dc.contributor.author |
Payne, LS |
|
dc.contributor.author |
Brown, PM |
|
dc.contributor.author |
Middleditch, MJ |
|
dc.contributor.author |
Baker, EN |
|
dc.contributor.author |
Cooper, GJS |
|
dc.contributor.author |
Loomes, KM |
|
dc.coverage.spatial |
England |
|
dc.date.accessioned |
2022-06-19T22:35:32Z |
|
dc.date.available |
2022-06-19T22:35:32Z |
|
dc.date.issued |
2008 |
|
dc.identifier.citation |
(2008). Biochemical Journal, 416(2), 281-288. |
|
dc.identifier.issn |
0264-6021 |
|
dc.identifier.uri |
https://hdl.handle.net/2292/59994 |
|
dc.description.abstract |
The modification of proteins by reducing sugars through the process of non-enzymatic glycation is one of the principal mechanisms by which hyperglycaemia may precipitate the development of diabetic complications. Fn3K (fructosamine 3-kinase) and Fn3KRP (Fn3K-related protein) are two recently discovered enzymes that may play roles in metabolizing early glycation products. However, although the activity of these enzymes towards various glycated substrates has been established, very little is known about their structure-function relationships or their respective mechanisms of action. Furthermore, their only structural similarities noted to date with members of other kinase families has been with the bacterial aminoglycoside kinases. In the present study, we employed affinity labelling with the ATP analogue FSBA {5'-p-[(fluorosulfonyl)benzoyl]adenosine} to probe the active-site topology of Fn3KRP as an example of this enigmatic family of kinases. FSBA was found to modify Fn3KRP at five distinct sites; four of these were predicted to be localized in close proximity to its ATP-binding site, based on alignments with the aminoglycoside kinase APH(3')-IIIa, and examination of its published tertiary structure. The results of the present studies provide evidence that Fn3KRP possesses an ATP-binding domain that is structurally related to that of both the aminoglycoside kinases and eukaryotic protein kinases. |
|
dc.format.medium |
Print |
|
dc.language |
eng |
|
dc.publisher |
Portland Press Ltd. |
|
dc.relation.ispartofseries |
Biochem. J. |
|
dc.rights |
Items in ResearchSpace are protected by copyright, with all rights reserved, unless otherwise indicated. Previously published items are made available in accordance with the copyright policy of the publisher. |
|
dc.rights.uri |
https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm |
|
dc.subject |
Cell Line, Tumor |
|
dc.subject |
Humans |
|
dc.subject |
Lung Neoplasms |
|
dc.subject |
Muramidase |
|
dc.subject |
Trypsin |
|
dc.subject |
Phosphotransferases (Alcohol Group Acceptor) |
|
dc.subject |
Kanamycin Kinase |
|
dc.subject |
Protein Kinases |
|
dc.subject |
Recombinant Proteins |
|
dc.subject |
Adenosine |
|
dc.subject |
DNA Primers |
|
dc.subject |
Adenosine Triphosphate |
|
dc.subject |
Affinity Labels |
|
dc.subject |
Reverse Transcriptase Polymerase Chain Reaction |
|
dc.subject |
Binding Sites |
|
dc.subject |
Glycosylation |
|
dc.subject |
1.1 Normal biological development and functioning |
|
dc.subject |
2.1 Biological and endogenous factors |
|
dc.subject |
Science & Technology |
|
dc.subject |
Life Sciences & Biomedicine |
|
dc.subject |
Biochemistry & Molecular Biology |
|
dc.subject |
SUBSTRATE-SPECIFICITY |
|
dc.subject |
AMINOGLYCOSIDE PHOSPHOTRANSFERASE |
|
dc.subject |
DIABETIC COMPLICATIONS |
|
dc.subject |
NUCLEOTIDE-BINDING |
|
dc.subject |
IDENTIFICATION |
|
dc.subject |
KINASES |
|
dc.subject |
SITES |
|
dc.subject |
APH(3')-IIIA |
|
dc.subject |
PURIFICATION |
|
dc.subject |
3-PHOSPHATE |
|
dc.subject |
0601 Biochemistry and Cell Biology |
|
dc.subject |
Biomedical |
|
dc.subject |
Basic Science |
|
dc.subject |
03 Chemical Sciences |
|
dc.subject |
06 Biological Sciences |
|
dc.subject |
11 Medical and Health Sciences |
|
dc.title |
Mapping of the ATP-binding domain of human fructosamine 3-kinase-related protein by affinity labelling with 5′-[p-(fluorosulfonyl)benzoyl]adenosine |
|
dc.type |
Journal Article |
|
dc.identifier.doi |
10.1042/BJ20080389 |
|
pubs.issue |
2 |
|
pubs.begin-page |
281 |
|
pubs.volume |
416 |
|
dc.date.updated |
2022-05-03T04:39:24Z |
|
dc.rights.holder |
Copyright: The author |
en |
dc.identifier.pmid |
18637789 (pubmed) |
|
pubs.author-url |
https://www.ncbi.nlm.nih.gov/pubmed/18637789 |
|
pubs.end-page |
288 |
|
pubs.publication-status |
Published |
|
dc.rights.accessrights |
http://purl.org/eprint/accessRights/RestrictedAccess |
en |
pubs.subtype |
Article |
|
pubs.elements-id |
92031 |
|
pubs.org-id |
Science |
|
pubs.org-id |
Biological Sciences |
|
pubs.org-id |
Science Research |
|
pubs.org-id |
Maurice Wilkins Centre (2010-2014) |
|
dc.identifier.eissn |
1470-8728 |
|
dc.identifier.pii |
BJ20080389 |
|
pubs.record-created-at-source-date |
2022-05-03 |
|
pubs.online-publication-date |
2008-11-12 |
|