Computational studies on a new cationic peroxidase isoenzyme from artichoke leaves.
Bioeng Bugs
; 3(1): 60-6, 2012 Jan 01.
Article
em En
| MEDLINE
| ID: mdl-22179146
ABSTRACT
Previously we presented the purification, biochemical characterization, and cloning of a cationic peroxidase isoenzyme (CysPrx) from artichoke (Cynara cardunculus subsp scolymus (L.) Hegi) leaves. The protein was shown to have some interesting properties, suggesting that CysPrx could be a considered as a potential candidate for industrial application. In addition, from the CysPrx sequence, two full-lengh cDNAs CysPrx1 and CysPrx2, differing for three amino acids, were isolated. A three-dimensional model was predicted from CysPrx1 by homology modeling, using two different computational tools. Herein we discuss the roles of particular amino acid residues and structural motifs or regions of both deduced sequences with the aim to find new understandings between the new plant peroxidase isoenzymes and their physiological substrates. Additionally, the obtained information may lead to new methods for improving the stability of the enzyme in several processes of biotechnological interest for peroxidase applications.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Peroxidases
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Folhas de Planta
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Biologia Computacional
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Cynara scolymus
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Isoenzimas
Idioma:
En
Ano de publicação:
2012
Tipo de documento:
Article