A major group of lipolytic enzymes typified by pancreatic lipase consists of nonspecific esterases probably of the serinehistidine type.
Another group, the phospholipases 2 of exocrine glands, are calcium activated and have exacting stereo-specific substrate requirements.
The enzymes of both groups hydrolyze water-insoluble esters.
They must not only adsorb to oil—water or micelle—water interfaces
but also must position their active sites toward the matrix (oil droplet, micelle, or membrane) in which the substrate molecules are imbedded,
the “supersubstrate” It is postulated that lipolytic enzymes are hydrolases that have developed supersubstrate binding sites for attachment and orientation toward lipids.
Such a binding site, which is topographically distinct from the substrate binding sites of the reactive center,
may have hydrophobic or electrostatic character.
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