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- W772526032 abstract "Tyrosine phenol-lyase (TPL) catalyzes the reversible hydrolysis of tyrosine to phenol and ammonium pyruvate (Scheme 1) [9]. Pyridoxal 5’-phosphate is a cofactor of the enzyme. TPL has been found in various bacteria, mostly in Enterobacteriaceae and also in some arthropods. The enzyme catalyzes β-elimination of a number of 3-substituted amino acids with good leaving groups, as, for example, Oand S-derivatives of serine and cysteine, 3-chloroalanine [7]. TPL also racemizes alanine [6] and exchanges α-proton with a solvent in some other amino acids [4]. The enzyme catalyzes reverse reaction of the synthesis of tyrosine and its derivatives starting form various phenol and pyruvate derivatives [11]. The mechanism of TPL action consists of several steps [9], main transitions are drawn in Scheme 2. The first step is the formation of external aldimine − the Schiff base between tyrosine and PLP, which is followed by the abstraction of α-proton leading to the quinoid intermediate. Subsequently, ring-1’ carbon is protonated and the phenol moiety is converted to cyclohexadieCarbon isotope effects in the studies of the mechanism of action of tyrosine phenol-lyase Wojciech Augustyniak, Ryszard Kanski, Marianna Kanska" @default.
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- W772526032 date "2006-01-01" @default.
- W772526032 modified "2023-10-05" @default.
- W772526032 title "Carbon isotope effects in the studies of the mechanism of action of tyrosine phenol-lyase" @default.
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