Hey scientists, can you use your creativity to think about any and all effects a mutation might have on an enzyme?
I know most are deleterious, but some increase Vmax or lower Km or change substrate specificity. What else could a mutation do?
Adam B Shapiro
Popular answer
- Prevent the protein from folding correctly.
- Cause the protein to self associate when it isn't supposed to (sickle cell hemoglobin being the textbook example)
- Prevent the protein from self-associating or associating with other proteins, or change the affinity of such interactions
- Change the affinity of the protein for a ligand
- Increase or decrease the thermal stability of the protein
- Change the biological half-life of the protein by changing its interaction with cellular mechanisms for protein turnover (e.g. N-end rule)
- Alter post-translational modification (glycosylation, phosphorylation, acetylation, etc.)
- Prevent the covalent attachment of a prosthetic group
- Make the protein more or less likely to form crystals useful for x-ray crystallography
- Interfere with conformational changes required for catalysis or signaling, or for time-dependent inhibition by ligands
- Change the rate of translation
- Interfere with or enhance progression through the secretory pathway
- Interfere or enhance removal of a signal sequence
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Adam B Shapiro
- Prevent the protein from folding correctly.
- Cause the protein to self associate when it isn't supposed to (sickle cell hemoglobin being the textbook example)
- Prevent the protein from self-associating or associating with other proteins, or change the affinity of such interactions
- Change the affinity of the protein for a ligand
- Increase or decrease the thermal stability of the protein
- Change the biological half-life of the protein by changing its interaction with cellular mechanisms for protein turnover (e.g. N-end rule)
- Alter post-translational modification (glycosylation, phosphorylation, acetylation, etc.)
- Prevent the covalent attachment of a prosthetic group
- Make the protein more or less likely to form crystals useful for x-ray crystallography
- Interfere with conformational changes required for catalysis or signaling, or for time-dependent inhibition by ligands
- Change the rate of translation
- Interfere with or enhance progression through the secretory pathway
- Interfere or enhance removal of a signal sequence
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Luisa Moretto
Depending on where the mutation is located it can change the surface of a protein and therefore change the interaction with partner molecules or ligands. Protein-protein interaction can be affect positively or negatively.
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Engelbert Buxbaum
Many mutations also affect the mRNA by introducing or removing splice sites (15% of clinically important mutations) or by affecting its synthesis, translation or degradation. Introduction of stop-codons has also been observed.
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