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Literature summary extracted from

  • Zhu, J.; Dizin, E.; Hu, X.; Wavreille, A.S.; Park, J.; Pei, D.
    S-Ribosylhomocysteinase (LuxS) is a mononuclear iron protein (2003), Biochemistry, 42, 4717-4726.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.4.1.21
-
 Bacillus subtilis

Protein Variants

EC Number Protein Variants Comment Organism
4.4.1.21 C84A no catalytic activity Bacillus subtilis
4.4.1.21 C84D more than 220fold reduced activity Bacillus subtilis
4.4.1.21 C84S more than 220fold reduced activity Bacillus subtilis
4.4.1.21 E57A no detectable activity Bacillus subtilis
4.4.1.21 E57D 220fold reduced activity Bacillus subtilis
4.4.1.21 E57Q no detectable activity Bacillus subtilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.4.1.21 additional information
-
 additional information KM-values of enzyme forms enriched in either Fe2+, Co2+ or Zn2+ Bacillus subtilis
4.4.1.21 0.0025
-
 S-ribosylhomocysteine native enzyme Bacillus subtilis
4.4.1.21 0.18
-
 S-ribosylhomocysteine mutant enzyme E57D Bacillus subtilis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.4.1.21 Fe2+ contains Bacillus subtilis
4.4.1.21 additional information to gain insight into the catalytic mechanism of the unusual reaction and the function of the metal cofactor, an efficient expression and purification system is developed to produce LuxS enriched in either Fe2+, Co2+ or Zn2+ Bacillus subtilis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.4.1.21 S-ribosylhomocysteine Bacillus subtilis key step in biosynthesis pathway of type II autoinducer AI-2 L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.4.1.21 Bacillus subtilis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.4.1.21
-
 Bacillus subtilis

Reaction

EC Number Reaction Comment Organism Reaction ID
4.4.1.21 S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = L-homocysteine + (4S)-4,5-dihydroxypentan-2,3-dione catalytic mechanism in which the metal ion catalyzes an intramolecular redox reaction, shifting the carbonyl group from the C-1 position to the C-3 position of the ribose. Subsequent beta-elimination at the C-4 and C-5 position releases homocysteine as a free thiol Bacillus subtilis
a

Storage Stability

EC Number Storage Stability Organism
4.4.1.21 -80°C, when stored in the frozen form, the LuxS proteins are stable for at least 6 months Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.4.1.21 S-ribosylhomocysteine
-
 Bacillus subtilis L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
 ?
4.4.1.21 S-ribosylhomocysteine key step in biosynthesis pathway of type II autoinducer AI-2 Bacillus subtilis L-homocysteine + 4,5-dihydroxy-2,3-pentanedione
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.4.1.21 LuxS protein
-
 Bacillus subtilis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.4.1.21 additional information
-
 additional information turnover numbers of enzyme forms enriched in either Fe2+, Co2+ or Zn2+ Bacillus subtilis