ArticleProtein science : a publication of the Protein Society2021
Criticality of a conserved tyrosine residue in the SpeG protein from Escherichia coli.
Article in Protein science : a publication of the Protein Society, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 7 citations in OpenAlex.
- Roles of acidic residues in SpeG acetyltransferases-insights into importance for kinetic activity and polyamine binding in allosteric and acceptor sites.The Biochemical journal · 2026Article
- Structural, functional, and regulatory evaluation of a cysteine post-translationally modified Gcn5-related N-acetyltransferase.Biochemical and biophysical research communications · 2025Article
- A Structurally Diverse Compound Screening Library to Identify Substrates for Diamine, Polyamine, and Related Acetyltransferases.ACS omega · 2024Article
- Spermine enhances the activity of anti-tuberculosis drugs.Microbiology spectrum · 2024Article
- The efflux pumps Rv1877 and Rv0191 play differential roles in the protection ofFrontiers in microbiology · 2024Article
- Article
- GLO1 Contributes to the Drug Resistance ofInfection and drug resistance · 2022Article
- Criticality of a conserved tyrosine residue in the SpeG protein from Escherichia coli.Protein science : a publication of the Protein Society · 2021Article
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4 authors at 1 institution in 1 country.
Funding
Abstract
The SpeG spermidine/spermine N-acetyltransferase (SSAT) from Escherichia coli belongs to the Gcn5-related N-acetyltransferase (GNAT) superfamily of proteins. In vitro characterization of this enzyme shows it acetylates the polyamines spermine and spermidine, with a preference toward spermine. This enzyme has a conserved tyrosine residue (Y135) that is found in all SSAT proteins and many GNAT functional subfamilies. It is located near acetyl coenzyme A in the active center of these proteins and has been suggested to act as a general acid in a general acid/base chemical mechanism. In contrast, a previous study showed this residue was not critical for E. coli SpeG enzymatic activity when mutated to phenylalanine. This result was quite different from previous studies with a comparable residue in the human and mouse SSAT proteins, which also acetylate spermine and spermidine. Therefore, we constructed several mutants of the E. coli SpeG Y135 residue and tested their enzymatic activity. We found this conserved residue was indeed critical for E. coli SpeG enzyme activity and may behave similarly in other SSAT proteins.
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