dc.contributor.author | Black, Amanda | |
dc.date.accessioned | 2023-06-15T17:05:49Z | |
dc.date.available | 2023-06-15T17:05:49Z | |
dc.date.issued | 2023-06-13 | |
dc.identifier.uri | http://hdl.handle.net/10222/82655 | |
dc.description.abstract | Isoleucine 2-epimerase participates in production of branched-chain D-amino acids. We showed that L- and D-neopentyl glycine are substrates of LbIleE, with Km values of 0.65 ± 0.03 mM and 0.43 ± 0.03 mM, respectively. The corresponding kcat/Km values (1.45 ± 0.04 mM–1s–1 and 1.58 ± 0.14 mM–1s–1) were reduced ~ 45-fold relative to that of L-Ile. The fluorinated derivative NV-5138 was also shown to be a substrate, with the fluorines having little effect on binding.
CTP synthase catalyzes the formation of CTP from UTP. We constructed EcCTPS lid L11 variants: G357A, G357V, F353Y, F353H, F353W, and F353L. All variants were fully active with exogenous NH3 but exhibited decreased catalytic and activation efficiency with Gln and GTP (WT ~ G357A > G357V, WT > F353Y > F353H > F353W and F353L). NH3 transport and GTP binding were unaffected; however, the glutaminase activity was markedly reduced. | en_US |
dc.language.iso | en | en_US |
dc.subject | Antiviral | en_US |
dc.subject | Anti-cancer | en_US |
dc.subject | Enzyme inhibition | en_US |
dc.subject | Medicinal chemistry | en_US |
dc.subject | Binding interactions | en_US |
dc.subject | Substrate specificity | en_US |
dc.subject | Catalysis | en_US |
dc.title | Studies on Ligand Binding and Catalysis by Isoleucine Epimerase and CTP Synthase | en_US |
dc.type | Thesis | en_US |
dc.date.defence | 2023-05-12 | |
dc.contributor.department | Department of Biochemistry & Molecular Biology | en_US |
dc.contributor.degree | Master of Science | en_US |
dc.contributor.external-examiner | Dr. Greg Fairn | en_US |
dc.contributor.graduate-coordinator | Dr. James Kramer | en_US |
dc.contributor.thesis-reader | Dr. Vanya Ewart | en_US |
dc.contributor.thesis-reader | Dr. David Langelaan | en_US |
dc.contributor.thesis-supervisor | Dr. Stephen Bearne | en_US |
dc.contributor.ethics-approval | Not Applicable | en_US |
dc.contributor.manuscripts | Not Applicable | en_US |
dc.contributor.copyright-release | Not Applicable | en_US |