Cloned (Comment) | Organism |
---|---|
- |
Bacillus subtilis |
Protein Variants | Comment | Organism |
---|---|---|
C84A | no catalytic activity | Bacillus subtilis |
C84D | more than 220fold reduced activity | Bacillus subtilis |
C84S | more than 220fold reduced activity | Bacillus subtilis |
E57A | no detectable activity | Bacillus subtilis |
E57D | 220fold reduced activity | Bacillus subtilis |
E57Q | no detectable activity | Bacillus subtilis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | KM-values of enzyme forms enriched in either Fe2+, Co2+ or Zn2+ | Bacillus subtilis | |
0.0025 | - |
S-ribosylhomocysteine | native enzyme | Bacillus subtilis | |
0.18 | - |
S-ribosylhomocysteine | mutant enzyme E57D | Bacillus subtilis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | contains | Bacillus subtilis | |
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 | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
S-ribosylhomocysteine | Bacillus subtilis | key step in biosynthesis pathway of type II autoinducer AI-2 | L-homocysteine + 4,5-dihydroxy-2,3-pentanedione | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus subtilis | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Bacillus subtilis |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
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 |
Storage Stability | Organism |
---|---|
-80°C, when stored in the frozen form, the LuxS proteins are stable for at least 6 months | Bacillus subtilis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
S-ribosylhomocysteine | - |
Bacillus subtilis | L-homocysteine + 4,5-dihydroxy-2,3-pentanedione | - |
? | |
S-ribosylhomocysteine | key step in biosynthesis pathway of type II autoinducer AI-2 | Bacillus subtilis | L-homocysteine + 4,5-dihydroxy-2,3-pentanedione | - |
? |
Synonyms | Comment | Organism |
---|---|---|
LuxS protein | - |
Bacillus subtilis |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | turnover numbers of enzyme forms enriched in either Fe2+, Co2+ or Zn2+ | Bacillus subtilis |