Arginine residues are generally considered poor candidates for the role of general bases
because they are predominantly protonated at physiological pH. Nonetheless, Arg residues …

Abstract Pyridoxal-5′-phosphate (PLP) is a versatile cofactor that enzymes use to catalyze
a wide variety of reactions of amino acids, including transamination, decarboxylation …

l-Tyrosine derivatives were obtained in> 97% ee via a biocatalytic one-pot two-step cascade
using substituted benzenes, pyruvate, and NH3 as starting materials. In the first step …

The l-tryptophan degradation product indole is a purported extracellular signaling molecule
that influences biofilm formation in various bacteria. Here we analyzed the mechanisms of …

Abstract Pyridoxal 5′‐phosphate (PLP)‐dependent enzymes represent about 4% of the
enzymes classified by the Enzyme Commission. The versatility of PLP in carrying out a large …

The chemical synthesis of 3‐substituted tyrosine derivatives requires a minimum of four
steps to access optically enriched material starting from commercial precursors. Attempting …

Tyrosine phenol-lyase (TPL) catalyzes the reversible cleavage of l-tyrosine to phenol,
pyruvate and ammonia. When pyrocatechol is substituted for phenol, l …

Genetic circuit-based biosensors are useful in detecting target metabolites or in vivo
enzymes using transcription factors (Tx) as a molecular switch to express reporter signals …

The key step in the enzymatic reaction catalyzed by tyrosine phenol-lyase (TPL) is reversible
cleavage of the Cβ–Cγ bond of l-tyrosine. Here, we present X-ray structures for two …

Tyrosine phenol-lyase (TPL) and tryptophan indole-lyase (Trpase) catalyse the reversible
hydrolytic cleavage of l-tyrosine or l-tryptophan to phenol or indole, respectively, and …