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- W1971715251 abstract "The gene (nprV), encoding the extracellular neutral protease, vibrilysin (NprV), of the Gram− marine microorganism, Vibrio proteolyticus, was isolated from a V. proteolyticus DNA library constructed in Escherichia coli. The recombinant E. coli produced a protease that co-migrated with purified neutral protease from V. proteolyticus on non-denaturing polyacrylamide gels, and that demonstrated enzymatic specificity towards the neutral protease substrate N-[3-(2-furyl acryloyl]-l-alanyl- phenylalanine amide. The nucleotide (nt) sequence of the cloned nprV gene revealed an open reading frame encoding 609 amino acids (aa) including a putative signal peptide sequence followed by a long ‘pro’ sequence consisting of 172 aa. The N-terminal aa sequence of NprV purified fom cultures of V. proteolyticus, identified the beginning of the mature protein within the aa sequence deduced from the nt sequence. Comparative analysis of mature NprV to the sequences of the neutral proteases from Bacillus thermoproteolyticus (thermolysin) and Bacillus stearothermophilus identified extensive regions of conserved aa homology, particularly with respect to active-site residues, zinc-binding residues, and calcium-binding sites. NprV was overproduced in Bacillus subtilis by placing the DNA encoding the ‘pro’ and mature enzyme downstream from a Bacillus promoter and signal sequence." @default.
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- W1971715251 date "1992-03-01" @default.
- W1971715251 modified "2023-10-17" @default.
- W1971715251 title "Cloning, sequencing and expression of the gene encoding the extracellular neutral protease, vibriolysin, of Vibrio proteolyticus" @default.
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- W1971715251 doi "https://doi.org/10.1016/0378-1119(92)90310-l" @default.
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