Fumarase 2: Difference between revisions
From Proteopedia
Jump to navigationJump to search
Ann Taylor (talk | contribs) No edit summary |
Ann Taylor (talk | contribs) No edit summary |
||
| Line 1: | Line 1: | ||
=Fumarase= | =Fumarase= | ||
[[Image:Fumarase biological unit.JPG|right|300px]] | |||
===Overview=== | ===Overview=== | ||
| Line 7: | Line 8: | ||
===Stucture and Classification=== | ===Stucture and Classification=== | ||
Fumarase is classified as an all alpha protein which belongs to the L-aspartase/fumarase family, and the enzyme specifically consists of four identical subunits which form a tetramer. From the four subunits, fumarase has three domains which comprise two binding sites: the active site and B site. Although the active site has a mostly solid structure and shifts very little when it binds, the B site shifts substantially more upon binding, and this shift helps regulate affinity for molecule binding at the active site ( | Fumarase is classified as an all alpha protein which belongs to the L-aspartase/fumarase family, and the enzyme specifically consists of four identical subunits which form a tetramer (see image on right). From the four subunits, fumarase has three domains which comprise two binding sites: the active site and B site. Although the active site has a mostly solid structure and shifts very little when it binds, the B site shifts substantially more upon binding, and this shift helps regulate affinity for molecule binding at the active site <ref>Weaver,T. Structure of free fumarase C from 'Escherichia coli. Acta Crystallographica' (2005). [http://dx.doi.org/10.1107 DOI: 10.1107 </ref> | ||
[ | |||
