1. Revision in sequence of CAD aspartate transcarbamylase domain of Drosophila.
- Author
-
Davidson JN and Kern CB
- Subjects
- Amino Acid Sequence, Animals, Aspartate Carbamoyltransferase genetics, Base Sequence, Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing) genetics, Dihydroorotase genetics, Drosophila melanogaster genetics, Molecular Sequence Data, Multienzyme Complexes genetics, Sequence Homology, Amino Acid, Sequence Homology, Nucleic Acid, Aspartate Carbamoyltransferase chemistry, Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing) chemistry, Dihydroorotase chemistry, Drosophila melanogaster enzymology, Multienzyme Complexes chemistry
- Abstract
The Drosophila CAD gene, also known as rudimentary, encodes a protein that carries out the first three enzymatic steps of de novo pyrimidine biosynthesis. The sequence for this gene, as previously published, appears to contain several errors. The correction of six bases in a 250 bp stretch encoding the aspartate transcarbamylase domain leads to changes of frame in two areas of the predicted amino acid sequence, consisting of lengths of 30 and 15 amino acid residues, respectively. The revised sequence shows significantly improved positional identity with both Syrian hamster and Escherichia coli aspartate transcarbamylases.
- Published
- 1994
- Full Text
- View/download PDF