Structural basis for substrate recognition and hydrolysis by mouse carnosinase CN2
Laboratory studyOther animals
- Design
- Laboratory study
- What was measured
- Crystal structures of mouse cytosolic carnosinase CN2 bound to the inhibitor bestatin with zinc and manganese.
What the authors reported
Crystal structures of mouse CN2 complexed with bestatin and Zn2+ (1.7 angstrom) and with Mn2+ (2.3 angstrom) closely resembled each other. CN2 is a homodimer, each subunit having domain A (bound to bestatin and two metal ions) and domain B (the main dimer interface). Bestatin interacts with residues of domain B of the other subunit, which the authors say is likely essential for activity. Because bestatin is not accessible to bulk water, they propose substrate binding needs conformational flexibility between domains A and B.
Limits of this study
Structural study of the mouse enzyme. Full text not read.
Source
PubMed 18550540 · doi:10.1074/jbc.M801657200
Entry checked against PubMed abstract (E-utilities) on 2026-10-19. The dose shown is the dose the researchers used. It is not a recommendation. How to read this page.