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Literature summary extracted from

  • Huang, W.; Gherib, R.; Gauld, J.W.
    An active site water broadens substrate specificity in S-ribosylhomocysteinase (LuxS): a docking, MD, and QM/MM study (2012), J. Phys. Chem. B, 116, 8916-8929.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
4.4.1.21 C84A site-directed mutagenesis, catalytically inactive mutant, the mutant contains a Co2+ ion, in the wild-type the substrate's cyclic ribosyl moiety is positioned adjacent to the Zn2+ ion, while in the mutant the noncyclic ribosyl is ligated to the Co2+ via its C2-O carbonyl oxygen Bacillus subtilis
4.4.1.21 C84D site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Bacillus subtilis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.4.1.21 Zn2+ 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 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-(5-deoxy-D-ribos-5-yl)-L-homocysteine Bacillus subtilis
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L-homocysteine + (4S)-4,5-dihydroxypentan-2,3-dione
-
?

Organism

EC Number Organism UniProt Comment Textmining
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, the substrate may bind within the active site when its ribosyl moiety is in the alpha- or beta-furanose configuration or as a linear aldose, docking and molecular dynamics simulations Bacillus subtilis

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
-
Bacillus subtilis L-homocysteine + (4S)-4,5-dihydroxypentan-2,3-dione
-
?
4.4.1.21 S-(5-deoxy-D-ribos-5-yl)-L-homocysteine furanose-containing S-ribosylhomocysteine Bacillus subtilis L-homocysteine + (4S)-4,5-dihydroxypentan-2,3-dione
-
?

Synonyms

EC Number Synonyms Comment Organism
4.4.1.21 LuxS
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Bacillus subtilis
4.4.1.21 S-ribosyl homocysteinase
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Bacillus subtilis
4.4.1.21 S-ribosylhomocysteinase
-
Bacillus subtilis

General Information

EC Number General Information Comment Organism
4.4.1.21 additional information elucidation of the mechanism of the first stage of the enzyme catalytic process by docking and molecular dynamics simulations, overview. An active site water stably locates within the active site, it can facilitate ring-opening of either alpha-S-ribosylhomocysteine or beta-furanose, leading to formation of a common active-site-bound 2-keto-S-ribosylhomocysteine intermediate, without the need to pass through a linear aldose S-ribosylhomocysteine configuration. Catalytic importance of several active site residues including Ser6, His11, Arg39, Cys84, and Glu57 Bacillus subtilis
4.4.1.21 physiological function S-ribosyl homocysteinase is a key enzyme in the formation of the signaling molecule of QS-2, autoinducer II Bacillus subtilis