Alliin lyase (ALL)

Alliin lyase, commonly known as alliinase, is a pyridoxal 5'-phosphate-dependent enzyme found in the vacuoles of garlic (Allium sativum) cells. When garlic tissue is crushed or damaged, the enzyme is released and comes into contact with its substrate, alliin, which is stored in the cytoplasm. This interaction triggers a rapid chemical reaction that produces allicin, the primary organosulfur compound responsible for the characteristic pungent aroma and the majority of garlic's biological activities. From a therapeutic perspective, alliin lyase is the 'bioactive trigger' that generates compounds capable of modulating human health. The resulting allicin and its downstream metabolites (such as ajoene and diallyl sulfides) interact with various human targets, including HMG-CoA reductase for cholesterol management and cyclooxygenase for anti-inflammatory effects. While not a human drug target in the traditional sense, it is a critical target for pharmaceutical standardization in garlic-based supplements and has been explored in site-directed enzyme prodrug therapy (SDEPT) for cancer treatment, where the enzyme is conjugated to antibodies to generate cytotoxic allicin specifically at tumor sites.

Other names

AlliinaseAlliin alkyl-sulfenate-lyaseGarlic enzyme

Alliin lyase catalyzes the conversion of the non-protein amino acid alliin into sulfenic acids, which spontaneously condense to form allicin. Allicin and its derivatives then act as bioactive agents that inhibit various human enzymes such as HMG-CoA reductase and cyclooxygenase, providing antimicrobial, antihyperlipidemic, and anti-inflammatory effects.