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Thiaminase is an enzyme that ... prehistoric periplasmic binding protein that had been ... by the amidohydrolase ylmB and hydrolyzed to 5 ...
Aminopyrimidine aminohydrolase (EC 3.5.99.2, thiaminase, thiaminase II, tenA (gene)) is an enzyme with systematic name 4-amino-5-aminomethyl-2-methylpyrimidine aminohydrolase.
Hydrolyzed protein is a solution derived from the hydrolysis of a protein into its component amino acids and peptides. While many means of achieving this process exist, the most common method is prolonged heating with hydrochloric acid, [1] sometimes with an enzyme such as pancreatic protease to simulate the naturally occurring hydrolytic process.
Thiamine is one of the B vitamins and is also known as vitamin B 1. [1] [11] [12] It is a cation that is usually supplied as a chloride salt. [3]It is soluble in water, methanol and glycerol, but practically insoluble in less polar organic solvents.
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In several reactions, including that of pyruvate dehydrogenase, alpha-ketoglutarate dehydrogenase, and transketolase, TPP catalyses the reversible decarboxylation reaction (aka cleavage of a substrate compound at a carbon-carbon bond connecting a carbonyl group to an adjacent reactive group—usually a carboxylic acid or an alcohol).
In biochemistry, hydrolases constitute a class of enzymes that commonly function as biochemical catalysts that use water to break a chemical bond: + + This typically results in dividing a larger molecule into smaller molecules.
Most of the amino acids in the protein are then hydrolyzed, usually by the use of a strong acid such as hydrochloric acid. These amino acids are then separated using 2-dimensional thin layer chromatography , along with amino acid standards for the three amino acids that are phosphorylated in eukaryotes : serine , threonine , and tyrosine .