The polar interactions between pancreatic lipase, colipase and the triglyceride substrate

Borgström, Bengt; Donnér, Jakob

doi:10.1016/0014-5793(77)80633-9

Cited by 19 publications

(1 citation statement)

References 11 publications

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“…According to Rogalska et al [46], stereoselectivity of diacylglycerol hydrolysis by RML, LPL, Candida antartica B lipase (CAB), and human gastric lipase (HGL) increased with decreasing surface pressure in monolayers at the aidwater interface. Pancreatic lipase was shown to bind more easily to triacylglycer-01s as compared to tri-0-alkylglycerols [47]. Therefore, possible effects due to differences in emulsion that might arise as a consequence of distinct hydrophobicity of the various substrates had to be considered.…”

Section: Nomentioning

confidence: 99%

Stereoselectivity of Microbial Lipases

Stadler

Kovac

Haalck

et al. 1995

European Journal of Biochemistry

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In the present study, the stereoselectivity of purified lipases from Candida rugosa, Chromobacterium viscosum, Pseudomonas species and Rhizopus arrhizus towards triacylglycerols in comparison to various structural analogs were investigated. Different triacylglycerol analogs with distinct polarities at position sn-2 of the glycerol backbone (1,3-diacy1-2-X-glycerol, where 2-X = 2-acyloxy, 2-alkyloxy, 2-deoxy-2-alkyl, or 2-deoxy-2-phenyl) were synthesized. Substrate hydrophobicity and steric requirement was modified by variation of the alkyl and acyl chain length. Hydrolysis of these substrates demonstrated that minor structural variations at C2 of triacylglycerol strongly affect the stereoselectivity of the lipases tested. It was noteworthy that the variation of substrate structure did not only affect the quantity of stereoselectivity expressed as percentage enantiomeric excess, but also resulted in a reversal of stereopreference in some cases. Replacement of the acylester in position 2 of glycerol by a non-ester-linked aliphatic moiety shifted the preference of Chromobacterium viscosum lipase from sn-3 to sn-1 . Lipases from Chromobacterium viscosum, Pseudomonas species and Rhizopus arrhizus exhibited sn-3 preference with 2-deoxy-2-phenyl analogs, while towards substrates with a 2-deoxy-2-alkyl moiety sn-1 stereobias was recorded. Candida rugosa lipase was rather insensitive to substrate variations concerning the polarity at position 2 of the glycerol backbone. However, variation of the acyl chain length significantly influenced stereoselectivity of this lipase.

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Section: Nomentioning

confidence: 99%

Stereoselectivity of Microbial Lipases

Stadler

Kovac

Haalck

et al. 1995

European Journal of Biochemistry

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Computational study of colipase interaction with lipid droplets and bile salt micelles

et al. 2008

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Colipase is a key element in the lipase-catalyzed hydrolysis of dietary lipids. Although devoid of enzymatic activity, colipase promotes the pancreatic lipase activity in physiological intestinal conditions by anchoring the enzyme at the surface of lipid droplets. Analysis of structures of NMR colipase models and simulations of their interactions with various lipid aggregates, lipid droplet, and bile salt micelle, were carried out to determine and to map the lipid binding sites on colipase. We show that the micelle and the oil droplet bind to the same side of colipase 3D structure, mainly the hydrophobic fingers. Moreover, it appears that, although colipase has a single direction of interaction with a lipid interface, it does not bind in a specific way but rather oscillates between different positions. Indeed, different NMR models of colipase insert different fragments of sequence in the interface, either simultaneously or independently. This supports the idea that colipase finger plasticity may be crucial to adapt the lipase activity to different lipid aggregates.

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Triacylglycerol lipase

Schomburg¹,

Salzmann²

1991

Enzyme Handbook 3

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The polar interactions between pancreatic lipase, colipase and the triglyceride substrate

Cited by 19 publications

References 11 publications

Stereoselectivity of Microbial Lipases

Stereoselectivity of Microbial Lipases

Computational study of colipase interaction with lipid droplets and bile salt micelles

Triacylglycerol lipase

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