1.14.13.196	S257A	following oxygen consumption, the Km value of the S257A enzyme for NADPH was not significantly changed, whereas the kcat value increased. When the activity is determined by measuring the formation of N5-hydroxyornithine, the kcat value for the S257A enzyme is lower than that for the wild-type enzyme. The S257A mutation causes an increase in flexibility in two small loops, loop 253–257, which is within interacting distance of NADP+ (including Ser257 and Gln256, which are able to form hydrogen bonds with NADP during MD simulations), and loop 453–458, which resides 5 A from the FAD phosphate group. In contrast, loop 97–105 (including Gln-102, which makes a hydrogen bond with FAD) presents reduced flexibility in the mutant enzyme	725540