Title : Probing of active site structure of lipoprotein lipase: contribution of activation entropy in the catalysis.

Pub. Date : 1994 Apr 14

PMID : 8155728






3 Functional Relationships(s)
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1 In this study, I have utilized the chromogenic short-chain esters of p-nitrophenol as substrates for probing the active site structure of lipoprotein lipase (LPL). Esters lipoprotein lipase Homo sapiens
2 In this study, I have utilized the chromogenic short-chain esters of p-nitrophenol as substrates for probing the active site structure of lipoprotein lipase (LPL). Esters lipoprotein lipase Homo sapiens
3 The fact that butyrate ester has the optimum acyl-chain length to be a substrate of LPL can be attributed to its chain length being long enough for optimum interaction with the active site His-Ser-Asp triad in forming the transition state complex; yet it is short enough to provide freedom for optimum positioning of the ester bond for transition state complex formation. Esters lipoprotein lipase Homo sapiens