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Identification of an essential sequence for dihydroceramide C‐4 hydroxylase activity of mouse DES2
Author(s) -
Omae Fumio,
Miyazaki Masao,
Enomoto Ayako,
Suzuki Akemi
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.08.060
Subject(s) - zebrafish , biology , enzyme , xenopus , peptide sequence , tyrosine hydroxylase , biochemistry , gene
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 Δ 4 ‐desaturase activity and very low C‐4 hydroxylase activity, while MDES2 is similarly active as both a dihydroceramide Δ 4 ‐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 .