L-aspartate ammonia-lyase and fumarate hydratase share extensive sequence homology.
Based on our recent determinations of the nucleotide sequences of the L-aspartate ammonia-lyase genes from Escherichia coli and Pseudomonas fluorescens, primary structures of the two L-aspartate ammonia-lyases and fumarate hydratases from Bacillus subtilis and E. coli (N-terminal partial sequence) were compared by computer analysis. These four enzymes exhibited a significant homology of at least 37%, implying that L-aspartate ammonia-lyase and fumarate hydratase share a common evolutionary origin. To authors' knowledge, this feature appears to be the first example showing that two kinds of enzymes catalyzing different types of reactions, albeit similar, share such a high degree of sequence homology.
D000595:Amino Acid Sequence; D000642:Ammonia-Lyases / Q000235:genetics*; D001220:Aspartate Ammonia-Lyase / Q000235:genetics*; D001412:Bacillus subtilis / Q000201:enzymology / Q000235:genetics*; D001483:Base Sequence; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics*; D005649:Fumarate Hydratase / Q000235:genetics*; D005796:Genes; D005798:Genes, Bacterial; D011551:Pseudomonas fluorescens / Q000201:enzymology / Q000235:genetics*; D012689:Sequence Homology, Nucleic Acid; D013045:Species Specificity
D005649:Fumarate Hydratase; D000642:Ammonia-Lyases; D001220:Aspartate Ammonia-Lyase