PMID: 2508625Aug 1, 1989Paper

Further kinetic and molecular characterization of an extremely heat-stable carboxylesterase from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius

The Biochemical Journal
H Sobek, H Görisch

Abstract

The carboxylesterase (serine esterase, EC 3.1.1.1) from Sulfolobus acidocaldarius was purified 940-fold to homogeneity by an improved purification procedure with a yield of 57%. In the presence of alcohols the enzyme catalyses the transfer of the substrate acyl group to alcohols in parallel to hydrolysis. The results show the existence of an alcohol-binding site and a competitive partitioning of the acyl-enzyme intermediate between water and alcohols. Aniline acts also as a nucleophilic acceptor for the acyl group. On the basis of titration with diethyl p-nitrophenyl phosphate, a number of four active centres is determined for the tetrameric carboxylesterase. The sequence of 20 amino acid residues at the esterase N-terminus and the amino acid composition are reported.

Citations

Jun 9, 2004·Applied and Environmental Microbiology·Young J ChoiByong H Lee
Jul 31, 2002·Applied and Environmental Microbiology·Yuji HottaTadayuki Imanaka
Apr 13, 2010·Acta Biochimica Et Biophysica Sinica·Shanshan YuYan Feng
Aug 19, 2011·Applied Microbiology and Biotechnology·Yuxia MeiQunxin She
Jun 23, 2009·Extremophiles : Life Under Extreme Conditions·Mark LevissonServé W M Kengen
Jun 5, 2021·Colloids and Surfaces. B, Biointerfaces·Ummie Umaiera Mohd JohanMohd Shukuri Mohamad Ali
Sep 7, 2021·Applied Microbiology and Biotechnology·Siti Hajar HamdanThean Chor Leow

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