4.4.1.21: S-ribosylhomocysteine lyase
This is an abbreviated version!
For detailed information about S-ribosylhomocysteine lyase, go to the full flat file.
Word Map on EC 4.4.1.21
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4.4.1.21
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quorum
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quorum-sensing
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interspecies
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harveyi
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thioether
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4,5-dihydroxy-2,3-pentanedione
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nucleosidase
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luxs-dependent
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furanone
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medicine
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analysis
- 4.4.1.21
-
quorum
-
quorum-sensing
-
interspecies
- harveyi
- thioether
- 4,5-dihydroxy-2,3-pentanedione
- nucleosidase
-
luxs-dependent
-
furanone
- medicine
- analysis
Reaction
Synonyms
AI-2 synthase, autoinducer-2 synthase, BsLuxS, EC 3.13.1.2, EC 3.2.1.148, EC 3.3.1.3, EcLuxS, lsrR, Lux S, LuxS, LuxS protein, S-ribosyl homocysteinase, S-ribosylhomocysteinase, S-ribosylhomocysteine lyase, S-ribosylhomocysteinelyase, VhLuxS
ECTree
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Metals Ions
Metals Ions on EC 4.4.1.21 - S-ribosylhomocysteine lyase
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Al3+
Ca2+
Co2+
EDTA
Fe(III)
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Fe(III) upregulates expression of luxS and Fe(III) strongly enhances biofilm formation at concentrations above 50 microM
Fe2+
Mn2+
Zinc
zinc-dependent metalloenzyme, each active site contains a zinc ion coordinated by the conserved residues His54, His58 and Cys126, and includes residues from both subunits
Zn2+
additional information
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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+
ETF12584, ETF12641
1 mM, 110% of initial activity, respectively
Al3+
ETF12584, ETF12641
1 mM, 115% of initial activity, respectively
ETF12584, ETF12641
1 mM, 108% of initial activity, respectively
Ca2+
ETF12584, ETF12641
1 mM, 19% of initial activity, respectively
ETF12584, ETF12641
1 mM, 113% of initial activity, respectively
EDTA
ETF12584, ETF12641
1 mM, 123% of initial activity, respectively
Fe2+
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LuxS is a metalloenzyme containing a tetrahedrally coordinated Fe2+ ion in its active site
Fe2+
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LuxS is a metalloenzyme containing a tetrahedrally coordinated Fe2+ ion in its active site
Fe2+
ETF12584, ETF12641
1 mM, 110% of initial activity, respectively
Fe2+
ETF12584, ETF12641
1 mM, 99% of initial activity, respectively
Fe2+
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LuxS is a metalloenzyme containing a tetrahedrally coordinated Fe2+ ion in its active site
ETF12584, ETF12641
1 mM, 103% of initial activity, respectively
Mn2+
ETF12584, ETF12641
1 mM, 114% of initial activity, respectively
the metal center is composed of a Zn2+ atom coordinated by two histidines, a cysteine, and a solvent molecule
Zn2+
Zn2+ substitution produces an enzyme with 10fold lower activity
Zn2+
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required for activity, in the wild-type the substrate's cyclic ribosyl moiety is positioned adjacent to the Zn2+ ion, while in the mutant C84A the noncyclic ribosyl is ligated to the Co2+ via its C2-O carbonyl oxygen
Zn2+
Zn2+ substitution produces an enzyme with 10-fold lower activity
Zn2+
calculated molar ratio of Zn2+ ion to each LuxS monomer is about 1:1