Molecular cloning, characterization, and nucleotide sequence of an extracellular amylase gene from Aeromonas hydrophila.
The structural gene for excreted amylase from Aeromonas hydrophila JMP636 has been cloned within a 2.1-kilobase SmaI fragment of DNA. The amylase gene is transcribed from its own promoter in Escherichia coli, producing a gene product of Mr 49,000. The amylase gene product is secreted to the periplasm of E. coli; however, it is not excreted. Nucleotide sequencing revealed an open reading frame of 1,392 base pairs corresponding to a protein of 464 amino acid residues. A potential signal peptide of 21 amino acid residues is present at the NH2 terminal of the predicted protein. Three regions of homology with other procaryotic and eucaryotic alpha-amylases were detected within the predicted amino acid sequence.
D000333:Aeromonas / Q000201:enzymology / Q000235:genetics*; D000595:Amino Acid Sequence; D000681:Amylases / Q000235:genetics*; D001483:Base Sequence; D002872:Chromosome Deletion; D003001:Cloning, Molecular; D003062:Codon; D004252:DNA Mutational Analysis; D004262:DNA Restriction Enzymes; D004926:Escherichia coli / Q000235:genetics; D005110:Extracellular Space / Q000201:enzymology; D005786:Gene Expression Regulation; D005798:Genes, Bacterial; D008969:Molecular Sequence Data; D021382:Protein Sorting Signals
D003062:Codon; D021382:Protein Sorting Signals; D004262:DNA Restriction Enzymes; D000681:Amylases