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Gene Review

YPC1  -  phytoceramidase

Saccharomyces cerevisiae S288c

Synonyms: Alkaline ceramidase YPC1, YBR1305, YBR183W
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Disease relevance of YPC1


High impact information on YPC1

  • Here, we describe the generation of a conditional S. cerevisiae mutant (named YPC-1) whose functional IPP1 gene is under the control of a galactose-dependent promoter [2].
  • Thus, YPC-1 cells become growth arrested in glucose but they regain the ability to grow on this carbon source when transformed with autonomous plasmids bearing diverse foreign H+-PPase genes under the control of a yeast constitutive promoter [2].
  • In this study, we report the cloning and characterization of a novel mouse alkaline ceramidase (maCER1) with a highly restricted substrate specificity. maCER1 consists of 287 amino acids, and it has a 28 and 32% identity to the Saccharomyces alkaline ceramidases (YPC1p and YDC1p) and the human alkaline phytoceramidase, respectively [3].
  • In a previous study, we reported that the Saccharomyces cerevisiae gene YPC1 encodes an alkaline ceramidase with a dual activity, catalyzing both hydrolysis and synthesis of yeast ceramide (Mao, C., Xu, R., Bielawska, A., and Obeid, L. M. (2000) J. Biol. Chem. 275, 6876-6884) [4].
  • This ceramide synthase activity is CoA-independent and is resistant to fumonisin B1, thus explaining why YPC1 was cloned as a fumonisin B1-resistant gene [1].

Biological context of YPC1

  • Multiple copies of YPC1 were much more efficient than YDC1 in rescuing cell growth [5].
  • We show that these two ceramidases have different substrate specificity, such that YPC1p preferentially hydrolyzes phytoceramide, whereas the new ceramidase YDC1p hydrolyzes dihydroceramide preferentially and phytoceramide only slightly [4].

Associations of YPC1 with chemical compounds


Other interactions of YPC1

  • Neither deletion of LAC1 nor overexpression of YPC1 had a detectable effect on wild-type life span [5].


  1. Cloning of an alkaline ceramidase from Saccharomyces cerevisiae. An enzyme with reverse (CoA-independent) ceramide synthase activity. Mao, C., Xu, R., Bielawska, A., Obeid, L.M. J. Biol. Chem. (2000) [Pubmed]
  2. Functional complementation of yeast cytosolic pyrophosphatase by bacterial and plant H+-translocating pyrophosphatases. Perez-Castineira, J.R., Lopez-Marques, R.L., Villalba, J.M., Losada, M., Serrano, A. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  3. Cloning and characterization of a mouse endoplasmic reticulum alkaline ceramidase: an enzyme that preferentially regulates metabolism of very long chain ceramides. Mao, C., Xu, R., Szulc, Z.M., Bielawski, J., Becker, K.P., Bielawska, A., Galadari, S.H., Hu, W., Obeid, L.M. J. Biol. Chem. (2003) [Pubmed]
  4. Cloning and characterization of a Saccharomyces cerevisiae alkaline ceramidase with specificity for dihydroceramide. Mao, C., Xu, R., Bielawska, A., Szulc, Z.M., Obeid, L.M. J. Biol. Chem. (2000) [Pubmed]
  5. Suppressor analysis points to the subtle role of the LAG1 ceramide synthase gene in determining yeast longevity. Jiang, J.C., Kirchman, P.A., Allen, M., Jazwinski, S.M. Exp. Gerontol. (2004) [Pubmed]
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