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- W2043864540 abstract "1. Five additional phenylalanine (PHE)-requiring mutants have been isolated but they do not add to the number of loci already known which have been designated phenA ( phen2 and its alleles) and phenB ( phen6 ). 2. Two pathways for tyrosine (TYR) synthesis in A. nidulans have been proposed: the well-known one by the transamination of p -hydroxyphenylpyruvic acid and an alternative one, as in animals, by the hydroxylation of PHE. 3. Ten allelic partial TYR-requiring mutants ( tyrA ), presumably blocked in the transamination pathway, have been isolated after N-methyl-N′-nitro-N-nitrosoguanidine (NTG) treatment of bil;phenA 3 conidia. 4. Four partial TYR requirers (at another locus— tyrB ) have been isolated after NTG treatment of tyr A7, bi1 conidia. They are presumably blocked in an alternative pathway for TYR synthesis, i.e. in the PHE-hydroxylation pathway. 5. tyrA mutants have been found to be p -fluorophenylalanine (FPA)-resistant and allelic to mutants at the fpA locus. tyrB mutants have been found to be very leaky and FPA-sensitive. tyrA;tyrB double mutants have been found to be exacting TYR requirers. 6. Mutants at loci fpA ( tyrA ) and fpE (anthranilic acid-requiring) have been interpreted to be p -fluorophenylalanine-resistant due to an oversynthesis of PHE." @default.
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- W2043864540 date "1967-12-01" @default.
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- W2043864540 title "Aromatic amino acid biosynthesis and para-fluorophenylalanine resistance inAspergillus nidulans" @default.
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- W2043864540 doi "https://doi.org/10.1017/s0016672300011022" @default.
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