Covalent catalysis may use amino acids such as aspartate or lysine for protonation or proton abstraction.
The amino acid serving as a preferred acid needs to have a pKa more than physiological pH, in order that it's miles protonated in the enzyme lively website. not unusual amino acid residues able to act that function include His, Cys, Tyr, Lys, and Arg (all have pKa's close to or above 7).
Covalent catalysis involves the formation of a covalent bond between the enzyme and at least one of the substrates involved in the response. regularly times this entails nucleophilic catalysis that's a subclass of covalent catalysis.
This includes methionine, phenylalanine, tyrosine, and tryptophan. Chymotrypsin contains a serine amino acid within the energetic website that plays a prime nucleophilic position that catalyzes the hydrolysis of peptide bonds. The active site makes use of covalent catalysis and carries out a two-step system.
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