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

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 dihyd...

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Veröffentlicht in:FEBS letters 2004-10, Vol.576 (1), p.63-67
Hauptverfasser: Omae, Fumio, Miyazaki, Masao, Enomoto, Ayako, Suzuki, Akemi
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Miyazaki, Masao
Enomoto, Ayako
Suzuki, Akemi
description 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.
doi_str_mv 10.1016/j.febslet.2004.08.060
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subjects Amino Acid Sequence
Animals
C-4 hydroxylase
Chlorocebus aethiops
Conserved Sequence
COS Cells
DES1
DES2
Hydrolases - chemistry
Hydrolases - genetics
Hydrolases - metabolism
Mice
Molecular Sequence Data
Multienzyme Complexes - chemistry
Multienzyme Complexes - genetics
Oxidoreductases - chemistry
Oxidoreductases - genetics
Oxidoreductases - metabolism
Phylogeny
Recombinant Proteins - chemistry
Recombinant Proteins - metabolism
Sequence Homology, Amino Acid
Δ 4 desaturase
Δ4 desaturase
title Identification of an essential sequence for dihydroceramide C-4 hydroxylase activity of mouse DES2
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