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Literature summary for 1.14.16.1 extracted from

  • Lye, L.F.; Kang, S.O.; Nosanchuk, J.D.; Casadevall, A.; Beverley, S.M.
    Phenylalanine hydroxylase (PAH) from the lower eukaryote Leishmania major (2011), Mol. Biochem. Parasitol., 175, 58-67.
    View publication on PubMedView publication on EuropePMC
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Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50400
-
 deduced from cDNA Leishmania major

Organism

Organism UniProt Comment Textmining
Leishmania major Q6WRI4
-
-

Synonyms

Synonyms Comment Organism
phenylalanine hydroxylase
-
 Leishmania major

Cofactor

Cofactor Comment Organism Structure
tetrahydrobiopterin
-
 Leishmania major

General Information

General Information Comment Organism
malfunction a pah null mutant and an episomal complemented overexpressing derivative (pah-/+PAH) are generated. Wild-type but not null mutants parasites show reactivity with an antibody to melanin when grown with l-3,4-dihydroxyphenylalanine. Wild-type is auxotrophic for Phe, Trp and Tyr, suggesting that PAH activity is insufficient to meet normal Tyr requirements. PAH null mutants show an increased sensitivity to Tyr deprivation, while the pah-/+PAH overexpressor shows increased survival and can be adapted to grow well without added Tyr. PAH null mutant shows no alterations in tetrahydrobiopterin-dependent differentiation Leishmania major