University of Illinois at Urbana-Champaign
Mechanistic Investigations of Mandelate Racemase: The Electrophilic Catalysts
Abstract
dc:descriptionMR 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$\sp{2+}.$.
Degree
thesis:*- Name thesis:degree_name
- Ph.D.
- Level thesis:degree_level
- Dissertation
- Discipline thesis:degree_discipline
- Biochemistry
- Grantor
- University of Illinois at Urbana-Champaign
- Year dc:date
- 2015
Author and committee
dc:creator, dc:contributor.*- Author dc:creator
-
- Budihas, Scott Ronald
- Contributors dc:contributor
-
- Gerlt, John A.
Subjects
dc:subject × 1Rights
- Language dc:language
- eng
Identifiers
dc:identifier.*- Identifier
- (MiAaPQ)AAI9904398
- OAI identifier oai:identifier
- oai:www.ideals.illinois.edu:2142/84891