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NH4+
-
maximal activity at 33 mM, inhibition above 150 mM
KCl
-
requirement is dependent on the primer and the divalent cation used
KCl
-
maximal stimulation at 40 mM, inhibition above 250 mM
KCl
-
maximal activity at 33 mM, inhibition above 150 mM
KCl
-
optimal concentration: 60 mM
Mg2+
more active in presence of Mg2+ than Mn2+
Mg2+
-
more active in presence of Mn2+ than Mg2+
Mg2+
-
optimal concentration is about 5 mM
Mg2+
-
divalent cation requirement may be fulfilled by Mn2+, Mg2+ or a combination of the two depending on the source of the enzyme
Mg2+
-
more active in presence of Mn2+ than Mg2+
Mg2+
-
optimal concentration: 4-6 mM
Mg2+
-
more active in presence of Mg2+ than Mn2+
Mg2+
-
completely inactive in presence of Mg2+
Mg2+
-
one-fifth of the activity of Mg2+ in NTP activation
Mg2+
-
more active in presence of Mn2+ than Mg2+
Mg2+
Coturnix sp.
-
divalent cation requirement may be fulfilled by Mn2+, Mg2+ or a combination of the two depending on the source of the enzyme
Mg2+
-
divalent cation requirement may be fulfilled by Mn2+, Mg2+ or a combination of the two depending on the source of the enzyme
Mg2+
-
divalent cation requirement may be fulfilled by Mn2+, Mg2+ or a combination of the two depending on the source of the enzyme
Mg2+
-
more active in presence of Mn2+ than Mg2+
Mg2+
-
in presence of Mg2+ and a specificity factor required for correct cleavage at the poly(A) site of pre-mRNA
Mg2+
-
optimal concentration: 5 mM
Mg2+
-
Mg2+ or Mn2+ required
Mg2+
-
NE PAP I (isoenzyme from cytoplasmic fraction) and S100 PAP (isoenzyme from nuclear fraction): higher activity in presence of Mn2+ than in presence of Mg2+, NE PAP II: approximately equal levels in presence of Mn2+ and Mg2+
Mg2+
-
divalent cation requirement may be fulfilled by Mn2+, Mg2+ or a combination of the two depending on the source of the enzyme
Mg2+
-
HeLa cells contain one enzyme form that is stimulated by Mn2+ and also by Mg2+, and a second one that is absolutely dependent on the presence of Mg2+
Mg2+
-
in presence of Mg2+ and a specificity factor required for correct cleavage at the poly(A) site of pre-mRNA
Mg2+
-
Mg2+ ions can release the inhibition of PAPgamma by aminoglycosides
Mg2+
0.5 mM used in assay conditions
Mg2+
4 mM used in assay conditions. When Mg2+ is replaced by Mn2+, the protein becomes more potent in catalyzing polyadenylation
Mg2+
-
Mg2+ is inactive, maximum activity in presence of both Mn2+ and Mg2+
Mg2+
-
divalent cation requirement may be fulfilled by Mn2+, Mg2+ or a combination of the two depending on the source of the enzyme
Mg2+
0.5 mM used in assay conditions
Mg2+
-
more active in presence of Mg2+ than Mn2+
Mg2+
-
more active in presence of Mg2+ than Mn2+
Mg2+
-
10% of the activity with Mn2+
Mg2+
-
divalent cation requirement may be fulfilled by Mn2+, Mg2+ or a combination of the two depending on the source of the enzyme
Mg2+
-
optimal concentration: 8-10 mM, polymerase I from chromatin, polymerase II from nucleoplasm is inactive in presence of Mg2+
Mg2+
-
more active in presence of Mn2+ than Mg2+
Mg2+
essential for activity
Mg2+
required for activity
Mg2+
-
more active in presence of Mn2+ than Mg2+
Mg2+
-
optimal concentration depends on ATP concentration
Mg2+
-
divalent cation requirement may be fulfilled by Mn2+, Mg2+ or a combination of the two depending on the source of the enzyme
Mg2+
-
more active in presence of Mn2+ than Mg2+
Mg2+
-
Vaccinia virus enzyme is stimulated by Mn2+ and also by Mg2+
Mg2+
4 mM used in assay conditions. When Mg2+ is replaced by Mn2+, the protein becomes more potent in catalyzing polyadenylation
Mg2+
-
ATP is utilized 150-fold more with Mn2+ than with Mg2+
Mn2+
more active in presence of Mg2+ than Mn2+
Mn2+
-
exclusively activated by Mn2+
Mn2+
-
optimal concentration: 2-4 mM
Mn2+
-
more active in presence of Mn2+ than Mg2+
Mn2+
-
divalent cation requirement may be fulfilled by Mn2+, Mg2+ or a combination of the two depending on the source of the enzyme
Mn2+
-
more active in presence of Mn2+ than Mg2+
Mn2+
-
more active in presence of Mg2+ than Mn2+
Mn2+
-
optimal concentration: 0.5 mM (at 0.5 mM ATP)
Mn2+
-
required for NTP activation
Mn2+
-
more active in presence of Mn2+ than Mg2+
Mn2+
Coturnix sp.
