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In biochemistry, denaturation is a process in which proteins or nucleic acids lose folded structure present in their native state due to various factors, including application of some external stress or compound, such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), agitation and radiation, or heat. [3]
Ascorbate is a known cofactor of myrosinase, serving as a base catalyst in glucosinolate hydrolysis. [1] [7] For example, myrosinase isolated from daikon (Raphanus sativus) demonstrated an increase in V max from 2.06 μmol/min per mg of protein to 280 μmol/min per mg of protein on the substrate, allyl glucosinolate (sinigrin) when in the presence of 500 μM ascorbate. [4]
Enzymes are usually much larger than their substrates. Sizes range from just 62 amino acid residues, for the monomer of 4-oxalocrotonate tautomerase, [28] to over 2,500 residues in the animal fatty acid synthase. [29] Only a small portion of their structure (around 2–4 amino acids) is directly involved in catalysis: the catalytic site. [30]
T. aquaticus is a bacterium that lives in hot springs and hydrothermal vents, and Taq polymerase was identified [1] as an enzyme able to withstand the protein-denaturing conditions (high temperature) required during PCR. [2] Therefore, it replaced the DNA polymerase from E. coli originally used in PCR. [3]
The majority of molecular chaperones do not convey any steric information for protein folding, and instead assist in protein folding by binding to and stabilizing folding intermediates until the polypeptide chain is fully translated. The specific mode of function of chaperones differs based on their target proteins and location.
Pyrolobus fumarii are capable of cellular growth and survival in a temperature range between 90 °C and 113 °C with their optimum temperature being around 106 °C. There are only a few species that are known to survive at this temperature. They require a pH range of around 4 - 6.5 which is relatively more acidic than neutral to grow. [5]
An extremozyme is an enzyme, often created by archaea, which are known prokaryotic extremophiles that can function under extreme environments. Examples of such are those in highly acidic/basic conditions, high/low temperatures, high salinity, or other factors, that would otherwise denature typical enzymes (e.g. catalase, rubisco, carbonic anhydrase). [1]
Thermus aquaticus is a species of bacteria that can tolerate high temperatures, one of several thermophilic bacteria that belong to the Deinococcota phylum. It is the source of the heat-resistant enzyme Taq DNA polymerase, one of the most important enzymes in molecular biology because of its use in the polymerase chain reaction (PCR) DNA amplification technique.