Inhibition of aromatic L-amino acid decarboxylase by coenzyme-amino acid adducts

The coenzyme-amino acid adducts N-(5'-phosphopyridoxyl)-L-3,4-dihydroxyphenylalanine and N-(5'-phosphopyridoxyl)-L-m-NH sub(2)-tyrosine inhibit hog kidney aromatic L-amino acid decarboxylase (Dopa decarboxylase). Kinetic studies on the nature of the inhibition caused by these adducts appea...

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Bibliographic Details
Published in:Biochemistry (Easton) 1981-12, Vol.20 (26), p.7469-7475
Main Authors: Rudd, Edwin A, Thanassi, John W
Format: Article
Language:English
Subjects:
Amino Acids - pharmacology
Animals
Aromatic Amino Acid Decarboxylase Inhibitors
aromatic L-amino acid decarboxylase
Binding Sites
Coenzymes - pharmacology
Dopa Decarboxylase - isolation & purification
kidney
Kidney - enzymology
Kinetics
mechanisms
pigs
pyridoxal 5'-phosphate
Swine
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Summary:The coenzyme-amino acid adducts N-(5'-phosphopyridoxyl)-L-3,4-dihydroxyphenylalanine and N-(5'-phosphopyridoxyl)-L-m-NH sub(2)-tyrosine inhibit hog kidney aromatic L-amino acid decarboxylase (Dopa decarboxylase). Kinetic studies on the nature of the inhibition caused by these adducts appeared to distinguish two distinct decarboxylase activities in purified enzyme preparations. It is proposed that Dopa decarboxylase has either a second active site which has a low affinity for pyridoxal phosphate or a site(s) which when occupied by pyridoxal phosphate leads to an increase in the activity of the enzyme.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi00529a022