Phenylalanine hydroxylase fromLegionella pneumophila: a thermostable dimer
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چکیده
منابع مشابه
Phenylalanine Hydroxylase from Legionella pneumophila Is a Thermostable Enzyme with a Major Functional Role in Pyomelanin Synthesis
BACKGROUND Legionella pneumophila is a pathogenic bacterium that can cause Legionnaires' disease and other non-pneumonic infections in humans. This bacterium produces a pyomelanin pigment, a potential virulence factor with ferric reductase activity. In this work, we have investigated the role of phenylalanine hydroxylase from L. pneumophila (lpPAH), the product of the phhA gene, in the synthesi...
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The laboratory mouse represents an important model for the study of phenylalanine metabolism and the pathochemistry of phenylketonuria, yet mouse phenylalanine hydroxylase (PAH) has not been extensively studied. We report the cloning and sequencing of a mouse PAH cDNA, the expression of enzymic activity from the mouse PAH cDNA clone and the identification of mouse PAH and human PAH by two-dimen...
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Iron can be bound to phenylalanine hydroxylase (PAH) in two environments. The assignment of the electron paramagnetic resonance spectrum of PAH to two, overlapping high-spin ferric signals is confirmed by computer simulation. Both environments are shown to be populated in the crude enzyme. Reconstitution of the apoenzyme demonstrated that the two iron environments are not interconvertible. Oxyg...
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Phenylalanine hydroxylase [L-phenylalanine,tetrahydropteridine :oxygen oxidoreductase (4-hydroxylating); EC 1.14.16.11 catalyses the first reaction in the irreversible catabolism of the essential amino acid phenylalanine. Studies of the isolated enzyme and of phenylalanine metabolism in viuo and in oitro support the view that the hydroxylase plays the major role in regulating phenylalanine disp...
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ژورنال
عنوان ژورنال: Acta Crystallographica Section A Foundations of Crystallography
سال: 2012
ISSN: 0108-7673
DOI: 10.1107/s0108767312099321