MersV1, Main, Exploration, bibRecord, 004D27

Processivity and kinetics of the reaction of exonuclease I from Escherichia coli with polydeoxyribonucleotides.

Identifieur interne : 004D27 ( Main/Exploration ); précédent : 004D26; suivant : 004D28

Processivity and kinetics of the reaction of exonuclease I from Escherichia coli with polydeoxyribonucleotides.

Auteurs : R S Brody ; K G Doherty ; P D Zimmerman

Source :

The Journal of biological chemistry [ 0021-9258 ] ; 1986.

RBID : pubmed:3519606

Descripteurs français

KwdFr :
- Cinétique, Escherichia coli (enzymologie), Exodeoxyribonucleases, Fixation compétitive, Hydrolyse, Masse moléculaire, Oligodésoxyribonucléotides, Polydésoxyribonucléotides, Sites de fixation.
MESH :
- enzymologie : Escherichia coli.
- Cinétique, Exodeoxyribonucleases, Fixation compétitive, Hydrolyse, Masse moléculaire, Oligodésoxyribonucléotides, Polydésoxyribonucléotides, Sites de fixation.

English descriptors

KwdEn :
- Binding Sites, Binding, Competitive, Escherichia coli (enzymology), Exodeoxyribonucleases, Hydrolysis, Kinetics, Molecular Weight, Oligodeoxyribonucleotides, Polydeoxyribonucleotides.
MESH :
- chemical : Exodeoxyribonucleases, Oligodeoxyribonucleotides, Polydeoxyribonucleotides.
- enzymology : Escherichia coli.
- Binding Sites, Binding, Competitive, Hydrolysis, Kinetics, Molecular Weight.

Abstract

The enzyme exonuclease I from Escherichia coli hydrolyzes successive nucleotides from the 3'-termini of single-stranded deoxyribonucleotide homopolymers. When the reaction is stopped after partial hydrolysis, only intact starting material and small oligomers can be isolated. The distribution of oligomeric products varies with the base composition of the polymer but the largest oligomer that can be isolated from the reaction of exonuclease I with homopolymers of deoxyadenylate, deoxythymidylate, or deoxycytidylate is a decamer. These results suggest a model in which exonuclease I possesses at least two nucleotide binding sites. When both sites are filled, with 11-mers and longer polymers, the enzyme does not dissociate from the polymer during hydrolysis. When, with smaller oligomers, only a single site is filled, the reaction partitions at each oligomer between hydrolysis and dissociation. The kinetics of the reactions of exonuclease I with purified polydeoxyriboadenylates of defined size distributions have been investigated. The maximum rates of hydrolysis are nearly independent of polymer size while the apparent Michaelis constants are inversely proportional to the polymer size. A simple steady state model yields a kinetic equation that is consistent with our results. Competition experiments indicate that the rate at which exonuclease I associates with the 3'-terminus of a polydeoxyribonucleotide is independent of the polymer's chain length.

PubMed: 3519606

Affiliations:

Le document en format XML

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<term>Hydrolyse</term>
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<term>Fixation compétitive</term>
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<term>Masse moléculaire</term>
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<front><div type="abstract" xml:lang="en">The enzyme exonuclease I from Escherichia coli hydrolyzes successive nucleotides from the 3'-termini of single-stranded deoxyribonucleotide homopolymers. When the reaction is stopped after partial hydrolysis, only intact starting material and small oligomers can be isolated. The distribution of oligomeric products varies with the base composition of the polymer but the largest oligomer that can be isolated from the reaction of exonuclease I with homopolymers of deoxyadenylate, deoxythymidylate, or deoxycytidylate is a decamer. These results suggest a model in which exonuclease I possesses at least two nucleotide binding sites. When both sites are filled, with 11-mers and longer polymers, the enzyme does not dissociate from the polymer during hydrolysis. When, with smaller oligomers, only a single site is filled, the reaction partitions at each oligomer between hydrolysis and dissociation. The kinetics of the reactions of exonuclease I with purified polydeoxyriboadenylates of defined size distributions have been investigated. The maximum rates of hydrolysis are nearly independent of polymer size while the apparent Michaelis constants are inversely proportional to the polymer size. A simple steady state model yields a kinetic equation that is consistent with our results. Competition experiments indicate that the rate at which exonuclease I associates with the 3'-terminus of a polydeoxyribonucleotide is independent of the polymer's chain length.</div>
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Processivity and kinetics of the reaction of exonuclease I from Escherichia coli with polydeoxyribonucleotides.

Processivity and kinetics of the reaction of exonuclease I from Escherichia coli with polydeoxyribonucleotides.

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki

	Serveur d'exploration MERS
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