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- W1982908077 abstract "Abstract 1. 1. The inhibition of 5-HTP decarboxylation by 3,4′-dihydroxy-3′-carboxychalcone, 3,4,4′-trihydroxy-3′-carboxychalcone and 1-(5-hydroxyindolyl-3)-2-(3-carboxy-4-hydroxybenzoyl)ethylene was found to be competitive at both pH 6.8 and pH 8.0. 2. 2. The K m for 5-HTP decarboxylation was estimated to be 4.0 × 10 −5 at pH 8.0 and 1.7 × 10 −4 at pH 6.8. 3. 3. Preincubation experiments appear to rule out the possibility that 5-HTP irreversibly combines at a DOPA site while reacting at a different site. It appears possible but unlikely that DOPA irreversibly binds at a 5-HTP site while reacting at a different site. 4. 4. These experiments would seem to strengthen the view that one enzymic site is involved in the decarboxylation of DOPA and 5-HTP." @default.
- W1982908077 created "2016-06-24" @default.
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- W1982908077 date "1960-07-01" @default.
- W1982908077 modified "2023-09-23" @default.
- W1982908077 title "Studies on 5-hydroxytryptophan decarboxylase. II. Additional inhibition studies and suggestions on the nature of the enzymic site" @default.
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- W1982908077 doi "https://doi.org/10.1016/0003-9861(60)90025-4" @default.
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