| Autor: |
Aoyama, Misako, Toma, Claudia, Yasuda, Masaaki, Iwanaga, Masaaki |
| Zdroj: |
Microbiology and Immunology; May 2000, Vol. 44 Issue: 5 p389-393, 5p |
| Abstrakt: |
The complete nucleotide sequence of the gene encoding an alkaline serine proteinase (aprP) of Bacillus pumilusTYO‐67 was determined. The sequence analysis showed an open reading frame of 1,149 bp (383 amino acids) that encoded a signal peptide consisting of 29 residues and a propeptide of 79 residues. The deduced 3 amino acid residues, D32, H64, and S221, were identical with 3 essential amino acids in the catalytic center of subtilases. The sequence around these residues revealed that APRP was a new member of the true subtilisin subgroup of the subtilisin family. The highest homology was found in subtilisin NAT at 64.4% in the DNA sequence. The residue S189of APRP was different from those of other subtilases. |
| Databáze: |
Supplemental Index |
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