4. The amino acid Asp189 lies at the base of the substrate specificity pocket in the enzyme trypsin. a. How is this related to typsin’s substrate specificity? Briefly describe the interactions between the substrate and the Asp 189. b. If the Asp189 was replaced with a lysine residue, how would this affect substrate specificity? c. The scientists that actually mutated the Asp189 to a lysine analyzed the three-dimensional structure of the enzyme and found that the lysine is actually not located in the specificity pocket. Instead, the Lys side chain reaches out of the base of the pocket, rendering the pocket nonpolar. With this additional information, determine how the substrate specificity would differ in the lysine-mutated enzyme.
Neutral Amino Acids
Amino acids which do not have any charge on them are neutral amino acids.
Globular Protein
The globular proteins refer to the shape of protein specifically spherical in nature apart from spherical form fibrous, disordered and membrane-bound proteins exist. These globular proteins are miscible in water and form a colloidal solution rather than other types which might not exhibit solubility. Many classes of the fold are found in globular proteins, which render them a sphere shape. Globular fold containing proteins usually are referred to by the term globin.
Dimer
Dimers are basic organic compounds, which are derivates of oligomers. It is formed by the combination of two monomers which could potentially be strong or weak and in most cases covalent or intermolecular in nature. Identical monomers are called homodimer, the non-identical dimers are called heterodimer. The method by which dimers are formed is known as “dimerization”.
Dipeptide
A dipeptide is considered a mixture of two distinct amino acids. Since the amino acids are distinct, based on their composition, two dipeptide's isomers can be produced. Various dipeptides are biologically essential and are therefore crucial to industry.
4. The amino acid Asp189 lies at the base of the substrate specificity pocket in the enzyme trypsin.
a. How is this related to typsin’s substrate specificity? Briefly describe the interactions between the substrate and the Asp 189.
b. If the Asp189 was replaced with a lysine residue, how would this affect substrate specificity?
c. The scientists that actually mutated the Asp189 to a lysine analyzed the three-dimensional structure of the enzyme and found that the lysine is actually not located in the specificity pocket. Instead, the Lys side chain reaches out of the base of the pocket, rendering the pocket nonpolar. With this additional information, determine how the substrate specificity would differ in the lysine-mutated enzyme.
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