1OIL

STRUCTURE OF LIPASE

1OIL の概要

• エントリーDOI: 10.2210/pdb1oil/pdb
• 分子名称: LIPASE, CALCIUM ION (3 entities in total)
• 機能のキーワード: hydrolase, triacylglycerol lipase
• 由来する生物種: Burkholderia cepacia
• 細胞内の位置: Secreted : P22088
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 66381.69

構造登録者

Kim, K.K.,Song, H.K.,Shin, D.H.,Suh, S.W. (登録日: 1996-12-06, 公開日: 1997-05-15, 最終更新日: 2024-11-06)

主引用文献

Kim, K.K.,Song, H.K.,Shin, D.H.,Hwang, K.Y.,Suh, S.W.
The crystal structure of a triacylglycerol lipase from Pseudomonas cepacia reveals a highly open conformation in the absence of a bound inhibitor.
Structure, 5:173-185, 1997

PubMed Abstract: . 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.

PubMed: 9032073
DOI: 10.1016/S0969-2126(97)00177-9

実験手法

X-RAY DIFFRACTION (2.1 Å)