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Literature summary for 4.4.1.21 extracted from

  • He, Y.; Frye, J.G.; Strobaugh, T.P.; Chen, C.Y.
    Analysis of AI-2/LuxS-dependent transcription in Campylobacter jejuni strain 81-176 (2008), Foodborne Pathog. Dis., 5, 399-415.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information the DELTA luxS mutant abolishes AI-2 production and is more sensitive to hydrogen peroxide and cumene hydroperoxide than the wild type enzyme Campylobacter jejuni

Organism

Organism UniProt Comment Textmining
Campylobacter jejuni Q3I354
-
-
Campylobacter jejuni 81-176 Q3I354
-
-

Oxidation Stability

Oxidation Stability Organism
the DELTAluxS mutant shows higher sensitivity to both hydrogen peroxide and cumene hydroperoxide than the wild type enzyme with consistently greater zones of inhibition Campylobacter jejuni

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-ribosylhomocysteine
-
Campylobacter jejuni L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
?
S-ribosylhomocysteine
-
Campylobacter jejuni 81-176 L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
?

Synonyms

Synonyms Comment Organism
LuxS
-
Campylobacter jejuni
S-ribosylhomocysteinase
-
Campylobacter jejuni