Abstract
The SP diastereomer of adenosine 5'-O-(1-thiodiphosphate) (ADPαS) 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 ADPaS(5P) is present but is greatly activated by dinucleotide primers and ADPαS (RP), although the latter is not a substrate for the exchange reaction. Ap(S)A(RP) is an ~50% better activator of the exchange than the SP diastereomer. Furthermore, high levels of the ADPαS(SP) eliminate the activation by primers and by ADPαS (RP). A phosphatase activity is present with the I form of the enzyme which converts ADPaS(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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 2212-2219 |
| Number of pages | 8 |
| Journal | Biochemistry |
| Volume | 20 |
| Issue number | 8 |
| DOIs | |
| State | Published - Jan 1 1981 |
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All Science Journal Classification (ASJC) codes
- Biochemistry
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Stereochemical and Kinetic Investigation of 32P-Labeled Inorganic Phosphate Exchange Reaction Catalyzed by Primer-Independent and Primer-Dependent Polynucleotide Phosphorylase from Micrococcus luteus. / Marlier, John F.; Bryant, Floyd R.; Benkovic, Stephen.
In: Biochemistry, Vol. 20, No. 8, 01.01.1981, p. 2212-2219.Research output: Contribution to journal › Article
TY - JOUR
T1 - Stereochemical and Kinetic Investigation of 32P-Labeled Inorganic Phosphate Exchange Reaction Catalyzed by Primer-Independent and Primer-Dependent Polynucleotide Phosphorylase from Micrococcus luteus
AU - Marlier, John F.
AU - Bryant, Floyd R.
AU - Benkovic, Stephen
PY - 1981/1/1
Y1 - 1981/1/1
N2 - The SP diastereomer of adenosine 5'-O-(1-thiodiphosphate) (ADPαS) 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 ADPaS(5P) is present but is greatly activated by dinucleotide primers and ADPαS (RP), although the latter is not a substrate for the exchange reaction. Ap(S)A(RP) is an ~50% better activator of the exchange than the SP diastereomer. Furthermore, high levels of the ADPαS(SP) eliminate the activation by primers and by ADPαS (RP). A phosphatase activity is present with the I form of the enzyme which converts ADPaS(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.
AB - The SP diastereomer of adenosine 5'-O-(1-thiodiphosphate) (ADPαS) 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 ADPaS(5P) is present but is greatly activated by dinucleotide primers and ADPαS (RP), although the latter is not a substrate for the exchange reaction. Ap(S)A(RP) is an ~50% better activator of the exchange than the SP diastereomer. Furthermore, high levels of the ADPαS(SP) eliminate the activation by primers and by ADPαS (RP). A phosphatase activity is present with the I form of the enzyme which converts ADPaS(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.
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U2 - 10.1021/bi00511a022
DO - 10.1021/bi00511a022
M3 - Article
VL - 20
SP - 2212
EP - 2219
JO - Biochemistry
JF - Biochemistry
SN - 0006-2960
IS - 8
ER -