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• W1538879287 endingPage "760" @default.
• W1538879287 startingPage "752" @default.
• W1538879287 abstract "An extracellular serine proteinase purified from cultures of a psychrotrophic Vibrio species (strain PA-44) belongs to the proteinase K family of the superfamily of subtilisin-like proteinases. The enzyme is secreted as a 47-kDa protein, but under mild heat treatment (30 min at 40 °C) undergoes autoproteolytic cleavage on the carboxyl-side of the molecule to give a proteinase with a molecular mass of about 36 kDa that apparently shares most of the enzymatic characteristics and the stability of the 47-kDa protein. In this study, selected enzymatic properties of the Vibrio proteinase were compared with those of the related proteinases, proteinase K and aqualysin I, as representative mesophilic and thermophilic enzymes, respectively. The catalytic efficiency (kcat/Km) for the amidase activity of the cold-adapted enzyme against succinyl-AAPF-p-nitroanilide was significantly higher than that of its mesophilic and thermophilic counterparts, especially when compared with aqualysin I. The stability of the Vibrio proteinase, both towards heat and denaturants, was found to be significantly lower than of either proteinase K or aqualysin I. One or more disulfide bonds in the psychrotrophic proteinase are important for the integrity of the active enzyme structure, as disulfide cleavage, either by reduction with dithiothreitol or by sulfitolysis, led to a loss in its activity. Under the same conditions, aqualysin I was also partially inactivated by dithiothreitol, but the activity of proteinase K was unaffected. The disulfides of either proteinase K or aqualysin I were not reactive towards sulfitolysis, except under denaturing conditions, while all disulfides of the Vibrio proteinase reacted in absence of a denaturant. The reactivity of the disulfides of the proteins as a function of denaturant concentration followed the order: Vibrio proteinase > proteinase K > aqualysin I. The same order of reactivity was also observed for the inactivation of the enzymes by H2O2-oxidation, as a function of temperature. The order of reactivity observed in these reactions most likely reflects the accessibility of the reactive cystine or methionine side chains present in the three related proteinases, and hence a difference in the compactness of their protein structures." @default.
• W1538879287 created "2016-06-24" @default.
• W1538879287 creator A5014400762 @default.
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• W1538879287 creator A5053659969 @default.
• W1538879287 creator A5085464733 @default.
• W1538879287 creator A5090867811 @default.
• W1538879287 date "1999-03-05" @default.
• W1538879287 modified "2023-10-16" @default.
• W1538879287 title "Properties of a subtilisin-like proteinase from a psychrotrophic Vibrio species . Comparison with proteinase K and aqualysin I" @default.
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• W1538879287 cites W1500041659 @default.
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• W1538879287 cites W1551969996 @default.
• W1538879287 cites W1590376353 @default.
• W1538879287 cites W1619383772 @default.
• W1538879287 cites W1800889405 @default.
• W1538879287 cites W1869944834 @default.
• W1538879287 cites W1883093314 @default.
• W1538879287 cites W19018813 @default.
• W1538879287 cites W1964461863 @default.
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• W1538879287 cites W1968728042 @default.
• W1538879287 cites W1976118295 @default.
• W1538879287 cites W1982935962 @default.
• W1538879287 cites W1988098327 @default.
• W1538879287 cites W1988252316 @default.
• W1538879287 cites W1992241700 @default.
• W1538879287 cites W1997438353 @default.
• W1538879287 cites W2001367486 @default.
• W1538879287 cites W2002320749 @default.
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• W1538879287 cites W2023069584 @default.
• W1538879287 cites W2027539160 @default.
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• W1538879287 cites W2034756360 @default.
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• W1538879287 cites W2048610030 @default.
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• W1538879287 cites W2048908230 @default.
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• W1538879287 cites W2063894299 @default.
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• W1538879287 cites W2067133968 @default.
• W1538879287 cites W2068475565 @default.
• W1538879287 cites W2069695110 @default.
• W1538879287 cites W2070606233 @default.
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• W1538879287 cites W2089456529 @default.
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• W1538879287 cites W2093969953 @default.
• W1538879287 cites W2097086424 @default.
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• W1538879287 cites W2100837269 @default.
• W1538879287 cites W2118558198 @default.
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• W1538879287 cites W2171610577 @default.
• W1538879287 cites W349417349 @default.
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• W1538879287 cites W4249418134 @default.
• W1538879287 cites W4255525341 @default.
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• W1538879287 doi "https://doi.org/10.1046/j.1432-1327.1999.00205.x" @default.
• W1538879287 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/10103004" @default.
• W1538879287 hasPublicationYear "1999" @default.
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