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Literature summary for 2.3.1.28 extracted from

  • Brewitz, H.H.; Goradia, N.; Schubert, E.; Galler, K.; Kuehl, T.; Syllwasschy, B.; Popp, J.; Neugebauer, U.; Hagelueken, G.; Schiemann, O.; Ohlenschlaeger, O.; Imhof, D.
    Heme interacts with histidine- and tyrosine-based protein motifs and inhibits enzymatic activity of chloramphenicol acetyltransferase from Escherichia coli (2016), Biochim. Biophys. Acta, 1860, 1343-1353 .
    View publication on PubMed
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Inhibitors

Inhibitors Comment Organism Structure
heme identification and prediction of a His-based heme-regulatory motif. Heme interacts with chloroamphenicol acetyltransferase and displays an inhibitory effect on the protein activity Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P62577
-
-

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
 Escherichia coli
-

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.0577
-
 pH 7.8, 23°C Escherichia coli heme