What is the catalytic triad of chymotrypsin?

What is the catalytic triad of chymotrypsin?

Chymotrypsin contains a collection of three amino acids called the catalytic triad. This triad consists of serine-195, histidine-57 and aspartate-102. These amino acids work together to carry out the catalytic function of breaking peptide bonds.

What is the function of subtilisin?

Subtilisin is a protease (a protein-digesting enzyme) initially obtained from Bacillus subtilis. Subtilisins belong to subtilases, a group of serine proteases that – like all serine proteases – initiate the nucleophilic attack on the peptide (amide) bond through a serine residue at the active site.

What makes up the catalytic triad?

A catalytic triad is a set of three coordinated amino acids that can be found in the active site of some enzymes. Catalytic triads are most commonly found in hydrolase and transferase enzymes (e.g. proteases, amidases, esterases, acylases, lipases and β-lactamases).

Where does subtilisin cleave?

Subtilisin is a serine protease. A 77 amino acid propeptide is cleaved from the N-terminus of pro-Sub to create the mature active enzym.

What is the catalytic triad of subtilisin?

Subtilisins are a family of serine proteases, i.e. they possess an essential serine residue at the active site. This serine residue is part of a catalytic triad of Aspartate, Histidine and Serine that is very similar to that of mammalian intestinal digestive enzymes, trypsin and chymotrypsin.

How is subtilisin produced?

Subtilisin (EC 3.4. 21.62) is a type of serine protease that is of high commercial importance. It is mainly produced by Bacillus species as an extra cellular enzyme. Subtilisin being stable over a wide range of pH and temperature is exploited as a detergent enzyme and also favoured by its non-specificity.

Why is the catalytic triad important?

The catalytic triad provides a paradigm for the structural and chemical features of enzymes that allow them to facilitate a difficult reaction. The reaction in this case is hydrolysis of a peptide bond, which – although thermodynamically favorable – is kinetically inaccessible under normal physiological conditions.

Where is subtilisin found?

Subtilisins are to be found in archaebacteria, eubacteria, eukaryotes and viruses. The bacterial subtilisins are the subgroup of serine proteases of greater industrial significance and have been studied extensively, with regard to improving their catalytic efficiency and stabilities.

What is the function of catalytic triad?

What is Maxatase?

Maxatase is trademark of a protease used in laundry detergent. It is very similar to Alcalase. It is a subtilisin produced by Bacillus licheniformis.

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