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Full-Text Articles in Chemistry
Kinetic And Structural Characterization Of Pseudooxynicotine Amine Oxidase From Pseudomonas Putida S16, Vishakha Choudhary
Kinetic And Structural Characterization Of Pseudooxynicotine Amine Oxidase From Pseudomonas Putida S16, Vishakha Choudhary
Masters Theses
Our laboratory has previously shown that nicotine oxidoreductase (NicA2), a member of the flavin-containing amine oxidase family, uses a cytochrome c protein (CycN) as its electron acceptor rather than characteristically accepted molecular oxygen. Within the Pseudomonas putida S16 genome, the nicA2 gene forms an operon with cycN and pseudooxynicotine amine oxidase (pnao), another flavin containing amine oxidase enzyme. The first two steps in the nicotine catabolism pathway are catabolized by NicA2 and Pnao. Through redox chemistry, NicA2 converts nicotine to pseudooxynicotine and Pnao converts pseudooxynicotine to 3-succinoylsemialdehyde-pyridine. In this thesis, we characterize the kinetic and structural properties of …
Engineering Class A Sortases: Activity And Selectivity Of Hybrid And Ancestral Variants, Sarah Struyvenberg
Engineering Class A Sortases: Activity And Selectivity Of Hybrid And Ancestral Variants, Sarah Struyvenberg
WWU Graduate School Collection
Bacterial sortases are cysteine transpeptidases that anchor virulence factors to the surface of bacterial cells. Sortases are a powerful tool utilized for protein engineering that allow researchers to modify proteins at the protein level, not the DNA level. However, important limitations to utilization of sortases for engineering purposes exist; namely, SrtA from S. aureus is a relatively modest enzyme compared to other SrtA enzymes and is very specific for the LPXTG motif. Previous work from our collaborators and others revealed that sortases from different species can recognize alternative sequences and that activities can vary widely. We were curious about how …
Case Studies Of The Hot Dog-Fold And Acyl-Adenylate-Forming Superfamilies: Characterizing The Importance Of Functional Divergence In Cellular Metabolism, Lucas Zimney
Chemistry and Chemical Biology ETDs
Some of the biggest contributors to cellular respiration (and cellular metabolism in general) are acyl-CoA derivatives, a subclass of biological thioesters. Known to function in a variety of pathways, the regulation of their formation and breakdown are critical, carried about by acyl-CoA synthetases and thioesterases, respectively. The work reported within this dissertation will focus on functional divergence within two enzyme superfamilies -- the hot dog-fold and acyl-adenylate-forming superfamilies — and can be broken down into two main parts. Part one will look at tracking the functional divergence within the hot dog-fold superfamily thioesterases. A highly evolved thioesterase, flK, has been …
Kinetic Analysis And Inhibition Studies Of Iron-Dependent Histone Demethylases, Barbara Gordon Cascella
Kinetic Analysis And Inhibition Studies Of Iron-Dependent Histone Demethylases, Barbara Gordon Cascella
Arts & Sciences Electronic Theses and Dissertations
The research presented herein focuses on the kinetics and inhibition of the KDM4 subfamily of Jumonji C (JmjC) domain-containing histone demethylases (HDMs). Belonging to the larger class of alpha-ketoglutarate (alpha-KG)-dependent, non-heme iron monooxygenases, the JmjC-HDMs remove methyl groups from mono-, di-, and tri-methylated histone lysine residues through an Fe(IV)-oxo-catalyzed hydroxylation reaction. JmjC-HDMs have been found to play integral roles in the maintenance of genomic integrity as well as in the regulation of transcription. Three KDM4 members were studied: the mixed H3K9/H3K36 demethylases KDM4A and KDM4C, and the pure H3K9 demethylase KDM4E. KDM4C is a hypoxia-inducible factor 1 (HIF-1) target gene …
Characterization Of Suf Pathway For Fe-S Cluster Assembly In Escherichia Coli, Yuyuan Dai
Characterization Of Suf Pathway For Fe-S Cluster Assembly In Escherichia Coli, Yuyuan Dai
Theses and Dissertations
Fe-S clusters are critical metallocofactors required for cell function. Because of the toxicity of ferrous iron and sulfide to the cell, in vivo Fe-S cluster assembly is carried out by multiprotein biosynthetic pathways. Escherichia coli contains a stress-responsive Fe-S cluster assembly system, the SufABCDSE pathway, working under iron starvation and oxidative stress conditions. The cysteine desulfurase SufS and its accessory protein SufE work together to mobilize persulfide from L-cysteine. We collaborated with Dr. Laura S. Busenlehner to use hydrogen/deuterium exchange mass spectrometry (HDX-MS) to characterize SufS-SufE interactions and protein dynamics. HDX-MS analysis shows that SufE binds near the SufS active …