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Enzymatic decarboxylation of L-threo-3,4-dihydroxyphenylserine in rat heart.

I Ohmura·C Inagaki·H Araki·C Tanaka
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Abstract

Decarboxylation of L-threo-3,4-dihydroxyphenylserine (L-threo-DOPS) by the higher speed supernatant of the rat heart homogenate and the regional distribution of L-threo-DOPS decarboxylase activity were examined. Decarboxylation was demonstrated to occur specifically with L-isomer but not with D-isomer. Addition of pyrogallol was necessary for maximal recovery of norepinephrine. The optimal condition for decarboxylation of L-threo-DOPS by the rat heart enzyme was similar to conditions required with the enzymes from brain and kidney. Under the optimal conditions, Km and Vmax for L-threo-DOPS were 2.1 mM and 6.4 nmoles/mg protein/15 min, respectively. Decarboxylation of L-threo-DOPS was markedly inhibited by D-threo-DOPS and D-DOPA. The L-aromatic amino acid decarboxylase activity was highest in the right auricle followed by the atrial body, the left auricle, the right ventricle and the left ventricle.

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AnimalsCarboxy-LyasesDecarboxylationDihydroxyphenylalanineDroxidopaHydrogen-Ion ConcentrationIn Vitro TechniquesKineticsMaleMyocardiumNorepinephrinePyridoxal PhosphatePyrogallolRatsSerineTemperatureTime FactorsJournal Article

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I Ohmura, C Inagaki, H Araki, C Tanaka. 1978. Enzymatic decarboxylation of L-threo-3,4-dihydroxyphenylserine in rat heart.. https://doi.org/10.1254/jjp.28.747

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