Abstract
We have isolated and characterized the cDNA and the genomic DNA encoding Drosophila melanogaster pterin 4α-carbinolamine dehydratase (PCD). The amino acid sequence deduced from the cDNA sequence was very similar to those of PCDs previously reported in other species (19-57% identity). The protein coding region of the cDNA was expressed in E. coli as a histidine fusion protein, and the expressed protein proved to have PCD activity. The characterization of the Drosophila genomic clone revealed that the Drosophila PCD gene is interrupted by two introns. The potential promoter region, deduced from the determination of the transcription start point (tsp), lacks the distinct TATAAA box consensus sequence. Copyright (C) 1998 Elsevier Science B.V.
| Original language | English |
|---|---|
| Pages (from-to) | 273-278 |
| Number of pages | 6 |
| Journal | Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology |
| Volume | 1388 |
| Issue number | 1 |
| DOIs | |
| State | Published - 1998.10.14 |
Keywords
- Dimerization cofactor for HNF-1
- Drosophila melanogaster
- Gene characterization
- Pterin-4α-carbinolamine dehydratase
- Tetrahydrobiopterin
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