Show simple item record

dc.contributor.authorThongkham, Jaylong Wong
dc.creatorThongkham, Jaylong Wongen_US
dc.date.accessioned2011-10-24T19:16:47Z
dc.date.available2011-10-24T19:16:47Z
dc.date.issued2010-05
dc.identifier.urihttp://hdl.handle.net/10150/146665
dc.description.abstractRecently, a 22nd amino acid has been discovered, pyrrolysine. Pyrrolysine (pyl) is coded by the translation of a amber (UAG) codon. Pyl was first found in the active site for genes encoding for methylamine methyltransferases in Methanosarcinaceae. New discoveries have now identified pyl in the Gram-positive Desulfitobacterium hafniense, but the pylS gene is divided in half -- one corresponding to the C-terminal and one corresponding to the N-terminal of archaeal pylS. The pylBCD genes are responsible for the biosynthesis of pyrrolysine. Each pyl gene was cloned into E. coli to overexpress the protein in attempts to run kinetic reactions to determine the biosynthetic mechanism of pyrrolysine. The pylB and pylC genes have been successfully cloned into E. coli and proteins will be overexpressed. However, the pylD gene could not be ligated into pET28a vector. The pylB and pylC proteins will be expressed and purified.
dc.language.isoenen_US
dc.publisherThe University of Arizona.en_US
dc.rightsCopyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author.en_US
dc.titleStudies on Pyrrolysine - The 22nd Amino Aciden_US
dc.typetexten_US
dc.typeElectronic Thesisen_US
thesis.degree.grantorUniversity of Arizonaen_US
thesis.degree.levelbachelorsen_US
thesis.degree.disciplineHonors Collegeen_US
thesis.degree.disciplineBiochemistry and Molecular Biophysicsen_US
thesis.degree.nameB.S.en_US
refterms.dateFOA2018-06-27T11:50:56Z
html.description.abstractRecently, a 22nd amino acid has been discovered, pyrrolysine. Pyrrolysine (pyl) is coded by the translation of a amber (UAG) codon. Pyl was first found in the active site for genes encoding for methylamine methyltransferases in Methanosarcinaceae. New discoveries have now identified pyl in the Gram-positive Desulfitobacterium hafniense, but the pylS gene is divided in half -- one corresponding to the C-terminal and one corresponding to the N-terminal of archaeal pylS. The pylBCD genes are responsible for the biosynthesis of pyrrolysine. Each pyl gene was cloned into E. coli to overexpress the protein in attempts to run kinetic reactions to determine the biosynthetic mechanism of pyrrolysine. The pylB and pylC genes have been successfully cloned into E. coli and proteins will be overexpressed. However, the pylD gene could not be ligated into pET28a vector. The pylB and pylC proteins will be expressed and purified.


Files in this item

Thumbnail
Name:
azu_etd_mr20100145_sip1_m.pdf
Size:
607.6Kb
Format:
PDF

This item appears in the following Collection(s)

Show simple item record