H2N2V1, Main, Exploration, bibRecord, 001F98

Characterisation of an ionisable group involved in binding and catalysis by sialidase from influenza virus.

Identifieur interne : 001F98 ( Main/Exploration ); précédent : 001F97; suivant : 001F99

Characterisation of an ionisable group involved in binding and catalysis by sialidase from influenza virus.

Auteurs : A K Chong [Australie] ; M S Pegg ; M. Von Itzstein

Source :

Biochemistry international [ 0158-5231 ] ; 1991.

RBID : pubmed:1768256

Descripteurs français

KwdFr :
- Cinétique, Colorants fluorescents, Concentration en ions d'hydrogène, Fixation compétitive, Hymécromone (analogues et dérivés), Sialidase (antagonistes et inhibiteurs), Sialidase (métabolisme), Sites de fixation, Virus de la grippe A (enzymologie).
MESH :
- analogues et dérivés : Hymécromone.
- antagonistes et inhibiteurs : Sialidase.
- enzymologie : Virus de la grippe A.
- métabolisme : Sialidase.
- Cinétique, Colorants fluorescents, Concentration en ions d'hydrogène, Fixation compétitive, Sites de fixation.

English descriptors

KwdEn :
- Binding Sites, Binding, Competitive, Fluorescent Dyes, Hydrogen-Ion Concentration, Hymecromone (analogs & derivatives), Influenza A virus (enzymology), Kinetics, Neuraminidase (antagonists & inhibitors), Neuraminidase (metabolism).
MESH :
- chemical , analogs & derivatives : Hymecromone.
- chemical , antagonists & inhibitors : Neuraminidase.
- chemical , metabolism : Neuraminidase.
- chemical : Fluorescent Dyes.
- enzymology : Influenza A virus.
- Binding Sites, Binding, Competitive, Hydrogen-Ion Concentration, Kinetics.

Abstract

The effect of pH on the kinetics of sialidase purified from influenza virus (A/Tokyo/3/67, H2N2) was investigated. A pK of 9.0 for inhibition of the enzyme by three competitive inhibitors, due to an ionisable group in the active site, was observed. A similar pK was observed for V/Km for the fluorogenic substrate 2-(4-methylumbelliferyl)-N-acetyl-alpha-D-neuraminic acid. However, the shape of the V/Km profile indicates that this substrate is sticky. Solvent perturbation experiments indicated that the observed ionisable active site group is likely to be a cationic amino acid. The results provide evidence against the hypothesis that Glu 276 acts as a proton donor in the enzyme reaction and supports the proposal of a role for one of the active site cationic amino acids in binding and catalysis.

PubMed: 1768256

Affiliations:

Australie

Le document en format XML

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<author><name sortKey="Chong, A K" sort="Chong, A K" uniqKey="Chong A" first="A K" last="Chong">A K Chong</name>
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<author><name sortKey="Pegg, M S" sort="Pegg, M S" uniqKey="Pegg M" first="M S" last="Pegg">M S Pegg</name>
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<series><title level="j">Biochemistry international</title>
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<term>Hymecromone (analogs & derivatives)</term>
<term>Influenza A virus (enzymology)</term>
<term>Kinetics</term>
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<term>Neuraminidase (metabolism)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Cinétique</term>
<term>Colorants fluorescents</term>
<term>Concentration en ions d'hydrogène</term>
<term>Fixation compétitive</term>
<term>Hymécromone (analogues et dérivés)</term>
<term>Sialidase (antagonistes et inhibiteurs)</term>
<term>Sialidase (métabolisme)</term>
<term>Sites de fixation</term>
<term>Virus de la grippe A (enzymologie)</term>
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<keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Hymecromone</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Neuraminidase</term>
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<keywords scheme="MESH" type="chemical" xml:lang="en"><term>Fluorescent Dyes</term>
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<keywords scheme="MESH" qualifier="analogues et dérivés" xml:lang="fr"><term>Hymécromone</term>
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<keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Sialidase</term>
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<term>Sites de fixation</term>
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<front><div type="abstract" xml:lang="en">The effect of pH on the kinetics of sialidase purified from influenza virus (A/Tokyo/3/67, H2N2) was investigated. A pK of 9.0 for inhibition of the enzyme by three competitive inhibitors, due to an ionisable group in the active site, was observed. A similar pK was observed for V/Km for the fluorogenic substrate 2-(4-methylumbelliferyl)-N-acetyl-alpha-D-neuraminic acid. However, the shape of the V/Km profile indicates that this substrate is sticky. Solvent perturbation experiments indicated that the observed ionisable active site group is likely to be a cationic amino acid. The results provide evidence against the hypothesis that Glu 276 acts as a proton donor in the enzyme reaction and supports the proposal of a role for one of the active site cationic amino acids in binding and catalysis.</div>
</front>
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<tree><noCountry><name sortKey="Pegg, M S" sort="Pegg, M S" uniqKey="Pegg M" first="M S" last="Pegg">M S Pegg</name>
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<country name="Australie"><noRegion><name sortKey="Chong, A K" sort="Chong, A K" uniqKey="Chong A" first="A K" last="Chong">A K Chong</name>
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Characterisation of an ionisable group involved in binding and catalysis by sialidase from influenza virus.

Characterisation of an ionisable group involved in binding and catalysis by sialidase from influenza virus.

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 H2N2
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