Pregled bibliografske jedinice broj: 369570
Structural Studies of the Enzymatic Mechanism of Citrobacter freundii Tyrosine Phenol-lyase
Structural Studies of the Enzymatic Mechanism of Citrobacter freundii Tyrosine Phenol-lyase // The 2nd International Interdisciplinary Conference on Vitamins, Coenzymes, and Biofactors
Athens (GA), Sjedinjene Američke Države; Gruzija, 2008. str. 15-15 (pozvano predavanje, nije recenziran, sažetak, znanstveni)
CROSBI ID: 369570 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Structural Studies of the Enzymatic Mechanism of Citrobacter freundii Tyrosine Phenol-lyase
Autori
Milić, Dalibor ; Demidkina, Tatyana V. ; Matković-Čalogović, Dubravka ; Antson, Alfred A.
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni
Izvornik
The 2nd International Interdisciplinary Conference on Vitamins, Coenzymes, and Biofactors
/ - , 2008, 15-15
Skup
The Second International Interdisciplinary Conference on Vitamins, Coenzymes, and Biofactors
Mjesto i datum
Athens (GA), Sjedinjene Američke Države; Gruzija, 26.10.2008. - 31.10.2008
Vrsta sudjelovanja
Pozvano predavanje
Vrsta recenzije
Nije recenziran
Ključne riječi
tyrosine phenol-lyase; beta-elimination; quinonoid intermediate; closed conformation; pyridoxal 5'-phosphate; structural enzymology; X-ray structural analysis
Sažetak
Tyrosine phanol-lyase (TPL) catalyzes the reversible hydrolytic beta-elimination reaction of L-tyrosine to produce phenol and ammonium pyruvate. It is a homotetrameric protein which belongs to the Fold Type I (aspartate aminotransferase) family of the PLP-dependent enzymes (1). The active sites (one per subunit) are situated at the interface of two subunits forming the so-called catalytic dimer. Each protein subunit and the corresponding active site of Citrobacter freundii TPL can possess two different conformations: open and closed (2). The closed conformation is formed from the open one by the rotation of the small rigid region by 16° about a hinge connecting it with the large rigid region. Our crystallographic studies (3) have showed that the active-site closure protects the key quinonoid intermediate from the solvent and brings the catalytically important residues Arg381, Thr124 and Phe448 into positions suitable for the interaction with the substrate thus facilitating the abstraction of phenol during the beta-elimination of L-tyrosine. References 1. Antson, A. A., Demidkina, T. V., Gollnick, P., Dauter, Z., Von Tersch, R. L., Long, J., Berezhnoy, S. N., Phillips, R. S., Harutyunyan, E. H., and Wilson, K. S., Biochemistry, 32, 4195– 4206 (1993). 2. Milić, D., Matković-Čalogović, D., Demidkina, T. V., Kulikova, V. V., Sinitzina, N. I., and Antson, A. A., Biochemistry 45, 7544– 7552 (2006). 3. Milić, D., Demidkina, T. V., Faleev, N. G., Matković-Čalogović, D., and Antson, A. A., J. Biol. Chem., In press, (2008), doi:10.1074/jbc.M802061200.
Izvorni jezik
Engleski
Znanstvena područja
Kemija
POVEZANOST RADA
Projekti:
119-1193079-1084 - Strukturno istraživanje bioloških makromolekula metodom rentgenske difrakcije (Matković-Čalogović, Dubravka, MZOS ) ( CroRIS)
Ustanove:
Prirodoslovno-matematički fakultet, Zagreb