Mechanistic Investigations of Mandelate Racemase: The Electrophilic Catalysts
Budihas, Scott Ronald
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https://hdl.handle.net/2142/84891
Description
Title
Mechanistic Investigations of Mandelate Racemase: The Electrophilic Catalysts
Author(s)
Budihas, Scott Ronald
Issue Date
1998
Doctoral Committee Chair(s)
Gerlt, John A.
Department of Study
Biochemistry
Discipline
Biochemistry
Degree Granting Institution
University of Illinois at Urbana-Champaign
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
Chemistry, Biochemistry
Language
eng
Abstract
MR is a member of the enolase superfamily (Babbitt et al., 1996), which is a family of proteins which are both structurally and mechanistically related. All the family members have highly conserved metal ion ligands. Based on the homology to enolase, which requires two divalent metal ions, MR as well as other members of the enolase superfamily might require two metal ions. The stoichiometries of metal ion requirements for MR, muconate lactonizing enzyme (MLE), galactonate dehydratase (GalD) and glucarate dehydratase (GlucD) were determined. MR and MLE bind and require a single metal ion for activity. GalD and GlucD require two metals for activity and show inhibition at high metal ion concentrations with Mn$\sp{2+}.$.
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