2jev: Difference between revisions
No edit summary |
No edit summary |
||
| Line 31: | Line 31: | ||
[[Category: transferase]] | [[Category: transferase]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 17:32:08 2007'' | ||
Revision as of 18:27, 30 October 2007
|
CRYSTAL STRUCTURE OF HUMAN SPERMINE,SPERMIDINE ACETYLTRANSFERASE IN COMPLEX WITH A BISUBSTRATE ANALOG (N1-ACETYLSPERMINE-S-COA).
OverviewOverview
The N1-acetylation of spermidine and spermine by spermidine/spermine, acetyltransferase (SSAT) is a crucial step in the regulation of the, cellular polyamine levels in eukaryotic cells. Altered polyamine levels, are associated with a variety of cancers as well as other diseases, and, key enzymes in the polyamine pathway, including SSAT, are being explored, as potential therapeutic drug targets. We have expressed and purified, human SSAT in Escherichia coli and characterized its kinetic and chemical, mechanism. Initial velocity and inhibition studies support a random, sequential mechanism for the enzyme. The bisubstrate analogue, N1-spermine-acetyl-coenzyme A, exhibited linear, competitive inhibition, against both substrates with a true Ki of 6 nM. The pH-activity profile, was bell-shaped, ... [(full description)]
About this StructureAbout this Structure
2JEV is a [Single protein] structure of sequence from [Homo sapiens] with NHQ as [ligand]. Active as [Diamine N-acetyltransferase], with EC number [2.3.1.57]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Mechanistic and structural analysis of human spermidine/spermine N1-acetyltransferase., Hegde SS, Chandler J, Vetting MW, Yu M, Blanchard JS, Biochemistry. 2007 Jun 19;46(24):7187-95. Epub 2007 May 22. PMID:17516632
Page seeded by OCA on Tue Oct 30 17:32:08 2007