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- W1567127782 abstract "In addition to the usual decarboxylation, pig kidney 3,4-dihydroxyphenylalanine (dopa) decarboxylase catalyzes a decarboxylation-dependent transamination which converts dopa into 3,4-dihydroxyphenylacetaldehyde and sinultaneously converts enzyme-bound pyridoxal-P into pyridoxamine-P. Similar reactions occur when this enzyme acts on m-tyrosine, alpha-methyldopa, and alpha-methyl-m-tyrosine. The transamination occurs in about 0.02% of decarboxylations of dopa and m-tyrosine and in about 2% of decarboxylations of alpha-methyldopa and alpha-methyl-m-tyrosine. The fraction of decarboxylations proceeding by the transamination pathway is independent of pH. This reaction appears to result from a divergence in the normal mechanism of decarboxylation; the quinoid intermediate which is formed by decarboxylation of the substrate-pyridoxal-P-Schiff base ordinarily protonates on the alpha carbon of the amino acid, but protonation occasionally occurs at the benzylic carbon of the coenzyme, and this latter route leads to transamination." @default.
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- W1567127782 date "1977-10-01" @default.
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- W1567127782 title "Decarboxylation-dependent transamination catalyzed by mammalian 3,4-dihydroxyphenylalanine decarboxylase." @default.
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- W1567127782 doi "https://doi.org/10.1016/s0021-9258(19)66950-4" @default.
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