2014
DOI: 10.1515/pteridines-2014-0006
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Dynamic regulation of phenylalanine hydroxylase

Abstract: Phenylalanine hydroxylase (PAH) is the key enzyme in phenylalanine metabolism, catalyzing its oxidative breakdown to tyrosine. Its function in the committed step of amino acid metabolism requires strict regulation. Thus, several regulatory mechanisms are central for an understanding of PAH at the atomistic level. The enzyme is activated by incubation with phenylalanine and inhibited by tetrahydrobiopterin binding. Furthermore, phosphorylation of Ser-16 in the regulatory domain influences enzyme turnover. All m… Show more

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Cited by 8 publications
(9 citation statements)
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References 60 publications
(75 reference statements)
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“…We analyzed secondary structure elements and B-factors of Cα atoms (derived from root mean squared fluctuations) after a global alignment as a metric for flexibility. Total vibrational entropies were calculated via a normal mode analysis of the covariance matrix of Cα atoms 46 .…”
Section: Methodsmentioning
confidence: 99%
“…We analyzed secondary structure elements and B-factors of Cα atoms (derived from root mean squared fluctuations) after a global alignment as a metric for flexibility. Total vibrational entropies were calculated via a normal mode analysis of the covariance matrix of Cα atoms 46 .…”
Section: Methodsmentioning
confidence: 99%
“…Phenylalanine metabolism could be affected through the impairment of PAH activity due to immune activation and inflammation (Scholl-Bürgi et al, 2011). Increase of reactive oxygen species (ROS) during inflammatory conditions can cause irreversible oxidation of PAH cofactor, as well as influence on the tertiary structure of PAH resulting in an impairment of the substrate and/or the cofactor binding (Fuchs et al, 2014).…”
Section: Discussionmentioning
confidence: 99%
“…Still, we assume such major rearrangements soon in range given sampling times beyond the microsecond regime using dedicated simulation architectures . Additionally, enhanced sampling techniques are expected to further aid description of intermediate conformational states of the NLRP pyrin domain. Changes on the level of protein assembly state are increasingly recognized as key factors in biological systems and intrinsically require advanced sampling times and techniques …”
Section: Discussionmentioning
confidence: 99%