Assignment of Enzyme Function Through Characterization of the RuBisCO and Enolase Superfamilies

The second superfamily explored in this work is that of the enolase superfamily. Genomic context and primary amino acid sequence make it clear that although the enzymes in this superfamily are structurally and mechanistically related, the chemistry and substrates are varied. Two highly divergent enzymes from Thermotoga maritima and Enterococcus faecalis were targeted for characterization through a multi-disciplinary effort that included structural, computational, and bioinformatic analysis as well as classical enzymology. The T. maritima and E. faecalis enzymes were subsequently confirmed as dipeptide epimerases with unique specificity for hydrophobic dipeptides through screening of dipeptide libraries by mass spectrometry followed by full kinetic characterization of individual dipeptide substrates. These results have provided additional evidence for the utility of multi-disciplinary approaches to functional assignment through use of well-characterized enzyme superfamilies.

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 dc:creator

• Imker, Heidi J.

Contributors dc:contributor

• Gerlt, John A.

• Chemistry, Biochemistry

Language dc:language

eng

Identifier

(MiAaPQ)AAI3347396

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/84860