The crystal structure of the formiminotransferase domain of formiminotransferase-cyclodeaminase: implications for substrate channeling in a bifunctional enzyme.
Kohls, D., Sulea, T., Purisima, E.O., MacKenzie, R.E., Vrielink, A.(2000) Structure 8: 35-46
- PubMed: 10673422 
- DOI: https://doi.org/10.1016/s0969-2126(00)00078-2
- Primary Citation of Related Structures:  
1QD1 - PubMed Abstract: 
The bifunctional enzyme formiminotransferase-cyclodeaminase (FTCD) contains two active sites at different positions on the protein structure. The enzyme binds a gamma-linked polyglutamylated form of the tetrahydrofolate substrate and channels the product of the transferase reaction from the transferase active site to the cyclodeaminase active site. Structural studies of this bifunctional enzyme and its monofunctional domains will provide insight into the mechanism of substrate channeling and the two catalytic reactions.
Organizational Affiliation: 
Biochemistry Department, McIntyre Medical Sciences Building, Montréal Joint Center for Structural Biology, McGill University, Montréal, H3G 1Y6, Canada.