earticle

영어

Ketoprofen,anon-steroidalanti-inflammatorydrug, inhibits the synthesis of prostaglandin.
Previously, a novel hydrolase(Est25) with high ketoprofen specificity was identified using a
metagenomic library from environmental samples. Interestingly, the primary sequence of Est25
shows similarities to members of the hormone-sensitive lipase (HSL) family such as brefeldin A
esterase (BFAE, 48% identity) from B acillus subtilis, a carboxylesterase (AFEST, 33%) from
Archaeoglobus fulgidus, and a carboxyesterase (EST2, 30%) from Alicyclobacillus acidocaldarius.
The HSL family is a class of enzymes that mobilize fatty acids for energy metabolism in
adipose tissue. Although the members of the HSL family share an α/β-hydrolase fold, each
structure has its own arrangement of α-helices and β-sheets. Therefore, the crystal structure of
Est25 is essential to understand the enzyme’s catalytic mechanism and substrate specificities for
(R,S)-ketoprofen at the molecular level. In addition, the Est25 crystal structure is expected to
provide structural and functional insights into the HSL family. Est25 was crystallized from 2.4M
sodium malonate, pH7.0, and X-ray diffraction data to 1.49 Å were collected using synchrotron
radiation. The crystals belong to the monoclinic space group C2 with unit cell parameters a =
197.8 Å , b = 95.2 Å , c = 99.4 Å , and β = 97.1˚.