Molecular and functional characterization of polynucleotide phosphorylase from the antarctic eubacterium Pseudoalteromonas haloplanktis

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 degrees C. PhPNPase is quite se...

Full description

Saved in:
Bibliographic Details
Published inProtein and peptide letters Vol. 16; no. 9; p. 999
Main Authors Evangelista, G, Falasca, P, Ruggiero, I, Masullo, M, Raimo, G
Format Journal Article
LanguageEnglish
Published Netherlands 01.09.2009
Subjects
Amino Acid Sequence
Enzyme Stability
Molecular Sequence Data
Molecular Weight
Polyribonucleotide Nucleotidyltransferase - chemistry
Polyribonucleotide Nucleotidyltransferase - metabolism
Pseudoalteromonas - enzymology
Sequence Alignment
Temperature
Online AccessGet more information

Cover

More Information
Summary: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 degrees C. PhPNPase is quite sensitive to heat treatment and it is endowed with remarkable halotolerance.
ISSN:1875-5305
DOI:10.2174/092986609789055296