Cloned (Comment) | Organism |
---|---|
sequence comparison | Allium sativum |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
additional information | the enzyme alliinase resides in microcompartments separated by thin membranes, and is thus physically kept apart from its substrate alliin | Allium sativum | - |
- |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Allium sativum | alliinase catalyzes the synthesis of the chemically and therapeutically active compound allicin, i.e. diallyl thiosulfinate | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Allium sativum | Q41233 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
glycoprotein | - |
Allium sativum |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
activities of native enzyme and S-biotinylated alliinase | Allium sativum |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | alliinase catalyzes the synthesis of the chemically and therapeutically active compound allicin, i.e. diallyl thiosulfinate | Allium sativum | ? | - |
? | |
additional information | the disulfide bridge between Cys368 and Cys376, located near the C-terminal, plays an important role in maintaining both the rigidity of the catalytic domain and the substrate-cofactor relative orientation, but alliinase activity does not require free SH groups | Allium sativum | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | homodimer | Allium sativum |
More | there are 10 cysteine residues per alliinase monomer, eight of which form four disulfide bridges and two are free thiols. Cys368 and Cys376 form a SAS bridge located near the C-terminal and plays an important role in maintaining both the rigidity of the catalytic domain and the substrate-cofactor relative orientation | Allium sativum |
Synonyms | Comment | Organism |
---|---|---|
alliinase | - |
Allium sativum |
C-S lyase | - |
Allium sativum |
cys sulfoxide lyase | - |
Allium sativum |
More | the enzyme belongs to the fold-type I family of pyridoxal-5'-phosphate-dependent enzymes | Allium sativum |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
23 | - |
assay at | Allium sativum |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.5 | - |
assay at | Allium sativum |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | dependent on | Allium sativum |