Heme interacts with histidine- and tyrosine-based protein motifs and inhibits enzymatic activity of chloramphenicol acetyltransferase from Escherichia coli
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- 作者：Hans Henning Brewitza ; Nishit Goradiab ; Erik Schubertc ; Kerstin Gallerd ; e ; Toni Kü ; hlf ; Benjamin Syllwasschya ; Jü ; rgen Poppd ; e ; g ; Ute Neugebauerd ; e ; Gregor Hageluekenc ; Olav Schiemannc ; Oliver Ohlenschlä ; gerb ; oliver.ohlenschlaeger@leibniz-fli.de" class="auth_mail" title="E-mail the corresponding author ; Diana Imhofa ; dimhof@uni-bonn.de" class="auth_mail" title="E-mail the corresponding author
- 关键词：Cat ; chloramphenicol acetyltransferase ; CatIII ; chloramphenicol acetyltransferase III ; CcmE ; cytochrome c-type biogenesis protein ; ChaN ; campylobacter heme acquisition protein N ; RPB2 ; DNA-directed RNA polymerase II subunit ; DTNB ; 5 ; 5&prime ; -dithiobis-(2-nitrobenzoic acid) ; Far1 ; fatty acyl-CoA reductase 1 ; KCNH1 ; potassium voltage-gated channel subfamily H member 1 ; HlyC ; hemolysin-activating lysine-acyltransferase ; HRMs ; heme-regulatory motifs ; HrtR ; heme-regulated transporter regulator ; HTHP
- 刊名：Biochimica et Biophysica Acta (BBA) - General Subjects
- 出版年：2016
- 出版时间：June 2016
- 年：2016
- 卷：1860
- 期：6
- 页码：1343-1353
- 全文大小：1034 K
文摘
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Heme-binding affinity of His/Tyr-based motifs is lower compared to Cys-based motifs.
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Prediction and confirmation of a new heme-regulated/-binding protein
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Heme inhibits bioactivity of chloramphenicol acetyltransferase from E. coli.