First Author | Omae F | Year | 2004 |
Journal | FEBS Lett | Volume | 576 |
Issue | 1-2 | Pages | 63-7 |
PubMed ID | 15474011 | Mgi Jnum | J:93293 |
Mgi Id | MGI:3056825 | Doi | 10.1016/j.febslet.2004.08.060 |
Citation | Omae F, et al. (2004) Identification of an essential sequence for dihydroceramide C-4 hydroxylase activity of mouse DES2. FEBS Lett 576(1-2):63-7 |
abstractText | 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. |