Specificity and versatility of substrate binding sites in four catalytic domains of human N-terminal acetyltransferases

Nt-acetylation is among the most common protein modifications in eukaryotes. Although thought for a long time to protect proteins from degradation, the role of Nt-acetylation is still debated. It is catalyzed by enzymes called N-terminal acetyltransferases (NATs). In eukaryotes, several NATs, compos...

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Veröffentlicht in:	PloS one 2012-12, Vol.7 (12), p.e52642-e52642
Hauptverfasser:	Grauffel, Cédric, Abboud, Angèle, Liszczak, Glen, Marmorstein, Ronen, Arnesen, Thomas, Reuter, Nathalie
Format:	Artikel
Sprache:	eng
Schlagworte:	Acetyl Coenzyme A - chemistry Acetyl Coenzyme A - metabolism Acetylation Alanine Amino Acid Sequence Amino acids Analysis Binding Sites Biology Bonding strength Bonds (Securities) Catalysis Catalytic Domain Catalytic subunits Chemical bonds Chemistry Computer simulation Enzymes Eukaryotes Homology Humans Hydrogen Hydrogen Bonding Hydrogen bonds Hydrogen ion concentration Hydrophobicity Kinetics Ligands Molecular biology Molecular dynamics Molecular Dynamics Simulation Molecular Sequence Data Mutants N-Terminal Acetyltransferase E - chemistry N-Terminal Acetyltransferase E - genetics N-Terminal Acetyltransferase E - metabolism N-Terminal Acetyltransferases - chemistry N-Terminal Acetyltransferases - genetics N-Terminal Acetyltransferases - metabolism Nitrogen - chemistry Peptides Peptides - chemistry Point Mutation Protein Binding Proteins Sequence Alignment Sequences Studies Substrate Specificity Substrates
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