Increase of the Protease Activity of Aqualysin
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چکیده
subtilisins and proteinase K.]) Many protein cngincering studjes on subtilisins6) show that amino acid substitution can change the substrate specificity, pH depencience. thermostability, and eatalytie activity. Subtilisin BPN' mutant N218S (Asn218 is rcplaced by serine) has more thermostability than the wild-type cnzyme;7) Asn218 is threc rcsidues fi'om one of the catalytic residues. Ser221. The X-ray
منابع مشابه
Involvement of NH2-terminal pro-sequence in the production of active aqualysin I (a thermophilic serine protease) in Escherichia coli.
Aqualysin I is a heat-stable subtilisin-type protease produced by Thermus aquaticus YT-1. The precursor of aqualysin I consists of four domains: an NH2-terminal signal peptide, an NH2-terminal pro-sequence, a protease domain, and a COOH-terminal pro-sequence. In Escherichia coli cells harboring recombinant plasmid carrying the aqualysin I gene, proteolytic activity is obtained on treatment at 6...
متن کاملUnique precursor structure of an extracellular protease, aqualysin I, with NH2- and COOH-terminal pro-sequences and its processing in Escherichia coli.
Aqualysin I is a subtilisin-type serine protease which is secreted into the culture medium by Thermus aquaticus YT-1, an extremely thermophilic Gram-negative bacterium. The nucleotide sequence of the entire gene for aqualysin I was determined, and the deduced amino acid sequence suggests that aqualysin I is produced as a large precursor, consisting of at least three portions, an NH2-terminal pr...
متن کاملSubstrate Specificity of Aqualysin I, a Bacterial Thermophilic Alkaline Serine Protease from Thermus aquaticus YT-1: Comparison with Proteinase K, Subtilisin BPN' and Subtilisin Carlsberg.
Aqualysin I is the alkaline serine protease isolated from an extreme thermophile, Thermus aquaticus YT-1. We analyzed kinetic properties of aqualysin I, using sixteen kinds of chromogenic succinyl-tripeptide p-nitroanilides as substrates. And we compared the substrate specificity of aqualysin I with those of proteinase K, subtilisin BPN', and subtilisin Carlsberg. We found that aqualysin I had ...
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Aqualysin I is the alkaline serine protease isolated from an extreme thermophile, Thermus aquaticus YT-1. We have analyzed the kinetic properties of aqualysin I, using thirty-one kinds of chromogenic succinyl-tripeptide p-nitroanilides as substrates in the presence of 10% dimethylsulfoxide (DMSO). Aqualysin I hydrolyzed many peptides in a DMSO-containing mixture, however the substrate specifici...
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The effect of different thiourea (TU) concentrations (10 and 20 mM) on antioxidants, protease activity and protein content with and without H2O2 (50 mM) induced stress was investigated in wheat leaves. A gradual decrease in protein content with a peak at 72 hours was observed in stressed as well as control leaves. This gradual decrease in leaf protein content at different time intervals was com...
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