Thermostable carboxylesterases from hyperthermophiles

被引：17

作者：

Atomi, H ^{[1
]}

Imanaka, T ^{[1
]}

机构：

[1] Kyoto Univ, Grad Sch Engn, Dept Synthet Chem & Biol Chem, Nishikyo Ku, Kyoto 6158510, Japan

来源：

TETRAHEDRON-ASYMMETRY | 2004年 / 15卷 / 18期

关键词：

D O I：

10.1016/j.tetasy.2004.07.054

中图分类号：

O61 [无机化学];

学科分类号：

070301 ; 081704 ;

摘要：

This report focuses on the lipolytic enzymes from hyperthermophiles. Most of the enzymes characterized to date are carboxylesterases that are structurally related to the hormone-sensitive lipase family, and prefer medium chain (acyl chain length of 6) p-nitrophenyl substrates. The presence of a GGGX motif in these carboxylesterases suggest the ability of these enzymes to catalyze the hydrolysis of tertiary alcohol esters. We will also introduce studies that have examined the effects of temperature and organic solvents on the catalytic efficiency and enantioselectivity of the thermostable carboxylesterase from Sulfolobus solfataricus. Finally, a BLAST search of the hyperthermophile genome sequences reveal candidate genes that may encode novel, thermostable esterases. (C) 2004 Elsevier Ltd. All rights reserved.

引用

页码：2729 / 2735

页数：7

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