Compare the structures of ribonuclease A,DNA polymerase I and tryptophan synthase, in each case explaining how the structure relates to the enzymatic activity. Structural Analysis of Ribonuclease A, DNA Polymerase I and Tryptophan Synthase Enzymes

Structure Analysis of Ribonuclease I, DNA Polymerase I, and Tryptophan Synthase enzymes

Ribonuclease A, also known as RNase A, is a type endoribonuclease enzyme involved in hydrolysis single-strandedRNA into its constituent nucleotides. It is made up of two domains: a catalytic and an RNA binding domain. The enzyme has a globular structure and a deep crack between its two domains. In the cleft are the catalytic site and active residues. These interact with the backbone of RNA to aid in cleavage. On the other side, the RNA-binding domain contains several amphipathic helices which enable the enzyme to bind with the target RNA, and then stabilize it for hydrolysis. DNA Polymerase I (Pol I), a DNA-dependent DNA Polymerase, is an enzyme that plays a role in DNA repair and replication. It is a rod-like structure that consists of two domains: the thumb domain and the palm domain. The thumb domain binds the DNA template while the palmdomain houses active sites for catalytic activation. Cont…

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