PhanerochaeteV1, Main, Exploration, bibRecord, 000397

A steady-state theory for processive cellulases.

Identifieur interne : 000397 ( Main/Exploration ); précédent : 000396; suivant : 000398

A steady-state theory for processive cellulases.

Auteurs : Nicolaj Cruys-Bagger [Danemark] ; Jens Elmerdahl ; Eigil Praestgaard ; Kim Borch ; Peter Westh

Source :

The FEBS journal [ 1742-4658 ] ; 2013.

RBID : pubmed:23786663

Descripteurs français

KwdFr :
- Algorithmes (MeSH), Cellobiose (métabolisme), Cellulases (métabolisme), Cellulose (composition chimique), Cellulose (métabolisme), Cellulose 1,4-beta-cellobiosidase (métabolisme), Cinétique (MeSH), Hydrolyse (MeSH), Hypocrea (enzymologie), Hypocrea (métabolisme), Modèles moléculaires (MeSH), Phanerochaete (enzymologie), Phanerochaete (métabolisme), Protéines fongiques (métabolisme), Solubilité (MeSH).
MESH :
- composition chimique : Cellulose.
- enzymologie : Hypocrea, Phanerochaete.
- métabolisme : Cellobiose, Cellulases, Cellulose, Cellulose 1,4-beta-cellobiosidase, Hypocrea, Phanerochaete, Protéines fongiques.
- Algorithmes, Cinétique, Hydrolyse, Modèles moléculaires, Solubilité.

English descriptors

KwdEn :
- Algorithms (MeSH), Cellobiose (metabolism), Cellulases (metabolism), Cellulose (chemistry), Cellulose (metabolism), Cellulose 1,4-beta-Cellobiosidase (metabolism), Fungal Proteins (metabolism), Hydrolysis (MeSH), Hypocrea (enzymology), Hypocrea (metabolism), Kinetics (MeSH), Models, Molecular (MeSH), Phanerochaete (enzymology), Phanerochaete (metabolism), Solubility (MeSH).
MESH :
- chemical , chemistry : Cellulose.
- chemical , metabolism : Cellobiose, Cellulases, Cellulose, Cellulose 1,4-beta-Cellobiosidase, Fungal Proteins.
- enzymology : Hypocrea, Phanerochaete.
- metabolism : Hypocrea, Phanerochaete.
- Algorithms, Hydrolysis, Kinetics, Models, Molecular, Solubility.

Abstract

Processive enzymes perform sequential steps of catalysis without dissociating from their polymeric substrate. This mechanism is considered essential for efficient enzymatic hydrolysis of insoluble cellulose (particularly crystalline cellulose), but a theoretical framework for processive kinetics remains to be fully developed. In this paper, we suggest a deterministic kinetic model that relies on a processive set of enzyme reactions and a quasi steady-state assumption. It is shown that this approach is practicable in the sense that it leads to mathematically simple expressions for the steady-state rate, and only requires data from standard assay techniques as experimental input. Specifically, it is shown that the processive reaction rate at steady state may be expressed by a hyperbolic function related to the conventional Michaelis-Menten equation. The main difference is a 'kinetic processivity coefficient', which represents the probability of the enzyme dissociating from the substrate strand before completing n sequential catalytic steps, where n is the mean processivity number measured experimentally. Typical processive cellulases have high substrate affinity, and therefore this probability is low. This has significant kinetic implications, for example the maximal specific rate (V(max)/E₀) for processive cellulases is much lower than the catalytic rate constant (k(cat)). We discuss how relationships based on this theory may be used in both comparative and mechanistic analyses of cellulases.

DOI: 10.1111/febs.12397
PubMed: 23786663

Affiliations:

