The effect of histidine-228 on the catalytic efficiency and stereospecificity of the serine hydroxymethyltransferase catalysed exchange of the alpha-protons of amino acids.

doi:10.1016/s0167-4838(98)00112-5

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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...

Topics

Asparagine
Coenzymes
Glycine
Glycine Hydroxymethyltransferase
Histidine
Models, Chemical
Mutation
Protons
Pyridoxal Phosphate
Stereoisomerism
Substrate Specificity

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