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Literature summary for 4.4.1.4 extracted from

  • Shimon, L.J.; Rabinkov, A.; Shin, I.; Miron, T.; Mirelman, D.; Wilchek, M.; Frolow, F.
    Two structures of alliinase from Alliium sativum L.: apo form and ternary complex with aminoacrylate reaction intermediate covalently bound to the PLP cofactor (2007), J. Mol. Biol., 366, 611-625.
    View publication on PubMed
Search for more literature for 4.4.1.4

Crystallization (Commentary)

Crystallization (Comment) Organism
apo-enzyme crystallized in tetragonal form Allium sativum
enzyme crystallized in the presence of S-allyl-L-cysteine, forming dendrite-like monoclinic crystals Allium sativum

Localization

Localization Comment Organism GeneOntology No. Textmining
vacuole
-
 Allium sativum 5773
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
103000
-
-
 Allium sativum

Organism

Organism UniProt Comment Textmining
Allium sativum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Allium sativum

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-allyl-L-cysteine sulfoxide + H2O
-
 Allium sativum 2-propene-thioic acid + pyruvate + NH4+ + H+
-
 ?

Subunits

Subunits Comment Organism
homodimer two equal subunits of 448 amino acid residues Allium sativum

Synonyms

Synonyms Comment Organism
alliin lyase
-
 Allium sativum
alliinase
-
 Allium sativum
C-S-lyase
-
 Allium sativum
cys sulfoxide lyase
-
 Allium sativum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
-
 Allium sativum

Cofactor

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

pI Value

Organism Comment pI Value Maximum pI Value
Allium sativum between 6.0 and 7.0
-
 additional information