Title : Acyl-chain specificity of human milk bile-salt-activated lipase.

Pub. Date : 1991 Oct 1

PMID : 1930149






3 Functional Relationships(s)
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1 I further examined the reaction kinetics of BAL with water-soluble short-chain esters of p-nitrophenol. Esters carboxyl ester lipase Homo sapiens
2 The fact that butyrate ester has the optimum acyl chain to be a substrate of BAL can be attributed to its acyl-chain length being long enough for interaction with the active centre of BAL and short enough to provide adequate positioning of the ester bond for transition state complex formation. Esters carboxyl ester lipase Homo sapiens
3 The fact that butyrate ester has the optimum acyl chain to be a substrate of BAL can be attributed to its acyl-chain length being long enough for interaction with the active centre of BAL and short enough to provide adequate positioning of the ester bond for transition state complex formation. Esters carboxyl ester lipase Homo sapiens