Results 221 to 230 of about 35,074 (278)
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Annual Review of Biochemistry, 2001
▪ Abstract Transcriptional regulation in eukaryotes occurs within a chromatin setting and is strongly influenced by nucleosomal barriers imposed by histone proteins. Among the well-known covalent modifications of histones, the reversible acetylation of internal lysine residues in histone amino-terminal domains has long been positively linked to ...
S Y, Roth, J M, Denu, C D, Allis
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▪ Abstract Transcriptional regulation in eukaryotes occurs within a chromatin setting and is strongly influenced by nucleosomal barriers imposed by histone proteins. Among the well-known covalent modifications of histones, the reversible acetylation of internal lysine residues in histone amino-terminal domains has long been positively linked to ...
S Y, Roth, J M, Denu, C D, Allis
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Choline acetyltransferase and carnitine acetyltransferase in the placenta of the mouse
Comparative Biochemistry and Physiology Part C: Comparative Pharmacology, 1977Abstract 1. The major 1-14C-acetyl labelled metabolite as identified by high voltage electrophoresis and thin layer chromatography was 1-14C-acetylcarnitine when crude or dialyzed mouse placenta homogenates were incubated in the absence or presence of exogenous 1-carnitine respectively and with 1-14C-acetylcoenzyme A. 2.
F, Welsch, S K, McCarthy
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N-terminal acetylation and other functions of Nα-acetyltransferases
Biological Chemistry, 2012 Protein N-terminal acetylation by N-alpha-acetyltransferases (NATs) is an omnipresent protein modification that affects a large number of proteins. The exact biological role of N-terminal acetylation has, however, remained enigmatic for the overall ...
Petra Van Damme, Kris Gevaert
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Epigenetic Modulation Using Small Molecules - Targeting Histone Acetyltransferases in Disease
Current Medicinal Chemistry, 2017 Histone acetyltransferases (HATs) are epigenetic drivers that catalyze the acetyl transfer from acetyl-CoA to lysines of both histone and non-histone substrates and thereby induce transcription either by chromatin remodeling or direct transcription ...
Angela Koehler, André Richters
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A snapshot of carnitine acetyltransferase
Trends in Biochemical Sciences, 2003Carnitine acetyltransferase (CrAT) is part of the carnitine system that protects the acylation state of the pools of acetyl-coenzyme A, a key metabolic intermediate, by transferring excess acetate and other short-chain acyl groups to and from carnitine. The homology of CrAT with other carnitine acyltransferases, such as carnitine palmitoyltransferase I
Rona R, Ramsay, James H, Naismith
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Histone acetyltransferase complexes
Seminars in Cell & Developmental Biology, 1999Modification of histone amino terminal tails by acetylation has long been linked to the transcriptional capacity of genes in chromatin and to various aspects of chromatin dynamics. Over the last few years a flurry of reports have described the purification and identification of a large number of histone acetyltransferases.
P A, Grant, S L, Berger
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CRC Critical Reviews in Biochemistry, 1977
Acetylcholine is essential to neural function. It synthesis is catalyzed by choline acetyltransferase, the enzyme responsible for the acetylation of choline by acetyl coenzye A, a reaction favored slightly thermodymodynamically and not at all kinetically. An analytically pure enzyme still has not been obtained; however, method of purification have been
Henry G. Mautner, David Nachmansohn
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Acetylcholine is essential to neural function. It synthesis is catalyzed by choline acetyltransferase, the enzyme responsible for the acetylation of choline by acetyl coenzye A, a reaction favored slightly thermodymodynamically and not at all kinetically. An analytically pure enzyme still has not been obtained; however, method of purification have been
Henry G. Mautner, David Nachmansohn
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ACETYLCHOLINE AND CHOLINE ACETYLTRANSFERASE
Neurochemistry International, 1980The thermodynamics and kinetics of the alcoholysis of thiolesters are discussed and related to choline acetyltransferase. The conformation and rotational barriers of acetylcholine are described as is the specific inability of choline to induce depolarization. Evidence is presented for the involvement of imidazole and the non-involvement of thiol groups
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Human acetyltransferase polymorphisms
Mutation Research - Fundamental and Molecular Mechanisms of Mutagenesis, 1997Conjugation of primary amino and hydroxylamino groups with acetate, catalyzed by acetyl CoA-dependent arylamine acetyltransferase (NAT) enzymes, may play an important role in the intricate series of metabolic pathways that produce or prevent toxicity following exposure to homo- and heterocyclic arylamine and hydrazine xenobiotics.
D M, Grant +7 more
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1994
Publisher Summary Acetyltransferases play a central role in the metabolic disposition, detoxication, and bioactivation of a diverse group of drugs—carcinogens and other xenobiotics. Acetylation is a major metabolic pathway for primary aromatic amines (arylamines, ArNH) and hydrazines.
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Publisher Summary Acetyltransferases play a central role in the metabolic disposition, detoxication, and bioactivation of a diverse group of drugs—carcinogens and other xenobiotics. Acetylation is a major metabolic pathway for primary aromatic amines (arylamines, ArNH) and hydrazines.
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