Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 4.4.1.21 extracted from

  • Zhu, J.; Knottenbelt, S.; Kirk, M.L.; Pei, D.
    Catalytic mechanism of S-ribosylhomocysteinase: ionization state of active-site residues (2006), Biochemistry, 45, 12195-12203.
    View publication on PubMed
Search for more literature for 4.4.1.21

Cloned(Commentary)

Cloned (Comment) Organism
LuxS variants are overexpressed in Escherichia coli in their Fe2+, Zn2+- and Co2+-substituted forms Bacillus subtilis
mutant LuxS variants are overexpressed in Escherichia coli in both Zn2+- and Co2+-substituted forms Escherichia coli
mutant LuxS variants are overexpressed in Escherichia coli in both Zn2+- and Co2+-substituted forms Bacillus subtilis
mutant LuxS variants are overexpressed in Escherichia coli in both Zn2+- and Co2+-substituted forms Vibrio harveyi
mutant LuxS variants are overexpressed in Escherichia coli in their Fe2+, Zn2+- and Co2+-substituted forms Vibrio harveyi

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Protein Variants Comment Organism
C41A by site directed mutagenesis Escherichia coli
C83D by site directed mutagenesis Escherichia coli
H11Q by site directed mutagenesis Bacillus subtilis
R39M by site directed mutagenesis Bacillus subtilis
S6A by site directed mutagenesis Bacillus subtilis
Y89F by site directed mutagenesis Bacillus subtilis

General Stability

General Stability Organism
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
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

Inhibitors Comment Organism Structure
(2S)-2-amino-4-[(2R,3R)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid
-
 Bacillus subtilis
(2S)-2-amino-4-[(2R,3R)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid
-
 Vibrio harveyi
(2S)-2-amino-4-[(2R,3S)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid
-
 Bacillus subtilis
(2S)-2-amino-4-[(2R,3S)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid
-
 Vibrio harveyi
(2S)-2-amino-6-(N-formyl-N-hydroxyamino)hexanoic acid
-
 Bacillus subtilis
D-erythronohydroxamic acid
-
 Bacillus subtilis
D-erythronohydroxamic acid
-
 Vibrio harveyi
D-ribosylornithine
-
 Bacillus subtilis
methionine
-
 Bacillus subtilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0019
-
 S-ribosylhomocysteine Fe2+ containing BsLuxS Bacillus subtilis
0.0023
-
 S-ribosylhomocysteine Co2+ substituted BsLuxS Bacillus subtilis
0.016
-
 S-ribosylhomocysteine wild type enzyme Escherichia coli
0.016
-
 S-ribosylhomocysteine C41A mutant Escherichia coli
0.039
-
 S-ribosylhomocysteine Co2+ substituted VhLuxS Vibrio harveyi
0.058
-
 S-ribosylhomocysteine Zn2+ substituted BsLuxS Bacillus subtilis

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+
-
 Escherichia coli
Co2+
-
 Bacillus subtilis
Co2+
-
 Vibrio harveyi
Co2+ Co2+ substitution produces a highly stable enzyme Bacillus subtilis
Co2+ Co2+ substitution produces a highly stable enzyme Vibrio harveyi
Fe2+
-
 Escherichia coli
Fe2+
-
 Bacillus subtilis
Fe2+
-
 Vibrio harveyi
Fe2+ acts as a Lewis acid Bacillus subtilis
Fe2+ acts as a Lewis acid Vibrio harveyi
Zn2+ Zn2+ substitution produces an enzyme with 10fold lower activity Bacillus subtilis
Zn2+ Zn2+ substitution produces an enzyme with 10fold lower activity Vibrio harveyi

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
12500
-
 3 * 12500 Escherichia coli

Organism

Organism UniProt Comment Textmining
Bacillus subtilis O34667
-
-
Escherichia coli P45578
-
-
Vibrio harveyi Q9Z5X1
-
-

Purification (Commentary)

Purification (Comment) Organism
Q-Sepharose Fast-Flow column chromatography and ultrafiltration Escherichia coli
Q-Sepharose Fast-Flow column chromatography and ultrafiltration Bacillus subtilis
Q-Sepharose Fast-Flow column chromatography and ultrafiltration Vibrio harveyi

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine
-
 Escherichia coli L-homocysteine + (S)-4,5-dihydroxypentan-2,3-dione
-
 ?
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine
-
 Bacillus subtilis L-homocysteine + (S)-4,5-dihydroxypentan-2,3-dione
-
 ?
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine
-
 Vibrio harveyi L-homocysteine + (S)-4,5-dihydroxypentan-2,3-dione
-
 ?
S-ribosylhomocysteine
-
 Escherichia coli L-homocysteine + (S)-4,5-dihydroxypentan-2,3-dione
-
 ?
S-ribosylhomocysteine
-
 Bacillus subtilis L-homocysteine + (S)-4,5-dihydroxypentan-2,3-dione
-
 ?
S-ribosylhomocysteine
-
 Vibrio harveyi L-homocysteine + (S)-4,5-dihydroxypentan-2,3-dione
-
 ?

Subunits

Subunits Comment Organism
homodimer 3 * 12500 Escherichia coli

Synonyms

Synonyms Comment Organism
BsLuxS
-
 Bacillus subtilis
EcLuxS
-
 Escherichia coli
LuxS
-
 Escherichia coli
LuxS
-
 Bacillus subtilis
LuxS
-
 Vibrio harveyi
S-ribosylhomocysteinase
-
 Escherichia coli
S-ribosylhomocysteinase
-
 Bacillus subtilis
S-ribosylhomocysteinase
-
 Vibrio harveyi
S-ribosylhomocysteine lyase
-
 Escherichia coli
S-ribosylhomocysteine lyase
-
 Bacillus subtilis
S-ribosylhomocysteine lyase
-
 Vibrio harveyi
VhLuxS
-
 Vibrio harveyi

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.00037
-
 (2S)-2-amino-4-[(2R,3R)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid Co2+ substituted enzyme Bacillus subtilis
0.00043
-
 (2S)-2-amino-4-[(2R,3R)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid Fe2+ substituted enzyme Bacillus subtilis
0.00072
-
 (2S)-2-amino-4-[(2R,3S)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid Co2+ substituted enzyme Bacillus subtilis
0.00072
-
 (2S)-2-amino-4-[(2R,3S)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid Fe2+ substituted enzyme Bacillus subtilis
0.0097
-
 (2S)-2-amino-4-[(2R,3S)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid Co2+ substituted enzyme Vibrio harveyi
0.0106
-
 (2S)-2-amino-4-[(2R,3R)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid Zn2+ substituted enzyme Bacillus subtilis
0.0128
-
 (2S)-2-amino-4-[(2R,3R)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid Co2+ substituted enzyme Vibrio harveyi
0.0196
-
 (2S)-2-amino-4-[(2R,3S)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid Zn2+ substituted enzyme Bacillus subtilis
0.061
-
 methionine Co2+ substituted enzyme Bacillus subtilis
0.068
-
 D-ribosylornithine Co2+ substituted enzyme Bacillus subtilis
0.147
-
 D-erythronohydroxamic acid Fe2+ substituted enzyme Bacillus subtilis
0.156
-
 D-erythronohydroxamic acid Co2+ substituted enzyme Bacillus subtilis
0.55
-
 D-erythronohydroxamic acid Co2+ substituted enzyme Vibrio harveyi
2.4
-
 D-erythronohydroxamic acid Zn2+ substituted enzyme Bacillus subtilis