SEMINAR: Bayliss Seminar Series
|
|
Bayliss Seminar Series : The LINK to a Yin and Yang Mechanism of Enzyme Allostery |
Other events...
|
of enzyme allostery may not apply to DHDPS.
However, we show using biophysical analyses that DHDPS from Triticum aestivum (i.e. bread
wheat) is allosterically regulated by lysine-induced dissociation of the active oligomeric
species. This represents a rare example of the morpheein allosteric model – also known as the
dissociative concerted mechanism – first proposed by Jaffe in 2005.
Interestingly, our studies suggest that DHDPS is regulated by morpheein principles, but that
the mechanism is different in bacterial and plant species. Moreover, the allosteric model
appears to be a dissociative concerted process for T. aestivum DHDPS, where the binding of
lysine induces dissociation of active tetramers to inactive dimers. By contrast, the binding of
lysine to DHDPS from the bacterium Vibrio cholerae appears to conform to an associative
concerted mechanism, where lysine induces association of the active dimeric form to an
inactive tetrameric state. This is the first case where opposing morpheein principles have been
observed for orthologues from bacteria and plants. Accordingly, this mechanism has been
coined the Ligand-Induced dis/associatioN by Lysine (K) (LINK) model, which offers insight
into the evolution of enzyme allostery and quaternary structure.
Speaker(s) |
Matthew A. Perugini, Department of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe University, Melbourne
|
Location |
Bayliss Lecture Theatre G:33
|
|
Contact |
The School of Chemistry and Biochemistry Team
<[email protected]>
: 6488 4402
|
Start |
Tue, 09 Aug 2016 13:00
|
End |
Tue, 09 Aug 2016 14:00
|
Submitted by |
scbevents <[email protected]>
|
Last Updated |
Mon, 08 Aug 2016 15:16
|
Included in the following Calendars: |
|
- Locations of venues on the Crawley and Nedlands campuses are
available via the Campus Maps website.
- Download this event as:
Text |
iCalendar
-
Mail this event:
|