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== The Catalytic Mechanism of Carnitine Acyltransferases==
== The Catalytic Mechanism of Carnitine Acyltransferases==
[[Image:Machanism fatty acid transfer.jpg|thumb|400px|left]]
[[Image:Machanism fatty acid transfer.jpg|thumb|600px|left]]
It is assumed that the whole family of carnitine acyltransferases share the same catalytic mechanism, because certain residues in the catalytic side (histidine343, serine554) are conserved throughout the family.
It is assumed that the whole family of carnitine acyltransferases share the same catalytic mechanism, because certain residues in the catalytic side (histidine343, serine554) are conserved throughout the family.
Histidine 343 is probably the most important residue in catalysis.  First, it induces optimal substrate binding by forming a hydrogen bond between the hydrogen of the substrate’s reactive group and its side chain. After all substrate attained the right position, the catalytic histidine residue is ready to extract a proton from either the hydroxyl group of carnitine or the thiol group of CoA. Thus the catalytic histidine residue can be considered as a general base in catalysis.Which proton is extracted depends on the direction of the reaction. Acyl- carnitine is formed by extracting a proton from carnitine, whereas acyl-CoA is formed by extracting a proton from CoA.  
Histidine 343 is probably the most important residue in catalysis.  First, it induces optimal substrate binding by forming a hydrogen bond between the hydrogen of the substrate’s reactive group and its side chain. After all substrate attained the right position, the catalytic histidine residue is ready to extract a proton from either the hydroxyl group of carnitine or the thiol group of CoA. Thus the catalytic histidine residue can be considered as a general base in catalysis.Which proton is extracted depends on the direction of the reaction. Acyl- carnitine is formed by extracting a proton from carnitine, whereas acyl-CoA is formed by extracting a proton from CoA.  

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Ndeye Coumba, Alina Spielmann