Sandbox 212: Difference between revisions

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The exact role of the '''trimethylammonium group''' during carnitine binding hasn’t been fully revealed yet. Carnitine is rather required for catalysis than for binding. Even though the trimethylammonium 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''' during carnitine binding hasn’t been fully revealed yet. Carnitine is rather required for catalysis than for binding. Even though the trimethylammonium 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.“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.” <ref name="rasmol" /></StructureSection>
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.” <ref name="structure" /></StructureSection>
==Catalytic Mechanism of Carnitine Acyltransferases==
==Catalytic Mechanism of Carnitine Acyltransferases==
[[Image:Machanism fatty acid transfer.jpg|thumb|700px|left]]
[[Image:Machanism fatty acid transfer.jpg|thumb|700px|left]]