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  2. Trypsin inhibitor - Wikipedia

    en.wikipedia.org/wiki/Trypsin_inhibitor

    Trypsin inhibitor is present in various foods such as soybeans, grains, cereals and various additional legumes. [10] The main function of trypsin inhibitors in these foods is to act as a defense mechanism. By having this harmful component wild animals learn that any food that contains trypsin inhibitor is a food to avoid.

  3. Thiaminase - Wikipedia

    en.wikipedia.org/wiki/Thiaminase

    This enzyme can be found in a variety of different sources. It can be found in marine organisms, plants, and bacteria. Since thiamine (vitamin B 1) is a very important substance required for metabolic pathways by almost all organisms, it can be very detrimental to introduce Thiaminase to a system. Frequently an organism gains this enzyme by ...

  4. Selenium in biology - Wikipedia

    en.wikipedia.org/wiki/Selenium_in_biology

    A few of these appeared more recently, in the last 50–200 million years, in fruits and flowers of angiosperm plants. In fact, the angiosperms (the dominant type of plant today) and most of their antioxidant pigments evolved during the late Jurassic period. About 200 Mya, new selenoproteins were developed as mammalian GSH-Px enzymes. [51] [52 ...

  5. Enzyme inhibitor - Wikipedia

    en.wikipedia.org/wiki/Enzyme_inhibitor

    Many poisons produced by animals or plants are enzyme inhibitors that block the activity of crucial enzymes in prey or predators. Many drug molecules are enzyme inhibitors that inhibit an aberrant human enzyme or an enzyme critical for the survival of a pathogen such as a virus , bacterium or parasite .

  6. Organophosphate poisoning - Wikipedia

    en.wikipedia.org/wiki/Organophosphate_poisoning

    Enzyme bioscavengers are being developed as a pretreatment to sequester highly toxic OPs before they can reach their physiological targets and prevent the toxic effects from occurring. Significant advances with cholinesterases (ChEs), specifically human serum BChE (HuBChE) have been made. HuBChe can offer a broad range of protection for nerve ...

  7. Protein toxicity - Wikipedia

    en.wikipedia.org/wiki/Protein_toxicity

    Protein toxicity is the effect of the buildup of protein metabolic waste compounds, like urea, uric acid, ammonia, and creatinine.Protein toxicity has many causes, including urea cycle disorders, genetic mutations, excessive protein intake, and insufficient kidney function, such as chronic kidney disease and acute kidney injury.

  8. Inborn errors of metabolism - Wikipedia

    en.wikipedia.org/wiki/Inborn_errors_of_metabolism

    Inborn errors of metabolism form a large class of genetic diseases involving congenital disorders of enzyme activities. [1] The majority are due to defects of single genes that code for enzymes that facilitate conversion of various substances into others . In most of the disorders, problems arise due to accumulation of substances which are ...

  9. Maltase-glucoamylase - Wikipedia

    en.wikipedia.org/wiki/Maltase-glucoamylase

    This enzyme is a part of a family of enzymes called glycoside hydrolase family 31 (GH31). This is due to the digestive mechanism of the enzyme. GH31 enzymes undergo what is known as the Koshland double displacement mechanism [11] in which a glycosylation and deglycosylation step occurs, resulting in the retention of the overall configuration of the anomeric center.