Abstract
Polyribonucleotide phosphorilase from the psychrophilic Antarctic eubacterium Pseudoalteromonas haloplanktis (PhPNPase) has been purified. This enzyme catalyzes both the RNA polymerisation and degradation reaction, showing the highest activity at temperatures below 40°C. PhPNPase is quite sensitive to heat treatment and it is endowed with remarkable halotolerance.
Keywords: RNA metabolism, cold adapted enzymes, activity-stability relationship
Protein & Peptide Letters
Title: Molecular and Functional Characterization of Polynucleotide Phosphorylase from the Antarctic Eubacterium Pseudoalteromonas haloplanktis
Volume: 16 Issue: 9
Author(s): G. Evangelista, P. Falasca, I. Ruggiero, M. Masullo and G. Raimo
Affiliation:
Keywords: RNA metabolism, cold adapted enzymes, activity-stability relationship
Abstract: Polyribonucleotide phosphorilase from the psychrophilic Antarctic eubacterium Pseudoalteromonas haloplanktis (PhPNPase) has been purified. This enzyme catalyzes both the RNA polymerisation and degradation reaction, showing the highest activity at temperatures below 40°C. PhPNPase is quite sensitive to heat treatment and it is endowed with remarkable halotolerance.
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Cite this article as:
Evangelista G., Falasca P., Ruggiero I., Masullo M. and Raimo G., Molecular and Functional Characterization of Polynucleotide Phosphorylase from the Antarctic Eubacterium Pseudoalteromonas haloplanktis, Protein & Peptide Letters 2009; 16 (9) . https://dx.doi.org/10.2174/092986609789055296
DOI https://dx.doi.org/10.2174/092986609789055296 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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