Study on the structure-function relationship of polynucleotide phosphorylase: model of a proteolytic degraded polynucleotide phosphorylase.

Nucleic acids research ·Vol. 3 ·No. 11 ·1976-11-00 ·Pages 3015-24

Guissani A, Portier C

Abstract

It is already known that modification of E. coli polynucleotide phosphorylase by endogenous proteolysis induces drastic changes in both phosphorolysis and polymerisation reactions. The structural parameters of the proteolysed polynucleotide phosphorylase are described. The phosphorolysis of polynucleotide, which is quite progressive for the native enzyme, is shown to be only partially progressive for the degraded enzyme, owing to the loss of polymer attachment sites.

MeSH Terms

Escherichia coli/enzymology Kinetics Molecular Weight Peptide Hydrolases/metabolism Polyribonucleotide Nucleotidyltransferase/isolation & purification,metabolism Protein Conformation Structure-Activity Relationship

Chemicals

Polyribonucleotide Nucleotidyltransferase Peptide Hydrolases

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Guissani A

Portier C

References (11)

11 references, click to expand

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Article Info

Journal

Nucleic acids research

Abbr.

Nucleic Acids Res

ISSN

0305-1048

DOI

10.1093/nar/3.11.3015

Published

1976-11-00

Pages

3015-24

Language

English

Region

England

NLM ID

0411011

PMCID

PMC343148

Subset

External Links

PubMed source DOI: 10.1093/nar/3.11.3015 PMC Full Text View journal details

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Study on the structure-function relationship of polynucleotide phosphorylase: model of a proteolytic degraded polynucleotide phosphorylase.

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