Active site

The area where substrates and co-factors bind to the enzyme is called the active site. This is where the catalysis takes place. An active site often appears like a pocket, and consists of several amino acids which can have specific interactions with the substrate [1]. Figure 1 shows the active site of alcohol dehydrogenase where NAD⁺ binds. Amino acid residue 47, which is responsible for the Alcohol Flush syndrome, is located in this active site, and this amino acid is important in binding to NAD⁺. Figure 1 shows the active site of alcohol dehydrogenase where N A D plus binds. Amino acid residue 47, which is responsible for the Alcohol Flush syndrome, is located in this active site, and this amino acid is important in binding to N A D plus. If a mutation causes an amino acid substitution on this residue, the kinetic parameters may be altered, which is the case in the Alcohol Flush syndrome.

Figure 1: Surface model of alcohol dehydrogenase showing the active site (blue) for NAD⁺ N A D plus (red) binding. Generated with PyMOL from PDB entry 1HSZ

References

1. Lehninger, Albert L.; Nelson, David L.; Cox, Michael M. (2008). Principles of Biochemistry (5th ed.). New York, NY: W.H. Freeman and Company. ISBN 978-0-7167-7108-1.

ADH Substrate

Theory overview