Figure 1 - full size

Figure 1. Figure 1. UMPS Domain Structure and OMPD Biochemistry (A) Reaction catalyzed by OMPD. (B) Turnover of OMP substrate by wild-type OMPD (black) is abolished in the Asp312Asn mutant (red). If the detection limit of the assay is assumed to be 5% of the total signal over 4000 s, the Asp312Asn mutant is at least 1300-fold less active than the wild-type. (C) Michaelis-Menten kinetics of wild-type OMPD at 25°C. (D) OMPD is an obligatory dimer of high affinity.

The above figure is reprinted by permission from Cell Press: Structure (2008, 16, 82-92) copyright 2008.