Earticle

초록

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˚.

저자

• Seung Bum Kim [ Department of Molecular Science and Technology, Ajou University ]
• Sang bum Joo [ Department of Molecular Biology, School of Medicine, Sungkyunkwan University ]
• Yeon woo Ryu [ Department of Molecular Science and Technology, Ajou University ]
• Kyeong Kyu Kim [ Department of Molecular Biology, School of Medicine, Sungkyunkwan University ]
• Doo hun Kim [ Department of Molecular Science and Technology, Ajou University ]

참고문헌

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간행물

표지보기 관심저널 등록

• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576