베타-갈락토시다아제에 대한 금속 이온의 억제 효과 비교
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- 2021.08.04
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- 2016.02
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"베타-갈락토시다아제에 대한 금속 이온의 억제 효과 비교"에 대한 내용입니다.
목차
1. Introduction
2. Methods
3. Results
4. Discussion
본문내용
Introduction
There are mainly two ways to inhibit enzymes which are competitive and noncompetitive inhibitors. The significant difference between competitive and noncompetitive inhibitor is that a molecule will bind to an enzyme at either active site or the other site to inhibit any further reaction. In noncompetitive inhibition, an enzyme will be bound with noncompetitive inhibitor and there will be a change in an active site of the enzyme. Consequently, a substrate cannot bind to the changed-active site, unless the noncompetitive inhibitor leaves. Heavy metal poisoning is one of the examples of noncompetitive inhibitor of an enzyme due to no competition for the active site. In addition, covalent bond will be formed by heavy metal ions and affect to change the tertiary structure so that the shape of the active site will be changed (Berg, Tymoczko and Stryer, 2002).
β-galactosidase [3.2.1.23] (Escherichia coli) has four polypeptide chains with 1,023 amino acids per a monomer.
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