Crystal structure of Escherichia coli thioesterase I/protease I/lysophospholipase L1: consensus sequence blocks constitute the catalytic center of SGNH-hydrolases through a conserved hydrogen bond network (Q27641632)

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English	Crystal structure of Escherichia coli thioesterase I/protease I/lysophospholipase L1: consensus sequence blocks constitute the catalytic center of SGNH-hydrolases through a conserved hydrogen bond network	scientific article

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scholarly article

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Crystal structure of Escherichia coli thioesterase I/protease I/lysophospholipase L1: consensus sequence blocks constitute the catalytic center of SGNH-hydrolases through a conserved hydrogen bond network (English)

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crystal structure

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Escherichia coli

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3

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author name string

Yu-Chih Lo

1

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Su-Chang Lin

2

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Yen-Chywan Liaw

4

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language of work or name

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publication date

11 July 2003

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Journal of Molecular Biology

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330

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3

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539-51

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Isolation and some propeties of a proteolytic enzyme from Escherichia coli (protease I).

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The thioesterase I of Escherichia coli has arylesterase activity and shows stereospecificity for protease substrates.

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The Escherichia coli pldC gene encoding lysophospholipase L(1) is identical to the apeA and tesA genes encoding protease I and thioesterase I, respectively

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"Protease I" of Escherichia coli functions as a thioesterase in vivo

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