Abstract:
:Electrostatic interactions play important roles in the catalysis of chorismate to prephenate by chorismate mutase. Mutation of Gln88 to glutamate in the monofunctional chorismate mutase from Escherichia coli results in an enzyme with a pH profile of activity significantly different from that of the wild type protein. To investigate whether the mutation alters the substrate binding process or the catalysis, we have directly determined the thermodynamic parameters of a transition state analogue inhibitor binding to the wild-type chorismate mutase and its Q88E mutant using isothermal titration calorimetry. The results demonstrate that solvent reorganization and hydrophobic interactions contribute the predominant free energy to inhibitor binding. The charge state of Glu88 in the Q88E mutant was experimentally determined and was shown to be protonated at pH 4.5 and ionized at pH 7.8, consistent with earlier hypotheses. Most surprisingly, inhibitor binding energetics do not exhibit significant pH dependency for both enzymes. Our findings indicate that the charge state of Glu88 has a small impact on inhibitor binding but plays an important role in the catalytic process.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Lee AY,Zhang S,Kongsaeree P,Clardy J,Ganem B,Erickson JW,Xie Ddoi
10.1021/bi980217usubject
Has Abstractpub_date
1998-06-23 00:00:00pages
9052-7issue
25eissn
0006-2960issn
1520-4995pii
bi980217ujournal_volume
37pub_type
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