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Literature summary for 2.7.1.227 extracted from

  • Sato, K.; Noda, Y.; Yoda, K.
    Kei1 a novel subunit of inositolphosphorylceramide synthase, essential for its enzyme activity and Golgi localization (2009), Mol. Biol. Cell, 20, 4444-4457 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.1.227

Localization

Localization Comment Organism GeneOntology No. Textmining
Golgi apparatus Kei1 localizes to mid-Golgi and is cleaved by protease Kex2 Saccharomyces cerevisiae 5794
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Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae Q06346 and P36107 Q06346 i.e. regulatory subunit Kei1, P36107 i.e. catalytic subunit Aur1
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-alpha-phosphatidylinositol + C6-NBD-ceramide
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 Saccharomyces cerevisiae ?
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 ?

Synonyms

Synonyms Comment Organism
AUR1
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 Saccharomyces cerevisiae
KEI1
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 Saccharomyces cerevisiae

General Information

General Information Comment Organism
physiological function the growth defect of a temperature-sensitive mutant is effectively suppressed by the overexpression of Aur1, and Aur1 and Kei1 proteins form a complex in vivo. The temperature-sensitive mutant is hypersensitive to aureobasidin A, a specific inhibitor of IPC synthesis, and the IPC synthase activity in the mutant membranes is thermolabile. A part of Aur1 is missorted to the vacuole in Kei1 mutant cells. Aur1 without Kei1 has hardly detectable IPC synthase activity Saccharomyces cerevisiae