Danemark

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Le document en format XML

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<author><name sortKey="Cruys Bagger, Nicolaj" sort="Cruys Bagger, Nicolaj" uniqKey="Cruys Bagger N" first="Nicolaj" last="Cruys-Bagger">Nicolaj Cruys-Bagger</name>
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<author><name sortKey="Elmerdahl, Jens" sort="Elmerdahl, Jens" uniqKey="Elmerdahl J" first="Jens" last="Elmerdahl">Jens Elmerdahl</name>
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<author><name sortKey="Praestgaard, Eigil" sort="Praestgaard, Eigil" uniqKey="Praestgaard E" first="Eigil" last="Praestgaard">Eigil Praestgaard</name>
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<term>Cellobiose (metabolism)</term>
<term>Cellulases (metabolism)</term>
<term>Cellulose (chemistry)</term>
<term>Cellulose (metabolism)</term>
<term>Cellulose 1,4-beta-Cellobiosidase (metabolism)</term>
<term>Fungal Proteins (metabolism)</term>
<term>Hydrolysis (MeSH)</term>
<term>Hypocrea (enzymology)</term>
<term>Hypocrea (metabolism)</term>
<term>Kinetics (MeSH)</term>
<term>Models, Molecular (MeSH)</term>
<term>Phanerochaete (enzymology)</term>
<term>Phanerochaete (metabolism)</term>
<term>Solubility (MeSH)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Algorithmes (MeSH)</term>
<term>Cellobiose (métabolisme)</term>
<term>Cellulases (métabolisme)</term>
<term>Cellulose (composition chimique)</term>
<term>Cellulose (métabolisme)</term>
<term>Cellulose 1,4-beta-cellobiosidase (métabolisme)</term>
<term>Cinétique (MeSH)</term>
<term>Hydrolyse (MeSH)</term>
<term>Hypocrea (enzymologie)</term>
<term>Hypocrea (métabolisme)</term>
<term>Modèles moléculaires (MeSH)</term>
<term>Phanerochaete (enzymologie)</term>
<term>Phanerochaete (métabolisme)</term>
<term>Protéines fongiques (métabolisme)</term>
<term>Solubilité (MeSH)</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cellulose</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cellobiose</term>
<term>Cellulases</term>
<term>Cellulose</term>
<term>Cellulose 1,4-beta-Cellobiosidase</term>
<term>Fungal Proteins</term>
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<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Cellulose</term>
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<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Hypocrea</term>
<term>Phanerochaete</term>
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<term>Phanerochaete</term>
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<term>Cellulases</term>
<term>Cellulose</term>
<term>Cellulose 1,4-beta-cellobiosidase</term>
<term>Hypocrea</term>
<term>Phanerochaete</term>
<term>Protéines fongiques</term>
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<term>Hydrolysis</term>
<term>Kinetics</term>
<term>Models, Molecular</term>
<term>Solubility</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Algorithmes</term>
<term>Cinétique</term>
<term>Hydrolyse</term>
<term>Modèles moléculaires</term>
<term>Solubilité</term>
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<front><div type="abstract" xml:lang="en">Processive enzymes perform sequential steps of catalysis without dissociating from their polymeric substrate. This mechanism is considered essential for efficient enzymatic hydrolysis of insoluble cellulose (particularly crystalline cellulose), but a theoretical framework for processive kinetics remains to be fully developed. In this paper, we suggest a deterministic kinetic model that relies on a processive set of enzyme reactions and a quasi steady-state assumption. It is shown that this approach is practicable in the sense that it leads to mathematically simple expressions for the steady-state rate, and only requires data from standard assay techniques as experimental input. Specifically, it is shown that the processive reaction rate at steady state may be expressed by a hyperbolic function related to the conventional Michaelis-Menten equation. The main difference is a 'kinetic processivity coefficient', which represents the probability of the enzyme dissociating from the substrate strand before completing n sequential catalytic steps, where n is the mean processivity number measured experimentally. Typical processive cellulases have high substrate affinity, and therefore this probability is low. This has significant kinetic implications, for example the maximal specific rate (V(max)/E₀) for processive cellulases is much lower than the catalytic rate constant (k(cat)). We discuss how relationships based on this theory may be used in both comparative and mechanistic analyses of cellulases.</div>
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<Abstract><AbstractText>Processive enzymes perform sequential steps of catalysis without dissociating from their polymeric substrate. This mechanism is considered essential for efficient enzymatic hydrolysis of insoluble cellulose (particularly crystalline cellulose), but a theoretical framework for processive kinetics remains to be fully developed. In this paper, we suggest a deterministic kinetic model that relies on a processive set of enzyme reactions and a quasi steady-state assumption. It is shown that this approach is practicable in the sense that it leads to mathematically simple expressions for the steady-state rate, and only requires data from standard assay techniques as experimental input. Specifically, it is shown that the processive reaction rate at steady state may be expressed by a hyperbolic function related to the conventional Michaelis-Menten equation. The main difference is a 'kinetic processivity coefficient', which represents the probability of the enzyme dissociating from the substrate strand before completing n sequential catalytic steps, where n is the mean processivity number measured experimentally. Typical processive cellulases have high substrate affinity, and therefore this probability is low. This has significant kinetic implications, for example the maximal specific rate (V(max)/E₀) for processive cellulases is much lower than the catalytic rate constant (k(cat)). We discuss how relationships based on this theory may be used in both comparative and mechanistic analyses of cellulases.</AbstractText>
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A steady-state theory for processive cellulases.

A steady-state theory for processive cellulases.

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