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Descripción
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| C1A cysteine peptidases are synthesized as inactive proenzymes. Activation takes place by proteolysis cleaving off the inhibitory propeptide. The inhibitory capacity of propeptides from barley cathepsin L and B-like peptidases towards commercial and barley cathepsins has been characterized. Differences in selectivity have been found for propeptides from L-cathepsins against their cognate and non cognate enzymes. Besides, the propeptide from barley cathepsin B was not able to inhibit bovine cathepsin B. Modelling of their three-dimensional structures suggests that most propeptide inhibitory properties can be explained from the interaction between the propeptide and the mature cathepsin structures. Their potential use as biotechnological tools is discussed. | |
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Internacional
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Si |
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JCR del ISI
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Si |
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Título de la revista
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Plos One |
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ISSN
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1932-6203 |
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Factor de impacto JCR
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4,411 |
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Información de impacto
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Datos JCR del año 2010 |
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Volumen
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5 |
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DOI
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10.1371/journal.pone.0037234 |
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Número de revista
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Desde la página
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37234 |
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Hasta la página
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37240 |
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Mes
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SIN MES |
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Ranking
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