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- W2069254583 abstract "It has been generally assumed that a tetrahydropterin (2-amino-5,6,7,8-tetrahydro-4-pteridinone) is essential for activity of the three aromatic amino acid hydroxylases. In this report it is shown that appropriately substituted pyrimidines can assume the role of cofactor for phenylalanine hydroxylase. 2,5,6-Triamino-4-pyrimidinone(V) and 5-benzylamino-2,6-diamino-4-pyrimidinone(VI) possess the same Km values (0.1 mM and 0.003 mM) and stoichiometry of tyrosine generated to cofactor consumed (0.4 and 1.0) as their corresponding pteridine analogs, tetrahydropterin(III) and 6-phenyltetrahydropterin(IV). However, the rates with pyrimidines are lower. The ratio of rates VIII = 0.045 and VIIV = 0.015. These results indicate that pteridine carbons 6 and 7 are not fundamental to cofactor binding or function, though they markedly influence the maximum velocity of hydroxylation. Pyrimidine cofactors of phenylalanine hydroxylase are valuable probes for the elucidation of the binding forces, transition states, and mechanism of oxygen activation of these hydroxylases." @default.
- W2069254583 created "2016-06-24" @default.
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- W2069254583 date "1978-12-01" @default.
- W2069254583 modified "2023-09-23" @default.
- W2069254583 title "Pyrimidines as cofactors for phenylalanine hydroxylase" @default.
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- W2069254583 doi "https://doi.org/10.1016/0006-291x(78)91188-9" @default.
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