Structure and Mechanism of Plp-Dependent Enzymes

Phillips, Robert Stephen

Abstract

Funding Agency

• Agency: National Institute of Health (NIH)
• Institute: Fogarty International Center (FIC)
• Type: Small Research Grants (R03)
• Project #: 5R03TW000106-03
• Application #: 2291590
• Study Section: Special Emphasis Panel (SRC)
• Project Start: 1993-09-01
• Project End: 1998-04-30
• Budget Start: 1996-05-01
• Budget End: 1998-04-30
• Support Year: 3
• Fiscal Year: 1996

Institution

• Name: University of Georgia
• Department: Chemistry
• Type: Other Domestic Higher Education
• City: Athens
• State: GA
• Country: United States
• Zip Code: 30602

Publications

Demidkina, T V; Faleev, N G; Papisova, A I et al. (2006) Aspartic acid 214 in Citrobacter freundii tyrosine phenol-lyase ensures sufficient C--H-acidity of the external aldimine intermediate and proper orientation of the cofactor at the active site. Biochim Biophys Acta 1764:1268-76

Kulikova, Vitalia V; Zakomirdina, Ludmila N; Dementieva, Irene S et al. (2006) Tryptophanase from Proteus vulgaris: the conformational rearrangement in the active site, induced by the mutation of Tyrosine 72 to phenylalanine, and its mechanistic consequences. Biochim Biophys Acta 1764:750-7