Small-Molecule Acetylation by GCN5-Related N -Acetyltransferases in Bacteria | Zendy

Rachel M. Burckhardt | Zendy; Jorge C. EscalanteSemerena | Zendy

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Small-Molecule Acetylation by GCN5-Related N -Acetyltransferases in Bacteria

Author(s) -

Rachel M. Burckhardt,

Jorge C. EscalanteSemerena

Publication year - 2020

Publication title -

microbiology and molecular biology reviews

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 6.358

H-Index - 247

eISSN - 1098-5557

pISSN - 1092-2172

DOI - 10.1128/mmbr.00090-19

Subject(s) - acetyltransferases , acetylation , biology , acetyltransferase , biochemistry , enzyme , moiety , deubiquitinating enzyme , bacteria , gene , microbiology and biotechnology , stereochemistry , genetics , ubiquitin , chemistry

Acetylation is a conserved modification used to regulate a variety of cellular pathways, such as gene expression, protein synthesis, detoxification, and virulence. Acetyltransferase enzymes transfer an acetyl moiety, usually from acetyl coenzyme A (AcCoA), onto a target substrate, thereby modulating activity or stability. Members of theG CN5-N -a cetylt ransferase (GNAT) protein superfamily are found in all domains of life and are characterized by a core structural domain architecture.

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