Synthesis of L-tyrosine-related amino acids by beta-tyrosinase.
Synthesis of 2,3,4-trihydroxy-L-phenylalanine from s-methyl-L-cysteine and pyrogallol by L-tyrosine phenol-lyase.
Stereochemistry of beta-replacement reactions catalyzed by tyrosine phenol-lyase.
Elementary processes in the interaction of tyrosine phenol lyase with inhibitors and substrate.
Reactions of O-acyl-L-serines with tryptophanase, tyrosine phenol-lyase, and tryptophan synthase.
Tyrosine phenol-lyase from Citrobacter intermedius. Factors controlling substrate specificity.
Crystallization and crystal data on tyrosine phenol-lyase.
The polypeptide chain fold in tyrosine phenol-lyase, a pyridoxal-5'-phosphate-dependent enzyme.
Three-dimensional structure of tyrosine phenol-lyase.
Site-directed mutagenesis of tyrosine-71 to phenylalanine in Citrobacter freundii tyrosine phenol-lyase: evidence for dual roles of tyrosine-71 as a general acid catalyst in the reaction mechanism and in cofactor binding.
Purification and crystals of tyrosine phenol-lyase from Erwinia herbicola.
The crystal structure of Citrobacter freundii tyrosine phenol-lyase complexed with 3-(4'-hydroxyphenyl)propionic acid, together with site-directed mutagenesis and kinetic analysis, demonstrates that arginine 381 is required for substrate specificity.
Synthesis of (2S,3R)-beta-methyltyrosine catalyzed by tyrosine phenol-lyase.
Conversion of tyrosine phenol-lyase to dicarboxylic amino acid beta-lyase, an enzyme not found in nature.
The role of glutamic acid-69 in the activation of Citrobacter freundii tyrosine phenol-lyase by monovalent cations.
Interaction of tyrosine phenol-lyase with phosphoroorganic analogues of substrate amino acids.
Inhibition of tyrosine phenol-lyase from Citrobacter freundii by 2-azatyrosine and 3-azatyrosine.
Threonine-124 and phenylalanine-448 in Citrobacter freundii tyrosine phenol-lyase are necessary for activity with L-tyrosine.
Crystals of tryptophan indole-lyase and tyrosine phenol-lyase form stable quinonoid complexes.
This enzyme catalyzes several reactions; (A) Formation of external aldimine from internal aldimine (with pyridoxal phosphate;PLP) involves addition to double-bond and elimination accompanied by double-bond formation. (Arg217 can be involved in the formation.) (B) Elimination of phenol, accompanied by double-bond formation. (C) Return to internal aldimine involves addition to double-bond, and elimination accompanied by double-bond formation. (D) Hydrolysis of aldimine bond. However, the mechanism of hydrolysis has not been elucidated.