PMID:12297305

Citation	Tyukhtenko, SI, Litvinchuk, AV, Chang, CF, Leu, RJ, Shaw, JF and Huang, TH (2002) NMR studies of the hydrogen bonds involving the catalytic triad of Escherichia coli thioesterase/protease I. FEBS Lett. 528:203-6
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).
Links	PubMed
Keywords	Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Hydrogen Bonding; Hydrogen-Ion Concentration; Lysophospholipase/chemistry; Lysophospholipase/genetics; Lysophospholipase/metabolism; Nuclear Magnetic Resonance, Biomolecular; Periplasmic Proteins/chemistry; Periplasmic Proteins/genetics; Periplasmic Proteins/metabolism; Point Mutation; Protons; Serine/chemistry
edit table

Significance

You can help EcoliWiki by summarizing why this paper is useful

You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.

Add links to pages that link here (e.g. gene, product, method pages)

See Help:References for how to manage references in EcoliWiki.