Identification of an essential sequence for dihydroceramide C-4 hydroxylase activity of mouse DES2
| Autor: | Akemi Suzuki, Fumio Omae, Masao Miyazaki, Ayako Enomoto |
|---|---|
| Rok vydání: | 2004 |
| Předmět: |
Δ4 desaturase
Hydrolases Molecular Sequence Data Biophysics Xenopus Biochemistry Mice Structural Biology Multienzyme Complexes Chlorocebus aethiops Genetics Animals C-4 hydroxylase Amino Acid Sequence Molecular Biology Zebrafish Conserved Sequence Phylogeny Sequence (medicine) chemistry.chemical_classification biology Sequence Homology Amino Acid Cell Biology biology.organism_classification Sequence identity Recombinant Proteins Amino acid Enzyme chemistry COS Cells DES2 DES1 Oxidoreductases |
| Zdroj: | FEBS letters. 576(1-2) |
| ISSN: | 0014-5793 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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