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oai:www.ideals.illinois.edu:2142/84891 2023-07-11 col_2142_5131 col_2142_14795 com_2142_5130 com_2142_14794 com_2142_14793 com_2142_8903

Gerlt, John A. Budihas, Scott Ronald 2015-09-25T22:28:22Z 2015-09-25T22:28:22Z 10000-01-01 1998 1998 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$\sp{2+}.$. Made available in DSpace on 2015-09-25T22:28:22Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 9904398.pdf: 4176447 bytes, checksum: 5ffce56c8d23d6723247aa6178f36947 (MD5) Previous issue date: 1998 Embargo set by: Seth Robbins for item 86172 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs U of I Only 110 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1998. http://hdl.handle.net/2142/84891 (MiAaPQ)AAI9904398 eng Chemistry, Biochemistry Mechanistic Investigations of Mandelate Racemase: The Electrophilic Catalysts text Biochemistry Biochemistry University of Illinois at Urbana-Champaign Dissertation Ph.D.