Sandbox Reserved 951: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 40: | Line 40: | ||
=====Interaction with luciferin===== | =====Interaction with luciferin===== | ||
Luciferase holds the luciferin with the specific residues <scene name='60/604470/Residues_helding_luciferin/1'>arginin 218, phenylalanin 247, serin 347 and adenin 348</scene>, still with hydrogen bounds. This bindings makes the carboxylate oxygen of luciferin points toward the α phosphate of ATP, so the oxygen is well-positionned to attack the α phosphate. This promotes the luciferin-AMP formation. | Luciferase holds the luciferin with the specific residues <scene name='60/604470/Residues_helding_luciferin/1'>arginin 218, phenylalanin 247, serin 347 and adenin 348</scene>, still with hydrogen bounds. This bindings makes the carboxylate oxygen of luciferin points toward the α phosphate of ATP, so the oxygen is well-positionned to attack the α phosphate. This promotes the luciferin-AMP formation. | ||
=====Interaction with fatty acids===== | =====Interaction with fatty acids===== | ||
Fatty acids are highly similar to luciferin. Therefore, luciferase can use the luciferin binding site to bind fatty acids. That is why they can be used as substrates by luciferase and then, very high similar reaction as for luciferin occurs. | Fatty acids are highly similar to luciferin. Therefore, luciferase can use the luciferin binding site to bind fatty acids. That is why they can be used as substrates by luciferase and then, very high similar reaction as for luciferin occurs. | ||
[[Image:Luciferin_fatty-acid.gif| | [[Image:Luciferin_fatty-acid.gif|250px|left|thumb|Comparison of the chemical structures of (A) firefly | ||
D-LH2 and (B) arachidonic acid]] | D-LH2 and (B) arachidonic acid]] | ||
