Identification of an essential sequence for dihydroceramide C‐4 hydroxylase activity of mouse DES2
F Omae, M Miyazaki, A Enomoto, A Suzuki - FEBS letters, 2004 - Wiley Online Library
F Omae, M Miyazaki, A Enomoto, A Suzuki
FEBS letters, 2004•Wiley Online LibraryAlthough 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 Δ4‐desaturase activity and very low C‐4 hydroxylase activity, while
MDES2 is similarly active as both a dihydroceramide Δ4‐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 …
63% sequence identity, their enzymatic characteristics are quite different. MDES1 exhibits
high dihydroceramide Δ4‐desaturase activity and very low C‐4 hydroxylase activity, while
MDES2 is similarly active as both a dihydroceramide Δ4‐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 …
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 Δ4‐desaturase activity and very low C‐4 hydroxylase activity, while MDES2 is similarly active as both a dihydroceramide Δ4‐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.
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