Year: 2000
Type: article
Abstract: The complete nucleotide sequence of the gene encoding an alkaline serine proteinase (aprP) of Bacillus pumilus TYO-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 S189 of APRP was different from those of other subtilases.
Source: Microbiology and Immunology
Institution: University of the Ryukyus
Language: English
Subfield: Biotechnology
Domain: Life Sciences
Open Access status: bronze
OpenAlex ID: W1963993018