Pyridoxal 5'-phosphate dependent enzymes: from the primary structure to the catlytic versatility. Dopa decarboxylase and cystalysin: catalytic and inactivation mechanisms.

Starting date
November 1, 2001
Duration (months)
Managers or local contacts
Voltattorni Carla


Consorzio Interuniversitario per le Biotecnologie
Funds: assigned and managed by the department
Ministero dell'Istruzione dell'Università e della Ricerca
Funds: assigned and managed by the department
Syllabus: PRIN
Funds: assigned and managed by the department

Project participants

Mariarita Bertoldi
Associate Professor
Silvia Bianconi
Technical-administrative staff
Title Authors Year
Mutation of tyrosine 332 to phenylalanine converts dopa decarboxylase into a decarboxylation-dependent oxidative deaminase. Bertoldi M, Gonsalvi M, Contestabile R, Voltattorni CB. 2002
Spectroscopic and kinetic analyses reveal the pyridoxal 5'-phosphate binding mode and the catalytic features of Treponema denticola cystalysin Bertoldi M, Cellini B, Clausen T, Voltattorni CB. 2002
Dopa decarboxylase exhibits low pH half-transaminase and high pH oxidative deaminase activities toward serotonin (5-hydroxytryptamine) Bertoldi, M; Voltattorni, Cb 2001
Mutations of residues in the coenzyme binding pocket of Dopa decarboxylase: effect on catalytic properties M. Bertoldi, C. Castellani and C. Borri Voltattorni 2001
Structural insight into Parkinson's disease treatment from drug-inhibited DOPA decarboxylase. Burkhard P, Dominici P, Voltattorni BC, Jansonius JN, Malashkevich VN. 2001


Research facilities