Sandbox 212: Difference between revisions

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The exact role of the '''trimethylammonium group''' of carnitine hasn’t been fully revealed yet. Even though this group has a positive charge on its nitrogen it is not surrounded by negatively charged residues which could balance it. Instead, the trimethylammonium group is situated in a rather hydrophobic environment.
The exact role of the '''trimethylammonium group''' of carnitine hasn’t been fully revealed yet. Even though this group has a positive charge on its nitrogen it is not surrounded by negatively charged residues which could balance it. Instead, the trimethylammonium group is situated in a rather hydrophobic environment.


There are only  slight conformational changes in the enzyme upon carnitine binding.
There are only  slight conformational changes in the enzyme upon carnitine binding.“The only significant conformational difference in the active site between the free enzyme and the carnitine complex is in the side chain of <font color='#90E050'>'''serine454'''</font>, which adopts a different rotamer to have better hydrogen-bonding interactions with the carboxylate of carnitine.” (Cry. Structure)
“The only significant conformational difference in the active site between the free enzyme and the carnitine complex is in the side chain of <font color='#90E050'>'''serine454'''</font>, which adopts a different rotamer to have better hydrogen-bonding interactions with the carboxylate of carnitine.” (Cry. Structure)
</StructureSection>
</StructureSection>
== Substrate binding and mechanism ==
== Substrate binding and mechanism ==