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Literature summary for 4.4.1.4 extracted from

  • Mendez Lagunas, L.L.; Castaigne, F.
    Effect of temperature cycling on allinase activity in garlic (2008), Food Chem., 111, 56-60.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Allium sativum allinase catalyzes the conversion of alliin to allicin, the principal component of potential medicinal value in garlic ?
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?

Organism

Organism UniProt Comment Textmining
Allium sativum
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alliin + H2O
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Allium sativum allicin + pyruvate + NH3
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?
additional information allinase catalyzes the conversion of alliin to allicin, the principal component of potential medicinal value in garlic Allium sativum ?
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?

Synonyms

Synonyms Comment Organism
allinase
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Allium sativum

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
40 60 the enzyme is thermolabile und shows loss of activity during the preserving drying process, sugars present in the garlic and the high molecular mass of the enzyme were responsible for protection against degradation at high drying temperatures of 40-60°C. The 40-60°C drying cyclic with the 4times 20-min sequences preserves 91% of the enzyme activity, compared to 90% and 74% for constant temperatures of 40°C and 60°C, respectively, degradation mechanism, inactivation at 60°C, overview Allium sativum

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate dependent on Allium sativum