Transient-time analysis of substrate-channelling in interacting enzyme systems. - Wikidata - awgldk - TriplyDB

Transient-time analysis of substrate-channelling in interacting enzyme systems.

Transient-time analysis of substrate-channelling in interacting enzyme systems.

http://www.wikidata.org/entity/Q41888110

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Biochemical and Structural Characterization of the Arabidopsis Bifunctional Enzyme Dethiobiotin Synthetase–Diaminopelargonic Acid Aminotransferase: Evidence for Substrate Channeling in Biotin Synthesis Mathematical analysis of enzymic reaction systems using optimization principles.Enzyme-enzyme interactions and their metabolic role.Enzyme-enzyme interactions and control analysis. 2. The case of non-independence: heterologous associations.Understanding the molecular mechanism of substrate channeling and domain communication in protozoal bifunctional TS-DHFR.Proximity does not contribute to activity enhancement in the glucose oxidase-horseradish peroxidase cascade.The analysis of metabolite channelling in multienzyme complexes and multifunctional proteins Kinetic misinterpretation of a coupled enzyme reaction can lead to the assumption of an enzyme-enzyme interaction. The example of 3-phospho-D-glycerate kinase and glyceraldehyde-3-phosphate dehydrogenase couple.Strong control on the transit time in metabolic channelling Steady-state kinetic behaviour of functioning-dependent structures

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P2860

Transient-time analysis of substrate-channelling in interacting enzyme systems.

http://www.wikidata.org/entity/Q41888110

description

1989 nî lūn-bûn

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1989年の論文

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1989年論文

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1989年論文

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1989年論文

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1989年論文

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1989年論文

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1989年论文

@wuu

1989年论文

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1989年论文

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name

Transient-time analysis of substrate-channelling in interacting enzyme systems.

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Transient-time analysis of substrate-channelling in interacting enzyme systems.

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Transient-time analysis of substrate-channelling in interacting enzyme systems.

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Biochemical Journal

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Transient-time analysis of substrate-channelling in interacting enzyme systems.

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Keleti T

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Orosz F

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Ovádi J

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Tompa P

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Vértessy B

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Welch GR

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P2860

Properties and metabolism of the aqueous cytoplasm and its boundaries.

On the role of organized multienzyme systems in cellular metabolism: a general synthesis.

On the free energy "cost of transition" in intermediary metabolic processes and the evolution of cellular infrastructure.

Fractionation and structural assessment of oligosaccharides and glycopeptides by use of immobilized lectins.

Enzyme-enzyme interactions and the regulation of metabolic reaction pathways.

Mathematical analysis of multienzyme systems. I. Modelling of the glycolysis of human erythrocytes.

Macromolecular interactions in enzyme regulation.

Interactions between soluble enzymes and subcellular structure.

A generalized theory of the transition time for sequential enzyme reactions.

The evolution of enzyme kinetic power.

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187-190

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10.1042/BJ2570187

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