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 sensitive to heat treatment and it is endowed with remarkable halotolerance.
Dipartimento di Scienze e Tecnologie Ambiente e Territorio, C/da Fonte Lappone, I-86090, Pesche (IS), Italy. raimo@unimol.it
G
G
Evangelista
P
P
Falasca
I
I
Ruggiero
M
M
Masullo
G
G
Raimo
D000595:Amino Acid Sequence; D004795:Enzyme Stability; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011117:Polyribonucleotide Nucleotidyltransferase / Q000737:chemistry* / Q000378:metabolism; D031161:Pseudoalteromonas / Q000201:enzymology; D016415:Sequence Alignment; D013696:Temperature
D011117:Polyribonucleotide Nucleotidyltransferase