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Literature summary for 4.4.1.4 extracted from

  • Weiner, L.; Shin, I.; Shimon, L.J.; Miron, T.; Wilchek, M.; Mirelman, D.; Frolow, F.; Rabinkov, A.
    Thiol-disulfide organization in alliin lyase (alliinase) from garlic (Allium sativum) (2009), Protein Sci., 18, 196-205.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
sequence comparison Allium sativum

Localization

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
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Natural Substrates/ Products (Substrates)

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 ?
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?

Organism

Organism UniProt Comment Textmining
Allium sativum Q41233
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Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein
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Allium sativum

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
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activities of native enzyme and S-biotinylated alliinase Allium sativum

Substrates and Products (Substrate)

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 ?
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?
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 ?
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?

Subunits

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

Synonyms Comment Organism
alliinase
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Allium sativum
C-S lyase
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Allium sativum
cys sulfoxide lyase
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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 [°C] Temperature Optimum Maximum [°C] Comment Organism
23
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assay at Allium sativum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
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assay at Allium sativum

Cofactor

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