The crystal structure of a triacylglycerol lipase from Pseudomonas cepacia reveals a highly open conformation in the absence of a bound inhibitor

Kyeong Kyu Kim, Hyun Kyu Song, Dong Hae Shin, Kwang Yeon Hwang, Se Won Sun

Research output: Contribution to journalArticlepeer-review

300 Scopus citations


Background: Lipases, a family of enzymes which catalyze the hydrolysis of triglycerides, are widely distributed in many organisms. True lipases are distinguished from esterases by the characteristic interfacial activation they exhibit at an oil-water interface. Lipases are one of the most frequently used biocatalysts for organic reactions performed under mild conditions. Their biotechnological applications include food and oil processing and the preparation of chiral intermediates for the synthesis of enantiomerically pure pharmaceuticals. Recent structural studies on several lipases have provided some clues towards understanding the mechanisms of hydrolytic activity, interfacial activation, and stereoselectivity. This study was undertaken in order to provide structural information on bacterial lipases, which is relatively limited in comparison to that on the enzymes from other sources. Results: We have determined the crystal structure of a triacylglycerol lipase from Pseudomonas cepacia (PcL) in the absence of a bound inhibitor using X-ray crystallography. The structure shows the lipase to contain an α/β-hydrolase fold and a catalytic triad comprising of residues Ser87, His286 and Asp264. The enzyme shares several structural features with homologous lipases from Pseudomonas glumae (PgL) and Chromobacterium viscosum (CvL), including a calcium-binding site. The present structure of PcL reveals a highly open conformation with a solvent-accessible active site. This is in contrast to the structures of PgL and PcL in which the active site is buried under a closed or partially opened 'lid', respectively. Conclusions: PcL exhibits some structural features found in other lipases. The presence of the Ser-His-Asp catalytic triad, an oxyanion hole, and the opening of a helical lid suggest that this enzyme shares the same mechanisms of catalysis and interfacial activation as other lipases. The highly open conformation observed in this study is likely to reflect the activated form of the lipase at an oil-water interface. The structure suggests that the interfacial activation of bacterial lipases involves the reorganization of secondary structures and a large movement of the lid to expose the active site. This is similar to the mechanism described for other well characterized fungal and mammalian lipases.

Original languageEnglish
Pages (from-to)173-185
Number of pages13
Issue number2
StatePublished - 1997

Bibliographical note

Funding Information:
We thank MEM Noble and LN Johnson for supplying the coordinates of PgL, and D Ollis, Y Kim, and CH Chang for comments and assistance. We also thank the Korea Ministry of Education (International Cooperative Research Program), the Center for Molecular Catalysis, the Korea Sanhak Foundation, and the Basic Sciences Research Institute, MOE, (BSRI-96-3418) for financial support. The publication cost was supported in part by the Research Institute of Molecular Science. The X-ray equipment was provided by the Inter-University Center for Natural Science Research Facilities at Seoul National University. The X-ray equipment was supported in part by the Korea Science Engineering Foundation Specialization Support Fund.


  • Pseudomonas cepacia
  • X-ray structure
  • lipase


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