EC Number |
Protein Variants |
Reference |
---|
4.4.1.4 | C115A |
mutation leads to a decrease of the catalytic efficiency in the gamma-elimination reaction of the physiological substrate by more than an order of magnitude, reation of EC 4.4.1.11 |
747207 |
4.4.1.4 | C115H |
mutant cleaves S-alk(en)yl-L-cysteine sulfoxides more effectively than the wild type |
747211 |
4.4.1.4 | C115H |
mutation leads to loss of activity in the gamma-elimination reaction of the physiological substrate, reaction of EC 4.4.1.11. The catalytic efficiency in the beta-elimination reaction of S-substituted L-cysteine sulfoxides is increased by about an order of magnitude compared to the wild type |
747207 |
4.4.1.4 | K280A |
almost no detectable alliinase activity |
34622 |
4.4.1.4 | K280R |
almost no detectable alliinase activity |
34622 |
4.4.1.4 | more |
preparation of encapsulated alliinase from Allium sativum in alginate microparticles to improve the use of the enzyme from garlic for medical oral treatments, method, overview. The enzyme activity of the encapsulated enzyme is increased compared to non-encapsulated, especially at low pH |
729464 |
4.4.1.4 | more |
production of antibodies with alliinase activities by exploiting the molecular mimicry of Camelus bactrianus nanobodies: enrichment of variable domain of the heavy chain of a heavy-chain antibodies specific against the alliinase via phage display, recombinant expression of the selected His-tagged antibodies in Escherichia coli strain BL21(DE3), and purification by nickel affinity chromatography |
729980 |