Protein engineering of chymosin; modification of the optimum pH of enzyme catalysis.

doi:10.1093/protein/3.7.605

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Article

Protein engineering of chymosin; modification of the optimum pH of enzyme catalysis.

Protein engineering - 1 Jul 1990

Mantafounis D, Pitts J

Abstract excerpt

The aspartic proteinase chymosin exhibits a local network of hydrogen bonds involving the active site aspartates and surrounding residues which may have an influence on the rate and optimal pH of substrate cleavage. We have introduced into chymosin B the following substitutions: Asp304 to Ala (D3...

Topics

Amino Acid Sequence
Binding Sites
Catalysis
Chymosin
Escherichia coli
Hydrogen Bonding
Hydrogen-Ion Concentration
Molecular Sequence Data
Mutation
Protein Conformation
Protein Engineering

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