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Publication Type
Journal Article
UWI Author(s)
Author, Analytic
Goldson Barnaby, Andrea; Scaman, Christine
Author Affiliation, Ana.
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Article Title
Purification and characterization of phenylalanine ammonia lyase from Trichosporon cutaneum.
Medium Designator
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Connective Phrase
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Journal Title
Enzyme Research
Translated Title
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Reprint Status
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Date of Publication
2013
Volume ID
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Issue ID
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Page(s)
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Language
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Connective Phrase
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Location/URL
https:; www.hindawi.com/journals/er/2013/670702/
ISSN
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Notes
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Abstract
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 ?µmol/h?g wet weight) were induced by Tyr. The enzyme has a temperature optimum of 32°C and a pH optimum of 8–8.5 and shows no metal cofactor dependence. Michaelis-Menten kinetics (Phe, ?? ?? 5 . 0 ± 1 . 1 ?mM) and positive allostery (Tyr, ?? ? 2 . 4 ± 0 . 6 ?mM, Hill coefficient 1 . 9 ± 0 . 5 ) were observed. Anion exchange chromatography gave a purification fold of 50 with 20% yield. The His-Gln motif (substrate selectivity switch region) indicates the enzyme’s ability to act on both substrates.....
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