A new subtilisin family: nucleotide and deduced amino acid sequences of new high-molecular-mass alkaline proteases from Bacillus spp
| Autor: | Tohru Kobayashi, Shuji Kawai, Yasushi Takimura, Akinori Ogawa, Mitsuyoshi Okuda, Nobuyuki Sumitomo, Katsuhisa Saeki, Susumu Ito |
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| Rok vydání: | 2004 |
| Předmět: |
DNA
Bacterial Proteases Hot Temperature medicine.medical_treatment Proteolysis Molecular Sequence Data Bacillus Microbiology Serine Open Reading Frames medicine Alkaliphile Amino Acid Sequence Subtilisins Cloning Molecular Phylogeny Serine protease Protease Base Sequence Sequence Homology Amino Acid medicine.diagnostic_test biology Serine Endopeptidases fungi Subtilisin General Medicine Hydrogen-Ion Concentration Molecular biology Recombinant Proteins Molecular Weight Kinetics Biochemistry Genes Bacterial Multigene Family biology.protein Molecular Medicine |
| Zdroj: | Extremophiles. 8:229-235 |
| ISSN: | 1433-4909 1431-0651 |
| DOI: | 10.1007/s00792-004-0381-8 |
| Popis: | Six genes encoding high-molecular-mass subtilisins (HMSs) of alkaliphilic Bacillus spp. were cloned and sequenced. Their open reading frames of 2,394-2,424 bp encoded prosubtilisins of 798-808 amino acids (aa) consisting of the prepropeptides of 151-158 aa and the mature enzymes of 640-656 aa. The deduced aa sequences of the mature enzymes exhibited 60-95% identity to those of FT protease of Bacillus sp. strain KSM-KP43, a subtilisin-like serine protease, and a minor serine protease, Vpr, of Bacillus strains. Three of the six recombinant enzymes were susceptible to proteolysis, but the others were autodigestion resistant. All enzymes had optimal pH values of 10.5-11.0, optimal temperatures of 40-45 degrees C for hydrolysis of a synthetic substrate, and were heat labile. These alkaline proteases seem to form a new subtilisin family, as judged by their aa sequences and phylogenetic analysis. |
| Databáze: | OpenAIRE |
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