Abstract
The nucleotide sequence is reported of a cDNA clone encoding a Caenorhabditis elegans homolog of guinea pig and human alkyl-dihydroxyacetonephosphate synthase. The open reading frame encodes a protein of 597 amino acids which shows extensive homology with the mammalian enzymes (52% identical and about 76% similar in the overlapping region). In contrast to the mammalian enzymes, which carry a consensus peroxisomal targeting signal type 2 in a cleavable N-terminal presequence, this Caenorhabditis elegans homolog carries a consensus peroxisomal targeting signal type 1 (CKL) at its C-terminus. Expression of this protein in an in vitro transcription/translation system yielded a 65 kDa protein. Recombinant aenorhabditis elegans alkyl-DHAP synthase expressed in the yeast Pichia pastoris was enzymatically active.
| Original language | English |
|---|---|
| Pages (from-to) | 277-81 |
| Number of pages | 5 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 242 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 14 Jan 1998 |
Keywords
- Alkyl and Aryl Transferases
- Amino Acid Sequence
- Animals
- Base Sequence
- Caenorhabditis elegans
- Cloning, Molecular
- Electrophoresis, Polyacrylamide Gel
- Gene Expression Regulation, Fungal
- Helminth Proteins
- Microbodies
- Molecular Sequence Data
- Pichia
- Protein Biosynthesis
- Protein Sorting Signals
- Recombinant Proteins
- Sequence Alignment
- Sequence Analysis, DNA
- Transcription, Genetic
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