نتایج جستجو برای: acetyltransferase

تعداد نتایج: 12835  

Journal: :The Biochemical journal 1983
A D Bennett W V Shaw

Plasmid-encoded fusidic acid resistance in Escherichia coli is mediated by a common variant of chloramphenicol acetyltransferase (EC 2.3.1.28), an enzyme which is an effector of chloramphenicol resistance. Resistance to chloramphenicol is a consequence of acetylation of the antibiotic catalysed by the enzyme and the failure of the 3-acetoxy product to bind to bacterial ribosomes. Cell-free coup...

Journal: :Journal of bacteriology 2015
Xin-Xin Liu Wei-Bing Liu Bang-Ce Ye

UNLABELLED NADP(+) is a vital cofactor involved in a wide variety of activities, such as redox potential and cell death. Here, we show that NADP(+) negatively regulates an acetyltransferase from Myxococcus xanthus, Mxan_3215 (MxKat), at physiologic concentrations. MxKat possesses an NAD(P)-binding domain fused to the Gcn5-type N-acetyltransferase (GNAT) domain. We used isothermal titration calo...

Journal: :Bioscience, biotechnology, and biochemistry 2009
Choong-Soo Yun Hisakazu Hasegawa Hideaki Nanamiya Teruhiko Terakawa Yuzuru Tozawa

Phosphinothricin (PPT) is the active ingredient in bialaphos, which specifically inhibits glutamine synthetase in land plants. We isolated a novel PPT-resistant gene from a soil bacterium, Nocardia sp., and characterized it. The encoded protein, consisting of 177 amino acids, showed significant similarity to bacterial N-acetyltransferases, and we originally designated the gene MAT (methionine s...

Journal: :The Journal of biological chemistry 1999
M Iizuka B Stillman

The origin recognition complex (ORC) is an initiator protein for DNA replication, but also effects transcriptional silencing in Saccharomyces cerevisiae and heterochromatin function in Drosophila. It is not known, however, whether any of these functions of ORC is conserved in mammals. We report the identification of a novel protein, HBO1 (histone acetyltransferase binding to ORC), that interact...

Journal: :Cell 1996
Mark R Parthun Jonathan Widom Daniel E Gottschling

We have isolated the predominant cytoplasmic histone acetyltransferase activity from Saccharomyces cerevisiae. This enzyme acetylates the lysine at residue 12 of free histone H4 but does not modify histone H4 when packaged in chromatin. The activity contains two proteins, Hat1p and Hat2p. Hat1p is the catalytic subunit of the histone acetyltransferase and has an intrinsic substrate specificity ...

Journal: :European journal of clinical chemistry and clinical biochemistry : journal of the Forum of European Clinical Chemistry Societies 1993
D J Waldon M F Kubicek G A Johnson A E Buhl

In our attempt to measure hair growth by hair-specific markers, we used transgenic mice to express the chloramphenicol acetyltransferase gene under the control of an ultrahigh sulphur keratin gene promoter. To quantitate expression of the keratin gene, we required a chloramphenicol acetyltransferase assay which could measure enzyme activity in a single follicle and also could be used to assay a...

Journal: :Applied and environmental microbiology 2010
Justin J Donato Luke A Moe Brandon J Converse Keith D Smart Flora C Berklein Patricia S McManus Jo Handelsman

To gain insight into the diversity and origins of antibiotic resistance genes, we identified resistance genes in the soil in an apple orchard using functional metagenomics, which involves inserting large fragments of foreign DNA into Escherichia coli and assaying the resulting clones for expressed functions. Among 13 antibiotic-resistant clones, we found two genes that encode bifunctional prote...

2003
TARO HAYAKAWA TAMOTSU KANZAKI TSUTOMU KITAMURA

1. The pig heart pyruvate dehydrogenase complex was separated into lipoamide hydrogenase (&I,~ = 5.55 S) and a colorless fraction by the fractionation on a calcium phosphate gel-cellulose column in the presence of 4 M urea. Subsequently, in the presence of 0.3 M potassium iodide, the colorless fraction was fractionated into two additional components, pyruvate dehydrogenase (7.45 S) and partiall...

Journal: :The Journal of biological chemistry 1965
N R MARQUIS I B FRITZ

In an accompanying publication, we have shown that in most tissues there is an approximate correspondence between levels of carnitine acetyltransferase activity and concentrations of carnitine or acetylcarnitine (1). In addition, this correspondence may generally be related to the magnitude of the increase in fatty acid oxidation elicited by added carnitine in particular tissue preparations (1,...

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