| Title : NMR studies of the hydrogen bonds involving the catalytic triad of Escherichia coli thioesterase\/protease I - Tyukhtenko_2002_FEBS.Lett_528_203 |
| Author(s) : Tyukhtenko SI , Litvinchuk AV , Chang CF , Leu RJ , Shaw JF , Huang TH |
| Ref : FEBS Letters , 528 :203 , 2002 |
|
Abstract :
Escherichia coli thioesterase/protease I (TEP-I) is a lipolytic enzyme of the serine protease superfamily with Ser(10), Asp(154) and His(157) as the catalytic triad residues. Based on comparison of the low-field (1)H 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 His(157)-N(delta1)H, Ser(10)-O(gamma)H and His(157)-N(epsilon2)H, respectively. Thus, the presence of a strong Asp(154)-His(157) hydrogen bond in free TEP-I was observed. However, Ser(10)-O(gamma)H was shown to form a H-bond with a residue other than His(157)-N(epsilon2). |
| PubMedSearch : Tyukhtenko_2002_FEBS.Lett_528_203 |
| PubMedID: 12297305 |
Tyukhtenko SI, Litvinchuk AV, Chang CF, Leu RJ, Shaw JF, Huang TH (2002)
NMR studies of the hydrogen bonds involving the catalytic triad of Escherichia coli thioesterase\/protease I
FEBS Letters
528 :203
Tyukhtenko SI, Litvinchuk AV, Chang CF, Leu RJ, Shaw JF, Huang TH (2002)
FEBS Letters
528 :203