Abstract：
:Ceramidase plays an important role in regulating the metabolism of sphingolipids, such as ceramide, sphingosine (SPH), and sphingosine-1-phosphate (S1P), by controlling the hydrolysis of ceramide. Here we report the cloning and biochemical characterization of a neutral ceramidase from the red flour beetle Tribolium castaneum which is an important storage pest. The Tribolium castaneum neutral ceramidase (Tncer) is a protein of 696 amino acids. It shares a high degree of similarity in protein sequence to neutral ceramidases from various species. Tncer mRNA levels are higher in the adult stage than in pre-adult stages, and they are higher in the reproductive organs than in head, thorax, and midgut. The mature ovary has higher mRNA levels than the immature ovary. Tncer is localized to the plasma membrane. It uses various ceramides (D-erythro-C(6), C(12), C(16), C(18:1), and C(24:1)-ceramide) as substrates and has an abroad pH optimum for its in vitro activity. Tncer has an optimal temperature of 37 °C for its in vitro activity. Its activity is inhibited by Fe(2+). These results suggest that Tncer has distinct biochemical properties from neutral ceramidases from other species.
journal_name
Biochimiejournal_title
Biochimieauthors
Zhou Y,Lin XW,Yang Q,Zhang YR,Yuan JQ,Lin XD,Xu R,Cheng J,Mao C,Zhu ZRdoi
10.1016/j.biochi.2011.03.009subject
Has Abstractpub_date
2011-07-01 00:00:00pages
1124-31issue
7eissn
0300-9084issn
1638-6183pii
S0300-9084(11)00099-Xjournal_volume
93pub_type
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