Crystallographic studies of tyrosine phenol-lyase

Autor: Guy Dodson, Keith S. Wilson, S. V. Pletnev, Tatyana V. Demidkina, Alfred A. Antson, E. G. Harutyunyan
Rok vydání: 1994
Předmět:
Zdroj: Biochemistry of Vitamin B6 and PQQ ISBN: 9783034873956
DOI: 10.1007/978-3-0348-7393-2_30
Popis: Monovalent cation binding site of the enzyme was determined using X-ray data obtained from apoenzyme crystals soaked in K+ and Cs+ containing solutions. Glu 69 is involved in formation of that site and is conserved in all other tyrosine phenol-lyases and tryptophan indol-lyases with known sequence. Three dimensional structures of holoenzyme and its complex with 3-(4-hydroxyphenyl)propionic acid were solved and refined at 2.7A and 2.5 A respectively. The structures explicitly reveal the cofactor and substrate binding pockets.
Databáze: OpenAIRE