Abstract
The fatty acid and positional hydrolytic selectivity of lipid acyl hydrolase (UH; patatin) isolatedfi.om potato tubers was determined for acylglycerol and phospholipid substrates. LAH was about 3-foM more selective for decanoyl residues over other acyl groups of 8-18 carbons for partial glyceride substrates. For both mono- and diacylglycerols, UHpreferred substrates with primary (sn1 (3)-) ester linkages, indicating a regiobias for these sites over sn-2-linked acyl groups. Similarly, hydrolytic activity on phospholipid substrates was 5- to IOfold faster on sn-1-palmitoyl. sn-2-lysophospholipids than on intact phospholipids, indicating a preference for either lysophospholipids or sn-1-acyl sites, or both. LAH activity on partial glycerides was not activated by CaC12 and had a greater temperature optimwn relative to LAHactivity on phospholipid substrates. These differences are likely based on differences in forces and structural features conferring envme-substrate recognition for these substrates within a common active site.
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