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Information on EC 2.7.7.8 - polyribonucleotide nucleotidyltransferase and Organism(s) Streptomyces antibioticus and UniProt Accession Q53597

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IUBMB Comments
ADP, IDP, GDP, UDP and CDP can act as donors.
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This record set is specific for:
Streptomyces antibioticus
UNIPROT: Q53597
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The taxonomic range for the selected organisms is: Streptomyces antibioticus
The enzyme appears in selected viruses and cellular organisms
Synonyms
polynucleotide phosphorylase, hpnpase(old-35), pnpt1, polyribonucleotide nucleotidyltransferase, atmtpnpase, cppnpase, chloroplast pnpase, hpnpaseold-35, polyribonucleotide phosphorylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleoside diphosphate:polynucleotidyl transferase
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nucleotidyltransferase, polyribonucleotide
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PNPase
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polynucleotide phosphorylase
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polyribonucleotide phosphorylase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
polyribonucleotide:phosphate nucleotidyltransferase
ADP, IDP, GDP, UDP and CDP can act as donors.
CAS REGISTRY NUMBER
COMMENTARY hide
9014-12-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PNP_STRAT
740
0
79160
Swiss-Prot
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
81132
x * 81132, electrospray mass spectrometry
81133
x * 81133, deduced from nucleotide sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
protein solution mixed at 3/1 ratio with well solution consisting of 2 M ammonium sulfate, 100 mM Tris-HCl, pH 8.5, 5 mM dithiothreitol and 0.75 mM Na2AsO4, crystals are harvested in a so called mirror solution from equilibrated droplets with buffer replacing enzyme solution and no added Na2AsO4, crystals of native PNPase, a tungstate derivative and a seleno-methionyl derivative
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme, HiTrap Q, HiFlow Phenyl-Sepharose
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression of gpsI gene encoding PNPase in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Symmons, M.F.; Jones, G.H.; Luisi, B.F.
A duplicated fold is the structural basis for polynucleotide phosphorylase catalytic activity, processivity, and regulation
Structure Fold. Des.
8
1215-1226
2000
Streptomyces antibioticus (Q53597), Streptomyces antibioticus
Manually annotated by BRENDA team