title: Characterization of a neutral ceramidase orthologue from Aspergillus oryzae.
abstract: Ceramide is an important molecule not only structurally but also regulationally as a modulator of various cellular events. Ceramidase (CDase) are classified into three different types (acid, alkaline, and neutral CDases). Neutral CDase could play an important role in the regulation of ceramide levels in the extracellular space. In this study, we describe the characterization of a neutral CDase orthologue from the filamentous fungus Aspergillus oryzae. The gene encoding the neutral CDase orthologue was cloned and overexpressed in A. oryzae. The purified recombinant enzyme was optimally active at pH 4.0-4.5 and 40 degrees C. The apparent K(m) and V(max) values of the enzyme for C12-NBD-ceramide were 3.32 microM and 0.085 micromol min(-1) mg(-1), respectively.
authors: National Food Research Institute, Tsukuba, Ibaraki, Japan.
authors: Sawaki
authors: S
authors: Tada
authors: Mayumi
authors: M
authors: Matsushita-Morita
authors: Satoshi
authors: S
authors: Suzuki
authors: Ken-Ichi
authors: K
authors: Kusumoto
authors: Yutaka
authors: Y
authors: Kashiwagi
mesh_terms: D000595:Amino Acid Sequence; D001236:Aspergillus oryzae / Q000201:enzymology* / Q000235:genetics; D002518:Ceramides / Q000378:metabolism; D003001:Cloning, Molecular; D004795:Enzyme Stability; D015870:Gene Expression; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008969:Molecular Sequence Data; D055576:Neutral Ceramidase / Q000235:genetics* / Q000378:metabolism*; D011994:Recombinant Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D016415:Sequence Alignment; D013696:Temperature
chemical_list: D002518:Ceramides; D011994:Recombinant Proteins; D055576:Neutral Ceramidase