NMR studies of the hydrogen bonds involving the catalytic triad of Escherichia coli thioesterase/protease I

Sergiy I. Tyukhtenko; Alexandra V. Litvinchuk; Chi Fon Chang; Ruey Jyh Leu; Jei Fu Shaw; Tai Huang Huang

doi:10.1016/S0014-5793(02)03308-2

NMR studies of the hydrogen bonds involving the catalytic triad of Escherichia coli thioesterase/protease I

Sergiy I. Tyukhtenko, Alexandra V. Litvinchuk, Chi Fon Chang, Ruey Jyh Leu, Jei Fu Shaw, Tai Huang Huang^*

^*此作品的通信作者

研究成果: 雜誌貢獻 › 期刊論文 › 同行評審

15 引文斯高帕斯（Scopus）

摘要

Escherichia coli thioesterase/protease I (TEP-I) is a lipolytic enzyme of the serine protease superfamily with Ser¹⁰, Asp¹⁵⁴ and His¹⁵⁷ as the catalytic triad residues. Based on comparison of the low-field ¹H nuclear magnetic resonance spectra of two mutants (S10G and S12G) and two transition state analogue complexes we have assigned the exchangeable proton resonances at 16.3 ppm, 14.3 ppm, and 12.8 ppm at pH 3.5 to His¹⁵⁷-N^δ1H, Ser¹⁰-O^γH and His¹⁵⁷-N^ε2H, respectively. Thus, the presence of a strong Asp¹⁵⁴-His¹⁵⁷ hydrogen bond in free TEP-I was observed. However, Ser¹⁰-O^γH was shown to form a H-bond with a residue other than His¹⁵⁷-N^ε2.

原文	英語
頁（從 - 到）	203-206
頁數	4
期刊	FEBS Letters
卷	528
發行號	1-3
DOIs	https://doi.org/10.1016/S0014-5793(02)03308-2
出版狀態	已發佈 - 2002 9月 25
對外發佈	是

ASJC Scopus subject areas

生物物理學
結構生物學
生物化學
分子生物學
遺傳學
細胞生物學

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title = "NMR studies of the hydrogen bonds involving the catalytic triad of Escherichia coli thioesterase/protease I",

abstract = "Escherichia coli thioesterase/protease I (TEP-I) is a lipolytic enzyme of the serine protease superfamily with Ser10, Asp154 and His157 as the catalytic triad residues. Based on comparison of the low-field 1H nuclear magnetic resonance spectra of two mutants (S10G and S12G) and two transition state analogue complexes we have assigned the exchangeable proton resonances at 16.3 ppm, 14.3 ppm, and 12.8 ppm at pH 3.5 to His157-Nδ1H, Ser10-OγH and His157-Nε2H, respectively. Thus, the presence of a strong Asp154-His157 hydrogen bond in free TEP-I was observed. However, Ser10-OγH was shown to form a H-bond with a residue other than His157-Nε2.",

keywords = "Lipolytic enzyme, Low barrier hydrogen bond, Nuclear magnetic resonance, Serine protease, Thioesterase",

author = "Tyukhtenko, {Sergiy I.} and Litvinchuk, {Alexandra V.} and Chang, {Chi Fon} and Leu, {Ruey Jyh} and Shaw, {Jei Fu} and Huang, {Tai Huang}",

note = "Funding Information: We thank Dr. Yen-Chyan Liaw for the use of the X-ray crystal structure coordinates of TEP-I prior to publication. This work was supported by Grants from the National Science Council (NSC91-2113-M-001-038) (T.-H.H.) and Academia Sinica (T.-H.H. and J.-F.S.) of the Republic of China.",

year = "2002",

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doi = "10.1016/S0014-5793(02)03308-2",

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T1 - NMR studies of the hydrogen bonds involving the catalytic triad of Escherichia coli thioesterase/protease I

AU - Tyukhtenko, Sergiy I.

AU - Litvinchuk, Alexandra V.

AU - Chang, Chi Fon

AU - Leu, Ruey Jyh

AU - Shaw, Jei Fu

AU - Huang, Tai Huang

N1 - Funding Information: We thank Dr. Yen-Chyan Liaw for the use of the X-ray crystal structure coordinates of TEP-I prior to publication. This work was supported by Grants from the National Science Council (NSC91-2113-M-001-038) (T.-H.H.) and Academia Sinica (T.-H.H. and J.-F.S.) of the Republic of China.

PY - 2002/9/25

Y1 - 2002/9/25

N2 - Escherichia coli thioesterase/protease I (TEP-I) is a lipolytic enzyme of the serine protease superfamily with Ser10, Asp154 and His157 as the catalytic triad residues. Based on comparison of the low-field 1H nuclear magnetic resonance spectra of two mutants (S10G and S12G) and two transition state analogue complexes we have assigned the exchangeable proton resonances at 16.3 ppm, 14.3 ppm, and 12.8 ppm at pH 3.5 to His157-Nδ1H, Ser10-OγH and His157-Nε2H, respectively. Thus, the presence of a strong Asp154-His157 hydrogen bond in free TEP-I was observed. However, Ser10-OγH was shown to form a H-bond with a residue other than His157-Nε2.

AB - Escherichia coli thioesterase/protease I (TEP-I) is a lipolytic enzyme of the serine protease superfamily with Ser10, Asp154 and His157 as the catalytic triad residues. Based on comparison of the low-field 1H nuclear magnetic resonance spectra of two mutants (S10G and S12G) and two transition state analogue complexes we have assigned the exchangeable proton resonances at 16.3 ppm, 14.3 ppm, and 12.8 ppm at pH 3.5 to His157-Nδ1H, Ser10-OγH and His157-Nε2H, respectively. Thus, the presence of a strong Asp154-His157 hydrogen bond in free TEP-I was observed. However, Ser10-OγH was shown to form a H-bond with a residue other than His157-Nε2.

KW - Lipolytic enzyme

KW - Low barrier hydrogen bond

KW - Nuclear magnetic resonance

KW - Serine protease

KW - Thioesterase

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NMR studies of the hydrogen bonds involving the catalytic triad of Escherichia coli thioesterase/protease I

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