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Literature summary for 1.1.1.267 extracted from

  • Hui, X.; Yue, Q.; Zhang, D.D.; Li, H.; Yang, S.Q.; Gao, W.Y.
    Antimicrobial mechanism of theaflavins: They target 1-deoxy-D-xylulose 5-phosphate reductoisomerase, the key enzyme of the MEP terpenoid biosynthetic pathway (2016), Sci. Rep., 6, 38945.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.1.1.267

Inhibitors

Inhibitors Comment Organism Structure
theaflavin-3'-gallate non-competitive against 1-deoxy-D-xylulose 5-phosphate and un-competitive inhibitors with respect to NADPH Escherichia coli
theaflavin-3,3'-digallate non-competitive against 1-deoxy-D-xylulose 5-phosphate and un-competitive inhibitors with respect to NADPH Escherichia coli
theaflavin-3-gallate non-competitive against 1-deoxy-D-xylulose 5-phosphate and un-competitive inhibitors with respect to NADPH Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0133
-
 theaflavin-3,3'-digallate substrate 1-deoxy-D-xylulose 5-phosphate, pH 7.4, 37°C Escherichia coli
0.0182
-
 theaflavin-3,3'-digallate substrate NADPH, pH 7.4, 37°C Escherichia coli
0.0222
-
 theaflavin-3'-gallate substrate 1-deoxy-D-xylulose 5-phosphate, pH 7.4, 37°C Escherichia coli
0.0224
-
 theaflavin-3'-gallate substrate NADPH, pH 7.4, 37°C Escherichia coli
0.0247
-
 theaflavin-3-gallate substrate NADPH, pH 7.4, 37°C Escherichia coli
0.03
-
 theaflavin-3-gallate substrate 1-deoxy-D-xylulose 5-phosphate , pH 7.4, 37°C Escherichia coli