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): 24
Managers or local contacts: Voltattorni Carla

Sponsors:

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

Barbara Cellini
Carla Voltattorni: Emeritus Professor

Sections
Biological Chemistry Section

Publications
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	BERTOLDI M; VOLTATTORNI C	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
Reaction of dopa decarboxylase with L-aromatic amino acids under aerobic and anaerobic conditions	M. BERTOLDI; BORRI VOLTATTORNI C	2000