Examples of enzyme in the following topics:
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- Synthetic molecules, called artificial enzymes, also display enzyme-like catalysis.
- Inhibitors can decrease enzyme activity; activators can increase activity.
- Many drugs and poisons are enzyme inhibitors.
- In addition, some household products use enzymes to speed up biochemical reactions (e.g., enzymes in biological washing powders break down protein or fat stains on clothes; enzymes in meat tenderizers break down proteins into smaller molecules, making the meat easier to chew).
- Industrially-produced barley enzymes are widely used in the brewing process to substitute for the natural enzymes found in barley.
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- Taq polymerase is an enzyme that was first isolated from the microbe Thermus aquaticus.
- Restriction enzymes are a specific class of enzymes isolated from various bacteria and archaea, in which they grow naturally as a means of protection against viral infection.
- The enzymes have the ability to recognize foreign DNA and cut it up.
- The bacteria and archaea from which these enzymes are isolated from have innate mechanisms to protect their own DNA sequences from these enzymes, such as methylation.
- Describe how Taq polymerase, restriction enzymes and DNA ligase are used in molecular biology
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- Carboxysomes are intracellular structures that contain enzymes involved in carbon fixation and found in many autotrophic bacteria.
- They are proteinaceous structures resembling phage heads in their morphology; they contain the enzymes of carbon dioxide fixation in these organisms.
- Similar structures are known to harbor the B12-containing coenzyme glycerol dehydratase, the key enzyme of glycerol fermentation to 1,3-propanediol, in some Enterobacteriaceae, such as Salmonella.
- Carboxysomes are bacterial microcompartments that contain enzymes involved in carbon fixation.
- These compartments are thought to concentrate carbon dioxide to overcome the inefficiency of RuBisCo (ribulose bisphosphate carboxylase/oxygenase) - the predominant enzyme in carbon fixation and the rate limiting enzyme in the Calvin cycle.
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- Enzyme-linked immunosorbent assay (ELISA) is a solid-phase enzyme immunoassay used to detect the presence of a substance in solution.
- ELISA uses a specific antibody with a covalently coupled enzyme.
- Unbound antigen is removed by washing, and a second antibody which is linked to an enzyme is allowed to bind.
- This second antibody-enzyme complex constitutes the indicator system of the test.
- The antigen serves as bridge, so the more antigen in the test solution, the more enzyme-linked antibody will bind .
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- Protease inhibitors target viral proteases which are key enzymes for the completion of viral maturation.
- Proteases are enzymes that have the ability to cut proteins into peptides.
- Protease inhibitors are short peptide-like molecules that are competitive inhibitors of the enzyme.
- Mutations in the enzyme active site and other sites, which cause conformational changes, can cause resistance.
- The drug is ritonavir depicted here with a white molecule in the middle of the enzyme structure.
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- Antimicrobial drugs inhibit nucleic acid synthesis through differences in prokaryotic and eukaryotic enzymes.
- The antimicrobial actions of these agents are a result of differences in prokaryotic and eukaryotic enzymes involved in nucleic acid synthesis.
- RNA Polymerase, an enzyme that produces RNA, from T. aquaticus pictured during elongation.
- Portions of the enzyme were made transparent so as to make the path of RNA and DNA more clear.
- The magnesium ion (yellow) is located at the enzyme active site.
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- Reverse transcriptase is an enzyme that has the ability to transcribe single-stranded DNA from a single-stranded RNA chain.
- This enzyme is also found in tumors and cancer cells.
- Drugs that inhibit the function of this enzyme are divided into three groups:
- Resistance to the non-nucleotide inhibitors is caused by mutations in the inhibitor binding site of the enzyme.
- Such mutations prevent the binding of the inhibitor to the enzyme.
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- Each of these phases are tightly regulated and require unique and specific enzymes.
- RuBisCO is identified as the most abundant enzyme on earth, to date.
- The enzyme aldolase is typically characterized as a glycolytic enzyme with the ability to split fructose 1,6-bisphosphate into DHAP and G3P.
- This process requires ATP and specific enzymes.
- After this final enzyme performs this conversion, the Calvin cycle is considered complete.
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- These proteins are commonly enzymes.
- An inactive enzyme without the cofactor is called an apoenzyme, while the complete enzyme with cofactor is the holoenzyme.
- Some enzymes or enzyme complexes require several cofactors.
- Each class of group-transfer reaction is carried out by a particular cofactor, which is the substrate for a set of enzymes that produce it and a set of enzymes that consume it.
- Here, hundreds of separate types of enzymes remove electrons from their substrates and reduce NAD+ to NADH.
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- In biochemistry, an oxidoreductase is an enzyme that catalyzes the transfer of electrons from one molecule to another.
- In biochemistry, an oxidoreductase is an enzyme that catalyzes the transfer of electrons from one molecule, the reductant, also called the electron donor, to another the oxidant, also called the electron acceptor.
- This group of enzymes usually utilizes NADP or NAD+ as cofactors.
- For example, an enzyme that catalyzed this reaction would be an oxidoreductase: A– + B → A + B–.
- Oxidoreductases are classified as EC 1 in the EC number classification of enzymes.