Structure and enzymic properties of phospholipase A from porcine pancreas

Structural basis of the chiral selectivity of Pseudomonas cepacia lipase.

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Crystal structure of cutinase covalently inhibited by a triglyceride analogue.

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Phosphonate analogues of triacylglycerols are potent inhibitors of lipase.

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Competitive inhibition of lipolytic enzymes. XI. Estimation of the interfacial dissociation constants of porcine pancreatic phospholipase A2 for substrate and inhibitor in the absence of detergents.

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Structure and enzymic properties of phospholipase A from porcine pancreas

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Structural basis of the chiral selectivity of Pseudomonas cepacia lipase.

Crystal structure of cutinase covalently inhibited by a triglyceride analogue.

Phosphonate analogues of triacylglycerols are potent inhibitors of lipase.

Solution structure of porcine pancreatic phospholipase A2.

Competitive inhibition of lipolytic enzymes. XI. Estimation of the interfacial dissociation constants of porcine pancreatic phospholipase A2 for substrate and inhibitor in the absence of detergents.

Cutinase from Fusarium solani pisi hydrolyzing triglyceride analogues. Effect of acyl chain length and position in the substrate molecule on activity and enantioselectivity.

Characterization of FAD binding to the apo-form of diflavin-linked disulfide oxidoreductase derived from cyanobacterium Synechocystis sp. PCC6803.

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