Conversely, the L314H mutation sits in a position that has large implications for enzyme function. Residue 314 sits in a likely substrate entry channel in the enzyme (figure , red patch) and is just 5 Å from the disulfide active site of the enzyme (figure ). The leucine to histidine mutation significantly alters the chemistry of this residue -from hydrophobic to an acid-base active aromatic residue. We therefore hypothesize that enzyme activity alterations can be attributed to the L314H mutation, and we focus our analysis on this mutation.