Organic solvent changes the chymotrypsin specificity with respect to nucleophiles.
In alpha-chymotrypsin-catalyzed acyl-transfer reactions in water the specificity of the enzyme (the nucleophile reactivity of amino acid amides) is correlated with the substrate hydrophobicity and increases as the hydrophobicity of the side chain of the amino acid amides is increased. In a low water system (4% H2O) bulky amino acid amides are less efficient nucleophiles. The specificity of alpha-chymotrypsin towards the amino acid amides in acyl transfer reactions in this case does not depend on the hydrophobicity of the amino acid side chains but correlates with their size. Therefore, different factors can be responsible for the specificity of enzymes in water and in a mainly organic medium.
Gololobov MYu
Department of Biotechnology, University of Lund, Sweden.
Voyushina
T L
TL
Stepanov
V M
VM
Adlercreutz
P
P
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002918:Chymotrypsin / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D010179:Pancreas / Q000201:enzymology; D012997:Solvents; D013379:Substrate Specificity; D014867:Water
D012997:Solvents; D014867:Water; D002918:Chymotrypsin