Willow active extract of the bark, called salicin, was isolated to its crystalline form in 1828 by Henri Leroux, a French pharmacist, and Raffaele Piria, an Italian chemist, who then succeeded in separating out the compound in its pure state. In 1897, Felix Hoffmann created a synthetically altered version of salicin (in his case derived from the "Spiraea" plant), which caused less digestive upset than pure salicylic acid. The new drug, formally acetylsalicylic acid, was named Aspirin by Hoffmann's employer Bayer AG. This gave rise to the hugely important class of drugs known as nonsteroidal anti-inflammatory drugs (NSAIDs). Some of humans'
Cob(I)yrinic acid a,c-diamide adenosyltransferase as: Cob(I)yrinic acid a,c-diamide adenosyltransferase In molecular biology, cob(I)yrinic acid a,c-diamide adenosyltransferase (also known as ATP:cob(I)alamin adenosyltransferase or ATP:corrinoid adenosyltransferase) is an enzyme which catalyses the conversion of cobalamin (vitamin B12) into one of its coenzyme forms, adenosylcobalamin (coenzyme B12, AdoCbl). Adenosylcobalamin is required as a cofactor for the activity of certain enzymes. AdoCbl contains an adenosyl moiety liganded to the cobalt ion of cobalamin via a covalent Co-C bond. ATP:cob(I)alamin adenosyltransferases are classed into three groups: CobA-type, EutT-type and PduO-type. Each of the three enzyme types appears to be specialised for particular AdoCbl-dependent enzymes or for the de novo