Interfacial enzymology of glycerolipid hydrolases: lessons from secreted phospholipases A2.
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.
Gelb
M H
MH
Department of Chemistry, University of Washington, Seattle 98195, USA.
Jain
M K
MK
Hanel
A M
AM
Berg
O G
OG
D000818:Animals; D001665:Binding Sites; D002118:Calcium / Q000378:metabolism; D002384:Catalysis; D006801:Humans; D006868:Hydrolysis; D007700:Kinetics; D050356:Lipid Metabolism; D008055:Lipids / Q000737:chemistry; D015394:Molecular Structure; D010741:Phospholipases A / Q000737:chemistry / Q000378:metabolism*; D054467:Phospholipases A2; D013379:Substrate Specificity
D008055:Lipids; D010741:Phospholipases A; D054467:Phospholipases A2; D002118:Calcium