Abstract
Long known for their role in histone acetylation, recent studies have demonstrated that lysine acetyltransferases also carry out distinct "orphan" functions. These activities impact a wide range of biological phenomena including metabolism, RNA modification, nuclear morphology, and mitochondrial function. Here, we review the discovery and characterization of orphan lysine acetyltransferase functions. In addition to highlighting the evidence and biological role for these functions in human disease, we discuss the part emerging chemical tools may play in investigating this versatile enzyme superfamily.
MeSH terms
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Acetyl Coenzyme A / chemistry
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Acetyl Coenzyme A / metabolism
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Acetyl-CoA C-Acetyltransferase / chemistry
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Acetyl-CoA C-Acetyltransferase / metabolism
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Acetylation
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Acetyltransferases / chemistry
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Acetyltransferases / genetics
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Acetyltransferases / pharmacology*
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Animals
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Humans
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Lysine / metabolism*
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N-Terminal Acetyltransferase E / chemistry
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N-Terminal Acetyltransferase E / metabolism
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N-Terminal Acetyltransferases
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Protein Processing, Post-Translational*
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RNA Processing, Post-Transcriptional
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p300-CBP Transcription Factors / chemistry
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p300-CBP Transcription Factors / metabolism
Substances
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Acetyl Coenzyme A
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Acetyltransferases
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N-Terminal Acetyltransferase E
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p300-CBP Transcription Factors
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p300-CBP-associated factor
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N-Terminal Acetyltransferases
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NAT10 protein, human
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ACAT1 protein, human
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Acetyl-CoA C-Acetyltransferase
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Lysine
Grants and funding
National Institutes of Health, United States