Glycerol-3-Phosphate Dehydrogenase: Difference between revisions

Michal Harel (talk | contribs)
No edit summary
Michal Harel (talk | contribs)
No edit summary
Line 16: Line 16:
<scene name='Sandbox_189/Fad/2'>FAD Active Site</scene>
<scene name='Sandbox_189/Fad/2'>FAD Active Site</scene>


The N-terminal FAD-Domain exists in each monomer subunit of GlpD and is embedded into the phospholipid membrane bilayer.Substrate binding occurs at this domain which causes a conformational change to the structure of the GlpD enzyme. The FAD-domain plays a major role in metabolism and energy synthesis.
The N-terminal FAD-Domain exists in each monomer subunit of GlpD and is embedded into the phospholipid membrane bilayer.Substrate binding occurs at this domain which causes a conformational change to the structure of the GlpD enzyme. The FAD-domain plays a major role in metabolism and energy synthesis.  The active site is found in a cleft between the two domains<ref>PMID:14717590</ref>.


===Function===
===Function===

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Andrea Gorrell, Indu Toora, Andrew Rebeyka, David Canner, Michal Harel, Jaime Prilusky, Alexander Berchansky