INTERFACIAL ENZYMOLOGY OF GLYCEROLIPID HYDROLASES: Lessons from Secreted Phospholipases A2
Autor: | Otto G. Berg, Michael H. Gelb, Arthur M. Hanel, Mahendra K. Jain |
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Rok vydání: | 1995 |
Předmět: |
Kinetics
Phospholipase Biochemistry Catalysis Phospholipases A Substrate Specificity Phospholipase A2 Animals Humans Binding site chemistry.chemical_classification Binding Sites Molecular Structure biology Chemistry Hydrolysis Aqueous two-phase system Substrate (chemistry) Lipid Metabolism Lipids Phospholipases A2 Membrane Enzyme Biophysics biology.protein Calcium |
Zdroj: | Annual Review of Biochemistry. 64:653-688 |
ISSN: | 1545-4509 0066-4154 |
DOI: | 10.1146/annurev.bi.64.070195.003253 |
Popis: | Interfacial enzymes operate at an organized interface such as lipid aggregates in contact with the aqueous phase. The enzyme phospholipase A2 is a well studied interfacial enzyme, and a discussion of its behavior at interfaces is the topic of this review. Knowledge gained from studies of phospholipases A2 can be applied toward the quantitative analysis of other interfacial enzymes. The kinetic analysis of these enzymes is greatly simplified if one establishes certain experimental conditions that limit the exchange of enzyme and substrate between different substrate aggregates. With such constraints, the kinetics can be analyzed in terms of classical Michaelis-Menten theory adopted for the action of enzymes at interfaces. It is also possible to describe other enzyme properties such as inhibition and substrate preferences in a meaningful way using formalism that is well known in solution-phase enzymology. |
Databáze: | OpenAIRE |
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