Thermal Bifunctionality of Bacterial Phenylalanine Aminomutase and Ammonia Lyase Enzymes
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چکیده
منابع مشابه
Thermal bifunctionality of bacterial phenylalanine aminomutase and ammonia lyase enzymes.
Phenylalanine aminomutases (PAMs) are 4-methylideneimidazol-5-one (MIO)-dependent enzymes that catalyze the isomerization of (S)-a-phenylalanine to give (S)or (R)-bphenylalanine, which are precursors in the biosynthesis of various natural products. Several related tyrosine aminomutases (TAMs) have also been characterized. Furthermore, the mechanistically related MIO-dependent phenylalanine, tyr...
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Trichosporon cutaneum phenylalanine ammonia lyase was selected as a model to investigate the dual substrate activity of this family of enzymes. Sequencing of the PAL gene identified an extensive intron region at the N-terminus. Five amino acid residues differing from a prior report were identified. Highest Phe : Tyr activities (1.6 ± 0.3 : 0.4 ± 0.1 μ mol/h g wet weight) were induced by Tyr. ...
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ژورنال
عنوان ژورنال: Angewandte Chemie International Edition
سال: 2012
ISSN: 1433-7851
DOI: 10.1002/anie.201200669