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Title:Mechanistic Investigations of Mandelate Racemase: The Electrophilic Catalysts
Author(s):Budihas, Scott Ronald
Doctoral Committee Chair(s):Gerlt, John A.
Department / Program:Biochemistry
Discipline:Biochemistry
Degree Granting Institution:University of Illinois at Urbana-Champaign
Degree:Ph.D.
Genre:Dissertation
Subject(s):Chemistry, Biochemistry
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$\sp{2+}.$.
Issue Date:1998
Type:Text
Language:English
Description:110 p.
Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1998.
URI:http://hdl.handle.net/2142/84891
Other Identifier(s):(MiAaPQ)AAI9904398
Date Available in IDEALS:2015-09-25
Date Deposited:1998


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