Lysine: N 6 -Hydroxylase: Stability and Interaction with Ligands
dc.contributor.author | Marrone, Laura | en_US |
dc.contributor.author | Dick, Scott | en_US |
dc.contributor.author | Duewel, Henry | en_US |
dc.contributor.author | Beecroft, Michael | en_US |
dc.contributor.author | McCourt, Jennifer | en_US |
dc.contributor.author | Viswanatha, Thammaiah | en_US |
dc.date.accessioned | 2006-09-11T15:39:19Z | |
dc.date.available | 2006-09-11T15:39:19Z | |
dc.date.issued | 1999-11 | en_US |
dc.identifier.citation | Dick, Scott; Marrone, Laura; Duewel, Henry; Beecroft, Michael; McCourt, Jennifer; Viswanatha, Thammaiah; (1999). "Lysine: N 6 -Hydroxylase: Stability and Interaction with Ligands." Journal of Protein Chemistry 18(8): 893-903. <http://hdl.handle.net/2027.42/45085> | en_US |
dc.identifier.issn | 1573-4943 | en_US |
dc.identifier.issn | 0277-8033 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/45085 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=10839627&dopt=citation | en_US |
dc.description.abstract | Recombinant lysine:N 6 -hydroxylase, r IucD, which is isolated as an apoenzyme, requires FAD and NADPH for its catalytic function. r IucD preparations have been found to undergo time-dependent loss in monooxygenase function due to aggregation from the initial tetrameric state to a polytetrameric form(s), a process which is reversible by treatment with thiols. Ligand-in-duced conformational changes in r IucD were assessed by monitoring its CD spectra, DSC profile, and susceptibility to both endo- as well as exopeptidases. The first two methods indicated the absence of any significant conformational change in r IucD, while the last approach revealed that FAD, and its analog ADP, can protect the protein from the deleterious action of proteases. NADPH was partially effective and L-lysine was ineffective in this regard. Deletion of the C-terminal segment, either by treatment with carboxypeptidase Y or by mutagenesis of iucD, results in the loss of r IucD's monooxygenase activity. These findings demonstrate the crucial role of the C-terminal segment in maintaining r IucD in its native conformation. | en_US |
dc.format.extent | 1541713 bytes | |
dc.format.extent | 3115 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Kluwer Academic Publishers-Plenum Publishers; Plenum Publishing Corporation ; Springer Science+Business Media | en_US |
dc.subject.other | Ligand Protection | en_US |
dc.subject.other | Protein Stability | en_US |
dc.subject.other | Lysine Monooxygenase | en_US |
dc.subject.other | Biochemistry, General | en_US |
dc.subject.other | Mutagenesis | en_US |
dc.subject.other | Chemistry | en_US |
dc.subject.other | Organic Chemistry | en_US |
dc.subject.other | Bioorganic Chemistry | en_US |
dc.subject.other | Animal Anatomy / Morphology / Histology | en_US |
dc.subject.other | Flavoprotein | en_US |
dc.subject.other | Protease Probes | en_US |
dc.subject.other | C-terminus | en_US |
dc.title | Lysine: N 6 -Hydroxylase: Stability and Interaction with Ligands | en_US |
dc.type | Article | en_US |
dc.subject.hlbsecondlevel | Natural Resources and Environment | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbsecondlevel | Ecology and Evolutionary Biology | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | College of Pharmacy, University of Michigan, Ann Arbor, Michigan, 48109-1065 | en_US |
dc.contributor.affiliationother | Department of Chemistry, University of Waterloo, Waterloo, N2L3G1, Canada | en_US |
dc.contributor.affiliationother | Department of Chemistry, University of Waterloo, Waterloo, N2L3G1, Canada | en_US |
dc.contributor.affiliationother | Department of Chemistry, University of Waterloo, Waterloo, N2L3G1, Canada | en_US |
dc.contributor.affiliationother | Department of Chemistry, University of Waterloo, Waterloo, N2L3G1, Canada | en_US |
dc.contributor.affiliationother | Department of Chemistry, University of Waterloo, Waterloo, N2L3G1, Canada | en_US |
dc.contributor.affiliationumcampus | Ann Arbor | en_US |
dc.identifier.pmid | 10839627 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/45085/1/10930_2004_Article_409465.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1023/A:1020639514998 | en_US |
dc.identifier.source | Journal of Protein Chemistry | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
Files in this item
Remediation of Harmful Language
The University of Michigan Library aims to describe library materials in a way that respects the people and communities who create, use, and are represented in our collections. Report harmful or offensive language in catalog records, finding aids, or elsewhere in our collections anonymously through our metadata feedback form. More information at Remediation of Harmful Language.
Accessibility
If you are unable to use this file in its current format, please select the Contact Us link and we can modify it to make it more accessible to you.