Abstract —The inhibition by catechols and biopterin of tyrosine hydroxylase from guineapig caudate nuclei has been examined. Inhibitory constants of 10–20 μm were obtained for dopamine and noradrena‐line and 150–250 μmfor l‐DOPA and dihydroxyphenylacetic acid. When examined under similar conditions homovanillic acid was found not to be inhibitory. Using an acetone dried powder as the source of tyrosine hydroxylase no change in Km or Vmax was observed when cyclic AMP or Ca2+ were added to the medium. Enzyme mechanisms and a possible explanation of the mechanisms controlling catechol synthesis are discussed.
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Mann et al. (1979) studied this question.
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