User:Matt Whelihan: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 12: | Line 12: | ||
These seven highly conserved amino acids identify the <scene name='User:Matt_Whelihan/Active_site_residues/1'>active site</scene> which is located in the large hydrophobic cleft between the two adjacent N and C-terminal domains. | These seven highly conserved amino acids identify the <scene name='User:Matt_Whelihan/Active_site_residues/1'>active site</scene> which is located in the large hydrophobic cleft between the two adjacent N and C-terminal domains. | ||
Firefly luciferases catalyze the formation of the <scene name='User:Matt_Whelihan/Complete_active_site/1'>luciferin-adenylate intermediate</scene>. A proton is then abstracted in a steriospecific manner from the C-4 carbon, presumably by an <font color='gold'>enzyme base</font> believed to be <scene name='User:Matt_Whelihan/Complete_active_site/3'>Thr343</scene>. A conformational change then occurs which allows molecular oxygen addition to the newly formed anion. As the highly reactive dioxetanone intermediate decays to the ground state, it releases a photon of light<ref>PMID:7000855</ref><ref>PMID:4813372</ref>. | Firefly luciferases catalyze the formation of the <scene name='User:Matt_Whelihan/Complete_active_site/1'>luciferin-adenylate intermediate</scene>. A proton is then abstracted in a steriospecific manner from the C-4 carbon, presumably by an <font color='gold'>enzyme base</font> believed to be <scene name='User:Matt_Whelihan/Complete_active_site/3'>Thr343</scene>. A conformational change then occurs which allows molecular oxygen addition to the newly formed anion. As the highly reactive dioxetanone intermediate decays to the ground state, it releases a photon of light<ref>PMID:7000855</ref><ref>PMID:4813372</ref>. | ||
[[Image:redgreen.jpg]] | [[Image:redgreen.jpg]] | ||
