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Literature summary for 1.14.16.1 extracted from

  • Kinzie, S.D.; Thevis, M.; Ngo, K.; Whitelegge, J.; Loo, J.A.; Abu-Omar, M.M.
    Posttranslational hydroxylation of human phenylalanine hydroxylase is a novel example of enzyme self-repair within the second coordination sphere of catalytic iron (2003), J. Am. Chem. Soc., 125, 4710-4711.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information N-terminal deletion of amino acid residues 1-116, kinetics, thermal stability, oligomerization profile similar to wild-type. N-terminal deletion of amino acid residues 1-116 plus mutation Y325F, 3fold reduction in kcat-value Homo sapiens
Y325A no enzymic activity, aggregation of protein Homo sapiens
Y325F kinetics, thermal stability, oligomerization profile similar to wild-type Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
additional information self-hydroxylation mechanism at Phe325, dependent on iron at the active site Homo sapiens