Decarboxylation-dependent transamination catalyzed by mammalian 3,4-dihydroxyphenylalanine decarboxylase.
作者： M H O'Leary , R L Baughn
DOI: 10.1016/S0021-9258(19)66950-4
关键词:
摘要: 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 enzyme-bound pyridoxal-P pyridoxamine-P. Similar reactions occur when this enzyme acts on m-tyrosine, alpha-methyldopa, alpha-methyl-m-tyrosine. The occurs in about 0.02% of decarboxylations m-tyrosine 2% alpha-methyldopa fraction proceeding by pathway is independent pH. This reaction appears result from divergence normal mechanism decarboxylation; quinoid intermediate formed decarboxylation substrate-pyridoxal-P-Schiff base ordinarily protonates alpha carbon amino acid, but protonation occasionally at benzylic coenzyme, latter route leads transamination.
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