Any feedback?
Literature summary extracted from
- Catalytic mechanism of S-ribosylhomocysteinase: ionization state of active-site residues (2006), Biochemistry, 45, 12195-12203.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 4.4.1.21 | LuxS variants are overexpressed in Escherichia coli in their Fe2+, Zn2+- and Co2+-substituted forms | Bacillus subtilis |
| 4.4.1.21 | mutant LuxS variants are overexpressed in Escherichia coli in both Zn2+- and Co2+-substituted forms | Escherichia coli |
| 4.4.1.21 | mutant LuxS variants are overexpressed in Escherichia coli in both Zn2+- and Co2+-substituted forms | Bacillus subtilis |
| 4.4.1.21 | mutant LuxS variants are overexpressed in Escherichia coli in both Zn2+- and Co2+-substituted forms | Vibrio harveyi |
| 4.4.1.21 | mutant LuxS variants are overexpressed in Escherichia coli in their Fe2+, Zn2+- and Co2+-substituted forms | Vibrio harveyi |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 4.4.1.21 | Co2+-substituted BsLuxS is cocrystallized with inhibitors (2S)-2-amino-4-[(2R,3S)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid and (2S)-2-amino-4-[(2R,3R)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid by the hanging drop vapor diffusion method | Bacillus subtilis |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 4.4.1.21 | C41A | by site directed mutagenesis | Escherichia coli |
| 4.4.1.21 | C83D | by site directed mutagenesis | Escherichia coli |
| 4.4.1.21 | H11Q | by site directed mutagenesis | Bacillus subtilis |
| 4.4.1.21 | R39M | by site directed mutagenesis | Bacillus subtilis |
| 4.4.1.21 | S6A | by site directed mutagenesis | Bacillus subtilis |
| 4.4.1.21 | Y89F | by site directed mutagenesis | Bacillus subtilis |
General Stability
| EC Number | General Stability | Organism |
|---|---|---|
| 4.4.1.21 | absorption and electron paramagnetic resonance spectroscopic studies reveals that the active form of LuxS contains a metal-bound water and a thiolate ion at Cys-83, an invariant Arg-39 in the active site is partially responsible for stabilizing the thiolate anion of Cys-83 | Bacillus subtilis |
| 4.4.1.21 | absorption and electron paramagnetic resonance spectroscopic studies reveals that the active form of LuxS contains a metal-bound water and a thiolate ion at Cys-83, an invariant Arg-39 in the active site is partially responsible for stabilizing the thiolate anion of Cys-83 | Vibrio harveyi |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.4.1.21 | (2S)-2-amino-4-[(2R,3R)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid | - |
Bacillus subtilis |  |
| 4.4.1.21 | (2S)-2-amino-4-[(2R,3R)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid | - |
Vibrio harveyi | |
| 4.4.1.21 | (2S)-2-amino-4-[(2R,3S)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid | - |
Bacillus subtilis | |
| 4.4.1.21 | (2S)-2-amino-4-[(2R,3S)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid | - |
Vibrio harveyi | |
| 4.4.1.21 | (2S)-2-amino-6-(N-formyl-N-hydroxyamino)hexanoic acid | - |
Bacillus subtilis | |
| 4.4.1.21 | D-erythronohydroxamic acid | - |
Bacillus subtilis | |
| 4.4.1.21 | D-erythronohydroxamic acid | - |
Vibrio harveyi | |
| 4.4.1.21 | D-ribosylornithine | - |
Bacillus subtilis | |
| 4.4.1.21 | methionine | - |
Bacillus subtilis | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.4.1.21 | 0.0019 | - |
S-ribosylhomocysteine | Fe2+ containing BsLuxS | Bacillus subtilis | |
| 4.4.1.21 | 0.0023 | - |
S-ribosylhomocysteine | Co2+ substituted BsLuxS | Bacillus subtilis | |
| 4.4.1.21 | 0.016 | - |
S-ribosylhomocysteine | wild type enzyme | Escherichia coli | |
| 4.4.1.21 | 0.016 | - |
S-ribosylhomocysteine | C41A mutant | Escherichia coli | |
| 4.4.1.21 | 0.039 | - |
S-ribosylhomocysteine | Co2+ substituted VhLuxS | Vibrio harveyi | |
| 4.4.1.21 | 0.058 | - |
S-ribosylhomocysteine | Zn2+ substituted BsLuxS | Bacillus subtilis | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.4.1.21 | Co2+ | - |
Escherichia coli | |
| 4.4.1.21 | Co2+ | - |
Bacillus subtilis | |
| 4.4.1.21 | Co2+ | - |
Vibrio harveyi | |
| 4.4.1.21 | Co2+ | Co2+ substitution produces a highly stable enzyme | Bacillus subtilis | |
| 4.4.1.21 | Co2+ | Co2+ substitution produces a highly stable enzyme | Vibrio harveyi | |
| 4.4.1.21 | Fe2+ | - |
Escherichia coli | |
| 4.4.1.21 | Fe2+ | - |
Bacillus subtilis | |
| 4.4.1.21 | Fe2+ | - |
Vibrio harveyi | |
| 4.4.1.21 | Fe2+ | acts as a Lewis acid | Bacillus subtilis | |
