Nucleotide and Deduced Amino Acid Sequences of a New Subtilisin from an Alkaliphilic Bacillus Isolate
Autor: | Susumu Ito, Tohru Kobayashi, Marietta V. Magallones, Shuji Kawai, Katsuhisa Saeki, Yasushi Takimura, Yuji Hatada |
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Rok vydání: | 2003 |
Předmět: |
DNA
Bacterial Sequence analysis Molecular Sequence Data Bacillus Sequence alignment Protein Sorting Signals Applied Microbiology and Biotechnology Microbiology Open Reading Frames Surface-Active Agents Bacterial Proteins Catalytic Domain Enzyme Stability Catalytic triad Amino Acid Sequence Promoter Regions Genetic Peptide sequence Phylogeny chemistry.chemical_classification Sequence Homology Amino Acid biology Serine Endopeptidases fungi Subtilisin Temperature Hydrogen Peroxide Sequence Analysis DNA General Medicine Hydrogen-Ion Concentration biology.organism_classification Amino acid Alkanesulfonic Acids Biochemistry chemistry Sequence Alignment Subtilisins |
Zdroj: | Current Microbiology. 47:337-340 |
ISSN: | 1432-0991 0343-8651 |
DOI: | 10.1007/s00284-002-4018-9 |
Popis: | The gene for a new subtilisin from the alkaliphilic Bacillus sp. KSM-LD1 was cloned and sequenced. The open reading frame of the gene encoded a 97 amino-acid prepro-peptide plus a 307 amino-acid mature enzyme that contained a possible catalytic triad of residues, Asp32, His66, and Ser224. The deduced amino acid sequence of the mature enzyme (LD1) showed approximately 65% identity to those of subtilisins SprC and SprD from alkaliphilic Bacillus sp. LG12. The amino acid sequence identities of LD1 to those of previously reported true subtilisins and high-alkaline proteases were below 60%. LD1 was characteristically stable during incubation with surfactants and chemical oxidants. Interestingly, an oxidizable Met residue is located next to the catalytic Ser224 of the enzyme as in the cases of the oxidation-susceptible subtilisins reported to date. |
Databáze: | OpenAIRE |
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