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Literature summary for 4.4.1.21 extracted from

  • Malladi, V.L.; Sobczak, A.J.; Meyer, T.M.; Pei, D.; Wnuk, S.F.
    Inhibition of LuxS by S-ribosylhomocysteine analogues containing a [4-aza]ribose ring (2011), Bioorg. Med. Chem., 19, 5507-5519.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.4.1.21

Inhibitors

Inhibitors Comment Organism Structure
S-(1-amino-1,4-anhydro-1,5-dideoxy-D-ribitol-5-yl)-L-homocysteine inhibition of Co(II)-substituted enzyme Bacillus subtilis
S-(4-amino-4,5-dideoxy-alpha/beta-D-ribofuranos-5-yl)-L-homocysteine inhibition of Co(II)-substituted enzyme. The hemiaminal may undergo ring opening to form an aldehyde which may undergo the aldose-ketose isomerization reaction to form a 2-ketone, which presumably binds to the LuxS active site with higher affinity than the original ribose analogue Bacillus subtilis
S-(4-amino-4,5-dideoxy-D-ribono-1,4-lactam-5-yl)-L-homocysteine inhibition of Co(II)-substituted enzyme Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
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Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0035
-
 S-(4-amino-4,5-dideoxy-alpha/beta-D-ribofuranos-5-yl)-L-homocysteine pH 7.0, 22°C Bacillus subtilis
0.037
-
 S-(4-amino-4,5-dideoxy-D-ribono-1,4-lactam-5-yl)-L-homocysteine pH 7.0, 22°C Bacillus subtilis
0.048
-
 S-(1-amino-1,4-anhydro-1,5-dideoxy-D-ribitol-5-yl)-L-homocysteine pH 7.0, 22°C Bacillus subtilis