ArticleThe Journal of biological chemistry2012
Human protein N-terminal acetyltransferase hNaa50p (hNAT5/hSAN) follows ordered sequential catalytic mechanism: combined kinetic and NMR study.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 25 citations in OpenAlex.
- Backbone resonance assignments of dopamine N-acetyltransferase in free and cofactor-bound states.Biomolecular NMR assignments · 2025Article
- Optimized bisubstrate inhibitors for the actin N-terminal acetyltransferase NAA80.Frontiers in chemistry · 2023Article
- Characterisation and preliminary functional analysis of N-acetyltransferase 13 from Schistosoma japonicum.BMC veterinary research · 2021Article
- Novel Bisubstrate Inhibitors for Protein N-Terminal Acetyltransferase D.Journal of medicinal chemistry · 2021Article
- Structural basis of Naa20 activity towards a canonical NatB substrate.Communications biology · 2021Article
- Protein N-Terminal Acetylation: Structural Basis, Mechanism, Versatility, and Regulation.Trends in biochemical sciences · 2021Review
- Characterization of SpecificACS medicinal chemistry letters · 2020Article
- Biochemical and structural analysis of N-terminal acetyltransferases.Methods in enzymology · 2019Article
- Structural basis of HypK regulating N-terminal acetylation by the NatA complex.Nature communications · 2017Article
- Human Naa50 Protein Displays Broad Substrate Specificity for Amino-terminal Acetylation: DETAILED STRUCTURAL AND BIOCHEMICAL ANALYSIS USING TETRAPEPTIDE LIBRARY.The Journal of biological chemistry · 2016Article
- Resonance assignment of disordered protein with repetitive and overlapping sequence using combinatorial approach reveals initial structural propensities and local restrictions in the denatured state.Journal of biomolecular NMR · 2016Article
- Crystal Structure of the Golgi-Associated Human Nα-Acetyltransferase 60 Reveals the Molecular Determinants for Substrate-Specific Acetylation.Structure (London, England : 1993) · 2016Article
- Review
- N-terminal modifications of cellular proteins: The enzymes involved, their substrate specificities and biological effects.Proteomics · 2015Review
- Using MUSIC and CC(CO)NH for backbone assignment of two medium-sized proteins not fully accessible to standard 3D NMR.Molecules (Basel, Switzerland) · 2014Article
- Molecular basis for N-terminal acetylation by the heterodimeric NatA complex.Nature structural & molecular biology · 2013Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
N(α)-acetylation is a common protein modification catalyzed by different N-terminal acetyltransferases (NATs). Their essential role in the biogenesis and degradation of proteins is becoming increasingly evident. The NAT hNaa50p preferentially modifies peptides starting with methionine followed by a hydrophobic amino acid. hNaa50p also possesses N(ε)-autoacetylation activity. So far, no eukaryotic NAT has been mechanistically investigated. In this study, we used NMR spectroscopy, bisubstrate kinetic assays, and product inhibition experiments to demonstrate that hNaa50p utilizes an ordered Bi Bi reaction of the Theorell-Chance type. The NMR results, both the substrate binding study and the dynamic data, further indicate that the binding of acetyl-CoA induces a conformational change that is required for the peptide to bind to the active site. In support of an ordered Bi Bi reaction mechanism, addition of peptide in the absence of acetyl-CoA did not alter the structure of the protein. This model is further strengthened by the NMR results using a catalytically inactive hNaa50p mutant.
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