Article
The effect of histidine-228 on the catalytic efficiency and stereospecificity of the serine hydroxymethyltransferase catalysed exchange of the alpha-protons of amino acids.
Biochimica et biophysica acta - 28 Jul 1998
Fitzpatrick T B, Malthouse J P
Abstract excerpt
13C-NMR has been used to determine how replacing the histidine-228 residue of serine hydroxymethyltransferase (EC 2.1.2.1) by an asparagine residue effects the catalysis of the hydrogen-deuterium exchange of the alpha-protons of [2-13C]glycine at pH 7.8. The H228N mutation did not lead to a large change in the stereospecificity of the first order exchange rates of the alpha-protons of glycine both in the presence...
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