A comparative study of the kinetics and stereochemistry of the serine hydroxymethyltransferase- and tryptophan synthase-catalysed exchange of the pro-2R and pro-2S protons of glycine
Malthouse J.P.G., Milne J.J., Gariani L.S. A comparative study of the kinetics and stereochemistry of the serine hydroxymethyltransferase- and tryptophan synthase-catalysed exchange of the pro-2R and pro-2S protons of glycine. Biochem. J. 274:1991;807-812.
Factors affecting the stereospecificity and catalytic efficiency of the tryptophan synthase-catalysed exchange of the pro-2R and pro-2S protons of glycine
Milne J.J., Malthouse J.P.G. Factors affecting the stereospecificity and catalytic efficiency of the tryptophan synthase-catalysed exchange of the pro-2R and pro-2S protons of glycine. Biochem. J. 311:1995;1015-1019.
The effect of different amino acid side chains on the stereospecificity and catalytic efficiency of the tryptophan synthase-catalysed exchange of the alpha-protons of amino acids
Milne J.J., Malthouse J.P.G. The effect of different amino acid side chains on the stereospecificity and catalytic efficiency of the tryptophan synthase-catalysed exchange of the alpha-protons of amino acids. Biochem. J. 314:1996;787-791.
The effect of histidine-228 on the catalytic efficiency and stereospecificity of the serine hydroxymethyltransferase catalysed exchange of the alpha-protons of amino acids
Fitzpatrick T.B., Malthouse J.P.G. The effect of histidine-228 on the catalytic efficiency and stereospecificity of the serine hydroxymethyltransferase catalysed exchange of the alpha-protons of amino acids. Biochim. Biophys. Acta. 1386:1998;220-226.
A substrate-induced change in the stereospecificity of the serine-hydroxymethyltransferase-catalysed exchange of the alpha-protons of amino acids - Evidence for a second catalytic site
Fitzpatrick T.B., Malthouse J.P.G. A substrate-induced change in the stereospecificity of the serine-hydroxymethyltransferase-catalysed exchange of the alpha-protons of amino acids - evidence for a second catalytic site. Eur. J. Biochem. 252:1998;113-117.
The aspartate aminotransferase-catalysed exchange of the α-protons of aspartate and glutamate: The effects of the R386A and R292V mutations on this exchange reaction
Mahon M.M., Graber R., Christen P., Malthouse J.P.G. The aspartate aminotransferase-catalysed exchange of the α-protons of aspartate and glutamate: the effects of the R386A and R292V mutations on this exchange reaction. Biochim. Biophys. Acta. 1434:1999;191-201.
The pyridoxal-5′-phosphate-dependent catalytic antibody 15A9: Its efficiency and stereospecificity in catalysing the exchange of the alpha-protons of glycine
Mahon M.M., Gramatikova S.I., Christen P., Fitzpatrick T.B., Malthouse J.P.G. The pyridoxal-5′-phosphate-dependent catalytic antibody 15A9: its efficiency and stereospecificity in catalysing the exchange of the alpha-protons of glycine. FEBS Lett. 427:1998;74-78.