| 4.4.1.21 | Fe2+ | acts as a Lewis acid | Vibrio harveyi | |
| 4.4.1.21 | Zn2+ | Zn2+ substitution produces an enzyme with 10fold lower activity | Bacillus subtilis | |
| 4.4.1.21 | Zn2+ | Zn2+ substitution produces an enzyme with 10fold lower activity | Vibrio harveyi | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 4.4.1.21 | 12500 | - |
3 * 12500 | Escherichia coli |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.4.1.21 | Bacillus subtilis | O34667 | - |
- |
| 4.4.1.21 | Escherichia coli | P45578 | - |
- |
| 4.4.1.21 | Vibrio harveyi | Q9Z5X1 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 4.4.1.21 | Q-Sepharose Fast-Flow column chromatography and ultrafiltration | Escherichia coli |
| 4.4.1.21 | Q-Sepharose Fast-Flow column chromatography and ultrafiltration | Bacillus subtilis |
| 4.4.1.21 | Q-Sepharose Fast-Flow column chromatography and ultrafiltration | Vibrio harveyi |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.4.1.21 | S-(5-deoxy-D-ribos-5-yl)-L-homocysteine | - |
Escherichia coli | L-homocysteine + (S)-4,5-dihydroxypentan-2,3-dione | - |
? | |
| 4.4.1.21 | S-(5-deoxy-D-ribos-5-yl)-L-homocysteine | - |
Bacillus subtilis | L-homocysteine + (S)-4,5-dihydroxypentan-2,3-dione | - |
? | |
| 4.4.1.21 | S-(5-deoxy-D-ribos-5-yl)-L-homocysteine | - |
Vibrio harveyi | L-homocysteine + (S)-4,5-dihydroxypentan-2,3-dione | - |
? | |
| 4.4.1.21 | S-ribosylhomocysteine | - |
Escherichia coli | L-homocysteine + (S)-4,5-dihydroxypentan-2,3-dione | - |
? | |
| 4.4.1.21 | S-ribosylhomocysteine | - |
Bacillus subtilis | L-homocysteine + (S)-4,5-dihydroxypentan-2,3-dione | - |
? | |
| 4.4.1.21 | S-ribosylhomocysteine | - |
Vibrio harveyi | L-homocysteine + (S)-4,5-dihydroxypentan-2,3-dione | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 4.4.1.21 | homodimer | 3 * 12500 | Escherichia coli |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.4.1.21 | BsLuxS | - |
Bacillus subtilis |
| 4.4.1.21 | EcLuxS | - |
Escherichia coli |
| 4.4.1.21 | LuxS | - |
Escherichia coli |
| 4.4.1.21 | LuxS | - |
Bacillus subtilis |
| 4.4.1.21 | LuxS | - |
Vibrio harveyi |
| 4.4.1.21 | S-ribosylhomocysteinase | - |
Escherichia coli |
| 4.4.1.21 | S-ribosylhomocysteinase | - |
Bacillus subtilis |
| 4.4.1.21 | S-ribosylhomocysteinase | - |
Vibrio harveyi |
| 4.4.1.21 | S-ribosylhomocysteine lyase | - |
Escherichia coli |
| 4.4.1.21 | S-ribosylhomocysteine lyase | - |
Bacillus subtilis |
| 4.4.1.21 | S-ribosylhomocysteine lyase | - |
Vibrio harveyi |
| 4.4.1.21 | VhLuxS | - |
Vibrio harveyi |
Ki Value [mM]
| EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.4.1.21 | 0.00037 | - |
(2S)-2-amino-4-[(2R,3R)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid | Co2+ substituted enzyme | Bacillus subtilis | |
| 4.4.1.21 | 0.00043 | - |
(2S)-2-amino-4-[(2R,3R)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid | Fe2+ substituted enzyme | Bacillus subtilis | |
| 4.4.1.21 | 0.00072 | - |
(2S)-2-amino-4-[(2R,3S)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid | Co2+ substituted enzyme | Bacillus subtilis | |
| 4.4.1.21 | 0.00072 | - |
(2S)-2-amino-4-[(2R,3S)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid | Fe2+ substituted enzyme | Bacillus subtilis | |
| 4.4.1.21 | 0.0097 | - |
(2S)-2-amino-4-[(2R,3S)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid | Co2+ substituted enzyme | Vibrio harveyi | |
| 4.4.1.21 | 0.0106 | - |
(2S)-2-amino-4-[(2R,3R)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid | Zn2+ substituted enzyme | Bacillus subtilis | |
| 4.4.1.21 | 0.0128 | - |
(2S)-2-amino-4-[(2R,3R)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid | Co2+ substituted enzyme | Vibrio harveyi | |
| 4.4.1.21 | 0.0196 | - |
(2S)-2-amino-4-[(2R,3S)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid | Zn2+ substituted enzyme | Bacillus subtilis | |
| 4.4.1.21 | 0.061 | - |
methionine | Co2+ substituted enzyme | Bacillus subtilis | |
| 4.4.1.21 | 0.068 | - |
D-ribosylornithine | Co2+ substituted enzyme | Bacillus subtilis | |
| 4.4.1.21 | 0.147 | - |
D-erythronohydroxamic acid | Fe2+ substituted enzyme | Bacillus subtilis | |
| 4.4.1.21 | 0.156 | - |
D-erythronohydroxamic acid | Co2+ substituted enzyme | Bacillus subtilis | |
| 4.4.1.21 | 0.55 | - |
D-erythronohydroxamic acid | Co2+ substituted enzyme | Vibrio harveyi | |
| 4.4.1.21 | 2.4 | - |
D-erythronohydroxamic acid | Zn2+ substituted enzyme | Bacillus subtilis | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
