, and de novo synthesis of sphingolipids is disrupted in Lac1/Sur2 deletion strains. Loss of Lac1 but not Lag1 affects strain resistance to increased temperature Saccharomyces cerevisiae