3-D Structure and Activity of Lipase

DOI Web Site Web Site 35 References

Bibliographic Information

Other Title
  • リパーゼの立体構造と活性
  • リパーゼ ノ リッタイ コウゾウ ト カッセイ

Search this article

Description

One long recognized feature of lipases is the phenomenon termed “interfacial activation”, which refers to the fact that they exert their maximum activities when the substrate concentration exceeds its critical micelle concentration. Little was known about the molecular basis of the lipase reaction mechanism including the interfacial activation until 1990 when highresolution crystal structures of human pancreatic and Rhizomucor miehei lipases were reported. Both enzymes were shown to have triads of Ser, His, andAsp, reminiscent of the catalytic triads of chymotrypsin and subtilisin. These putative catalytic centers were not exposed to the solvent, but were buried under surface loops, suggesting significant conformational changes before the catalytic event. This review assesses current progress in crystallographic studies of lipases, which lead to understanding of the structure-function relationships of the enzymes.

Journal

References(35)*help

See more

Details 詳細情報について

Report a problem

Back to top