Enzyme kinetic and molecular modelling studies of sulphur-containing substrates of phenylalanine 4-monooxygenase

Previous investigations into the binding of substrates/cofactors to the PAH active site have only concentrated on Phe, thienylalanine and BH4. This is the first reported investigation to model aliphatic thioether amino acid substrates to PAH. The clearance of the thioether substrates (4.82-79.09% of...

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Veröffentlicht in:	Journal of enzyme inhibition and medicinal chemistry 2008-01, Vol.23 (6), p.958-963
Hauptverfasser:	Patel, N. G., Iliadou, C., Boonyapiwat, B., Barlow, D. J., Forbes, B., Mitchell, S. C., Steventon, G. B.
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Catalytic Domain computer modelling Humans inhibition Kinetics Models, Molecular Molecular Conformation Phenylalanine 4-monooxygenase Phenylalanine Hydroxylase - metabolism Rats S-oxidation Substrate Specificity Sulfur - analysis Sulfur - metabolism thioether substrates
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