Journal of Bacteriology · 1985 · 113 citations · 21 references
Life SciencesMicrobiologyMolecular BiologyEnzymologyMicrobial GeneticsProtein BiochemistryAmino Acid Sequence DeterminantsEnzyme CharacterizationEnzyme StructureProtein Sequence AnalysisThermostable EnzymesAmino Acid AnalysisAmino AcidsOpen Reading Frame IdentificationSignal Peptide AnalysisSignal Peptide MotifThermostable Amylases
The nucleotide sequence of the Bacillus stearothermophilus alpha-amylase gene and its flanking regions was determined. An open reading frame was found, comprising a total of 1,647 base pairs (549 amino acids) and starting from a GUG codon as methionine. It was shown by NH2-terminal amino acid sequence analysis that the extracellular amylase consisted of 515 amino acid residues, which corresponded to a molecular weight of 58,779. Thus the NH2-terminal portion of the gene encodes 34 amino acid residues as a signal peptide. The amino acid sequence deduced from the alpha-amylase gene was fairly homologous (61%) with that of another thermostable amylase from Bacillus amyloliquefaciens.
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Improved Estimation of Secondary Structure in Ribonucleic Acids
Ignacio Tinoco, Philip N. Borer, Barbara Dengler et al. · Nature New Biology · 1973 · 2.3K citations