Article
Gabaculine-resistant glutamate 1-semialdehyde aminotransferase of Synechococcus. Deletion of a tripeptide close to the NH2 terminus and internal amino acid substitution.
The Journal of biological chemistry - 5 Jul 1991
Grimm B, Smith A J, Kannangara C G, Smith M
Abstract excerpt
Glutamate 1-semialdehyde aminotransferase (GSA-AT) is the last enzyme in the C5 pathway converting glutamate into the tetrapyrrole precursor delta-aminolevulinate in plants, algae, and several bacteria. Sequence analysis of the genes encoding GSA-AT in barley, Synechococcus, and Escherichia coli revealed 50-70% similarity in the primary structures of the proteins. The enzyme is inhibited rapidly by gabaculine...
Topics
- Amino Acids
- Base Sequence
- Chromatography, DEAE-Cellulose
- Cyanobacteria
- Cyclohexanecarboxylic Acids
- DNA, Bacterial
- Drug Resistance, Microbial
- Electrophoresis, Polyacrylamide Gel
- Genes, Bacterial
- Genetic Vectors