Sandbox Reserved 774: Difference between revisions
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=Mechanism= | =Mechanism= | ||
Protein surfaces near the active site are characterized by a positive electrostatic potential. In each structure there are several multi-chain carbonyl groups without hydrogen bonding partners in the active site. These could act in a proton transfer pathway by helping locate water molecules. Around the acetyl group, there exists a hydrophobic pocket which would stabilize the neutral charge while the substrate is bound to the enzyme once the amino group is deprotonated. | Protein surfaces near the active site are characterized by a positive electrostatic potential.<ref name=Akhlaghi>Vetting, et al. "Structure and Functions of the GNAT Superfamily of Acetyltransferases." Arch Biochem Biophys 433(2004): Web. 26 Nov. 2013.</ref> In each structure there are several multi-chain carbonyl groups without hydrogen bonding partners in the active site. These could act in a proton transfer pathway by helping locate water molecules. Around the acetyl group, there exists a hydrophobic pocket which would stabilize the neutral charge while the substrate is bound to the enzyme once the amino group is deprotonated. | ||
==Kinetic Mechanism== | ==Kinetic Mechanism== | ||
