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Identification of an essential sequence for dihydroceramide C-4 hydroxylase activity of mouse DES2.

FEBS Lett.2004 Oct 8;576(1-2):63-7
Fumio Omae 1 , Masao Miyazaki , Ayako Enomoto , Akemi Suzuki
Fumio Omae 1 , Masao Miyazaki , Ayako Enomoto , Akemi Suzuki

[No authors listed]

Author information
  • 1 Sphingolipid Expression Laboratory, Frontier Research System, RIKEN, 2-1, Hirosawa, Wako-shi, Saitama 351-0198, Japan.

摘要


Although the amino acid sequences of mouse DES1 (MDES1) and DES2 (MDES2) have 63% sequence identity, their enzymatic characteristics are quite different. MDES1 exhibits high dihydroceramide delta4-desaturase activity and very low C-4 hydroxylase activity, while MDES2 is similarly active as both a dihydroceramide delta4-desaturase and a C-4 hydroxylase. We constructed several chimeras of MDES1 and MDES2 and identified a region important for C-4 hydroxylase activity in MDES2. This region contains the sequence XAFGY (X=T or A or V; Y=T or N) and occurs on the C-terminal side of the first His-box of MDES2. We confirmed the conservation of this region in DES2 family members sequenced from humans, pigs, rats, chickens, zebrafish, and Xenopus.

基因