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 .

Search for more literature for 2.3.1.28

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

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)