This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
Sandbox Wabash 21 Fumarase
From Proteopedia
(Difference between revisions)
(New page: ==Your Heading Here (Wabash Sandbox 21 Fumarase (Brady Boles))== <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> This is a default text...) |
|||
| Line 1: | Line 1: | ||
==Your Heading Here (Wabash Sandbox 21 Fumarase (Brady Boles))== | ==Your Heading Here (Wabash Sandbox 21 Fumarase (Brady Boles))== | ||
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | ||
| - | This | + | The enzyme known as fumarase catalyzes the conversion of malate to fumarase. Crystallographic studies using inhibitors revealed that the inhibitors bound to two different locations. This indicated that there were two potential active sites for fumarase. Site A was located within a pit and was made up of atoms from 3 of the 4 subunits present within fumarase. Site B was located towards the surface of the enzyme and was made up of only 1 of the 4 subunits. Debate about which of the sites was the true active site was centered around the fact that there was no known monomeric fumarase. Since site A was made up of atoms from multiple subunits, site A seemed like the likely active site for fumarase. This was tested by mutating the catalytic His on both of the sites and observing the amount of fumarase activity. |
| - | + | ||
== Function == | == Function == | ||
Revision as of 08:25, 28 February 2016
Your Heading Here (Wabash Sandbox 21 Fumarase (Brady Boles))
| |||||||||||
