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The enzyme DNA-(apurinic or apyrimidinic site) lyase, also referred to as DNA-(apurinic or apyrimidinic site) 5'-phosphomonoester-lyase (systematic name) or DNA AP lyase (EC 4.2.99.18) catalyzes the cleavage of the C-O-P bond 3' from the apurinic or apyrimidinic site in DNA via β-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate. [1]
Enzymes act on small molecules called substrates, which an enzyme converts into products. Almost all metabolic processes in the cell need enzyme catalysis in order to occur at rates fast enough to sustain life. The study of how fast an enzyme can transform a substrate into a product is called enzyme kinetics.
This course is designed for students who wish to pursue an interest in the life sciences. The College Board recommends successful completion of high school biology and high school chemistry [2] before commencing AP Biology, although the actual prerequisites vary from school to school and from state to state.
The collective goal is to contribute excellent biology diagrams to the Commons and to corresponding Wikipedia articles. This is done as part of an Advanced Placement Biology course. The lead editor is Chris Packard. This project is inspired by the 2009 Wikipedia AP Biology Project. There are many basic and important diagrams missing from ...
Enzyme denaturation is normally linked to temperatures above a species' normal level; as a result, enzymes from bacteria living in volcanic environments such as hot springs are prized by industrial users for their ability to function at high temperatures, allowing enzyme-catalysed reactions to be operated at a very high rate.
Biochemistry, or biological chemistry, is the study of chemical processes within and relating to living organisms. [1] A sub-discipline of both chemistry and biology, biochemistry may be divided into three fields: structural biology, enzymology, and metabolism. Over the last decades of the 20th century, biochemistry has become successful at ...
AP site reactivity. AP sites are extremely reactive. They fluctuate between a furanose ring and an open-chain free aldehyde and free alcohol conformation. Exposure to a nucleophile can cause a β-elimination reaction, wherein the 3' phosphoester bond is broken, causing a single-stranded break.
Carboxypeptidase A and the target enzyme of Captopril, angiotensin-converting enzyme, have very similar structures, as they both contain a zinc ion within the active site. This allowed for a potent carboxypeptidase A inhibitor to be used to inhibit the enzyme and, thus, lower blood pressure through the renin-angiotensin-aldosterone system. [1]
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