-
divalent cation requirement may be fulfilled by Mn2+, Mg2+ or a combination of the two depending on the source of the enzyme
Mn2+
-
divalent cation requirement may be fulfilled by Mn2+, Mg2+ or a combination of the two depending on the source of the enzyme
Mn2+
-
divalent cation requirement may be fulfilled by Mn2+, Mg2+ or a combination of the two depending on the source of the enzyme
Mn2+
-
more active in presence of Mn2+ than Mg2+
Mn2+
-
Mn2+ or Mg2+ required
Mn2+
-
optimal concentration: 2 mM
Mn2+
-
divalent cation requirement may be fulfilled by Mn2+, Mg2+ or a combination of the two depending on the source of the enzyme
Mn2+
-
HeLa cells contain one enzyme form that is stimulated by Mn2+ and also by Mg2+, and a second one that is absolutely dependent on the presence of Mg2+
Mn2+
-
NE PAP I (isoenzyme from nuclear fraction) and S100 PAP (isoenzyme from cytoplasmic fraction): higher activity in presence of Mn2+ than in presence of Mg2+, NE PAP II: approximately equal levels in presence of Mn2+ and Mg2+
Mn2+
-
nonspecific adenylation of RNA in presence of Mn2+
Mn2+
0.5 mM used in assay conditions
Mn2+
4 mM used in assay conditions
Mn2+
-
maximum activity in presence of both Mn2+ and Mg2+
Mn2+
-
optimal concentration: 4 mM (polymerase IIa), 4-8 mM (polymerase IIb)
Mn2+
-
divalent cation requirement may be fulfilled by Mn2+, Mg2+ or a combination of the two depending on the source of the enzyme
Mn2+
0.5 mM used in assay conditions
Mn2+
0.5 mM used in assay conditions
Mn2+
-
more active in presence of Mg2+ than Mn2+
Mn2+
-
absolute requirement
Mn2+
-
divalent cation requirement may be fulfilled by Mn2+, Mg2+ or a combination of the two depending on the source of the enzyme
Mn2+
-
more active in presence of Mn2+ than Mg2+
Mn2+
-
optimal concentration: 0.50-0.75 mM
Mn2+
-
optimal concentration: 0.25-1.0 mM
Mn2+
-
optimal concentration: 0.8 mM (polymerase I and II)
Mn2+
-
optimal concentration: 0.25-0.75 mM
Mn2+
-
more active in presence of Mn2+ than Mg2+
Mn2+
-
optimal concentration depends on ATP concentration
Mn2+
-
Mg2+ can partially replace Mn2+ in the reaction with polymerase II
Mn2+
-
divalent cation requirement may be fulfilled by Mn2+, Mg2+ or a combination of the two depending on the source of the enzyme
Mn2+
-
more active in presence of Mn2+ than Mg2+
Mn2+
-
Vaccinia virus enzyme is stimulated by Mn2+ and also by Mg2+
Mn2+
-
optimal concentration: 2 mM
Mn2+
4 mM used in assay conditions
Mn2+
-
ATP is utilized 150-fold more with Mn2+ than with Mg2+
additional information
-
overview: ion requirements, poly(A) polymerases purified from different sources, and in some cases even from the same source, respond differently to the presence of Mg2+ and Mn2+
additional information
Coturnix sp.
-
overview: ion requirements, poly(A) polymerases purified from different sources, and in some cases even from the same source, respond differently to the presence of Mg2+ and Mn2+
additional information
-
overview: ion requirements, poly(A) polymerases purified from different sources, and in some cases even from the same source, respond differently to the presence of Mg2+ and Mn2+
additional information
-
overview: ion requirements, poly(A) polymerases purified from different sources, and in some cases even from the same source, respond differently to the presence of Mg2+ and Mn2+
additional information
-
overview: ion requirements, poly(A) polymerases purified from different sources, and in some cases even from the same source, respond differently to the presence of Mg2+ and Mn2+
additional information
-
overview: ion requirements, poly(A) polymerases purified from different sources, and in some cases even from the same source, respond differently to the presence of Mg2+ and Mn2+
additional information
-
overview: ion requirements, poly(A) polymerases purified from different sources, and in some cases even from the same source, respond differently to the presence of Mg2+ and Mn2+
additional information
-
low ionic strength required for maximal activity
additional information
-
overview: ion requirements, poly(A) polymerases purified from different sources, and in some cases even from the same source, respond differently to the presence of Mg2+ and Mn2+