Results 221 to 230 of about 15,918,440 (250)

Protein acetylation in atherosclerosis: beyond inflammation to core cellular processes and therapeutic potential. [PDF]

open access: yesFront Immunol
Dong Z   +9 more
europepmc   +1 more source

Serum Metabolomics Reveals Carnitine Metabolism as a Possible Central Metabolic Axis of Pemafibrate Action. [PDF]

open access: yesInt J Mol Sci
Qian C   +15 more
europepmc   +1 more source

Flagellar glycosylation with pseudaminic acids is widespread in the genus Clostridium. [PDF]

open access: yesBMC Microbiol
Anderson OH   +5 more
europepmc   +1 more source

d-Amino acid-N-acetyltransferase of Saccharomyces cerevisiae: a close homologue of histone acetyltransferase Hpa2p acting exclusively on free d-amino acids

Archives of Microbiology, 2004
D-Amino acid N-acetyltransferase is a unique enzyme of Saccharomyces cerevisiae acting specifically on D-amino acids. The enzyme was found to be encoded by HPA3, a putative histone/protein acetyl transferase gene, and we purified its gene product, Hpa3p, from recombinant Escherichia coli cells.
Tohru Yoshimura
exaly   +3 more sources

Physiological role of d-amino acid-N-acetyltransferase of Saccharomyces cerevisiae: detoxification of d-amino acids

Archives of Microbiology, 2005
Saccharomyces cerevisiae is sensitive to D-amino acids: those corresponding to almost all proteinous L-amino acids inhibit the growth of yeast even at low concentrations (e.g. 0.1 mM). We have determined that D-amino acid-N-acetyltransferase (DNT) of the yeast is involved in the detoxification of D-amino acids on the basis of the following findings ...
Tohru Yoshimura
exaly   +3 more sources

Homology modeling and prediction of the amino acid residues participating in the transfer of acetyl-CoA to arylalkylamine by the N-acetyltransferase from Chryseobacterium sp.

Biotechnology Letters, 2017
To predict the amino acid residues playing important roles in acetyl-CoA and substrate binding and to study the acetyl group transfer mechanism of Chryseobacterium sp. 5-3B N-acetyltransferase (5-3B NatA).A 3-dimensional homology model of 5-3B NatA was constructed to compare the theoretical structure of this compound with the structures of previously ...
Ken-ichi Yoshida, Shinji Takenaka
exaly   +3 more sources

D-Amino-acid N-acetyltransferase

1996
Dietmar Schomburg, Dörte Stephan
exaly   +2 more sources

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