Oxyanion hole
An oxyanion hole is a pocket in the structure of an enzyme which stabilizes a deprotonated oxygen or alkoxide, often by placing it close to positively charged residues. This can contribute to binding affinity in two ways:
- It may directly stabilize the transition state of a reaction by stabilizing the anion (such as in the tetrahedral intermediate formed in the proteolytic reaction catalyzed by chymotrypsin)
- It may allow for insertion or positioning of a substrate which would suffer from steric hindrance if it could not occupy the hole (such as BPG in hemoglobin).
See also
- Serine proteases#Catalytic mechanism
References
- Albert Lehninger et al. (2008). Principles of Biochemistry (5th ed.). Macmillan. p. 207.