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|標題:||Enhanced preference for pi-bond containing substrates is correlated to Pro110 in the substrate-binding tunnel of Escherichia coli thioesterase I/protease I/lysophospholipase L-1|
|期刊/報告no：:||Biochimica Et Biophysica Acta-Proteins and Proteomics, Volume 1774, Issue 8, Page(s) 959-967.|
|摘要:||Escherichia coli thioesterase I/protease I/lysophospholipase L, (TAP) possesses multifunctional enzyme with thioesterase, esterase, arylesterase, protease, and lysophospholipase activities. Leu109, located at the substrate-binding tunnel, when substituted with proline (Pro) in TAP, shifted the substrate-preference from medium-to-long acyl chains to shorter acyl chains of triglyceride and p-nitrophenyl ester, and increased the preference for aromatic-amino acid-derived esters. In the three-dimensional TAP structures, the only noticeable alteration of backbone and side chain conformation was located at the downstream Pro 110-Alal 23 region rather than at Pro 109 itself The residue Pro I 10, adjacent to Leu 109 or Pro 109, was found to contribute to the substrate preference of TAP enzymes for esters containing acyl groups with pi bond(s) or aromatic group(s). Some of the interactions between the enzyme protein and the substrate may be contributed by an attractive force between the Pro I 10 C-H donor and the substrate pi-acceptor. (c) 2007 Elsevier B.V. All rights reserved.|
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