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

Research output: Contribution to journalArticle

14 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)203-206
Number of pages4
JournalFEBS Letters
Volume528
Issue number1-3
DOIs
Publication statusPublished - 2002 Sep 25

Fingerprint

Palmitoyl-CoA Hydrolase
Escherichia coli
Hydrogen
Hydrogen bonds
Peptide Hydrolases
Nuclear magnetic resonance
Serine Proteases
Protons
Magnetic Resonance Spectroscopy
Enzymes

Keywords

  • Lipolytic enzyme
  • Low barrier hydrogen bond
  • Nuclear magnetic resonance
  • Serine protease
  • Thioesterase

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

NMR studies of the hydrogen bonds involving the catalytic triad of Escherichia coli thioesterase/protease I. / Tyukhtenko, Sergiy I.; Litvinchuk, Alexandra V.; Chang, Chi Fon; Leu, Ruey Jyh; Shaw, Jei Fu; Huang, Tai-huang.

In: FEBS Letters, Vol. 528, No. 1-3, 25.09.2002, p. 203-206.

Research output: Contribution to journalArticle

Tyukhtenko, Sergiy I. ; Litvinchuk, Alexandra V. ; Chang, Chi Fon ; Leu, Ruey Jyh ; Shaw, Jei Fu ; Huang, Tai-huang. / NMR studies of the hydrogen bonds involving the catalytic triad of Escherichia coli thioesterase/protease I. In: FEBS Letters. 2002 ; Vol. 528, No. 1-3. pp. 203-206.
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AU - Chang, Chi Fon

AU - Leu, Ruey Jyh

AU - Shaw, Jei Fu

AU - Huang, Tai-huang

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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.

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