Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:2.7.7.8 (
polynucleotide phosphorylase
)
723
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
A new method for isolation of
polynucleotide phosphorylase
from E. coli, including ion-exchange chromatography and gel-filtration has been developed. The method results in 300-fold purification of the enzyme, which being devoid of nuclease and
phosphatase
activities can further be utilized for oligonucleotide synthesis. It was shown that upon storage the enzyme loses the primer-independent activity and in the absence of NaCl can be used for further syntheses. An addition of NaCl stimulates the elongation of the oligonucleotide chain. Some advantages of
polynucleotide phosphorylase
from E. coli in comparison with the M. luteus enzyme are discussed.
...
PMID:[Isolation and some properties of polynucleotide phosphorylase from E. coli]. 702 38
The SP diastereomer of adenosine 5'-O-(1-thiodiphosphate) (ADP alpha S) is a substrate for the 32P-labeled inorganic phosphate exchange reaction catalyzed by the T and I forms of
polynucleotide phosphorylase
. The exchange reaction occurs with retention of configuration. This exchange reaction is very slow when only ADP alpha S(SP) is presented but is greatly activated by dinucleotide primers and ADP alpha S(RP), although the latter is not a substrate for the exchange reaction. Ap(S)A(RP) is an approximately 50% better activator of the exchange than the SP diastereomer. Furthermore, high levels of the ADP alpha S(SP) eliminate the activation by primers and by ADP alpha S(RP). A
phosphatase
activity is present with the I form of the enzyme which converts ADP alpha S(RP) to AMPS. This activity may be responsible for the formation of the 5'-phosphate end group for de novo polymerization or for the processivity of this reaction.
...
PMID:Stereochemical and kinetic investigation of 32P-labeled inorganic phosphate exchange reaction catalyzed by primer-independent and primer-dependent polynucleotide phosphorylase from Micrococcus luteus. 723 93
