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 |
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 |
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 | - |
L-homocysteine + (4S)-4,5-dihydroxypentan-2,3-dione | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.4.1.21 | Bacillus subtilis | - |
- |
- |
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 |
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 | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
4.4.1.21 | LuxS | - |
Bacillus subtilis |
4.4.1.21 | S-ribosyl homocysteinase | - |
Bacillus subtilis |
4.4.1.21 | S-ribosylhomocysteinase | - |
Bacillus subtilis |
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 |