Acetoacetyl‐<scp>CoA</scp> synthetase activity is controlled by a protein acetyltransferase with unique domain organization in <i>Streptomyces lividans</i>
Acetoacetyl‐<scp>CoA</scp> synthetase activity is controlled by a protein acetyltransferase with unique domain organization in <i>Streptomyces lividans</i> is a research paper published in Molecular Microbiology (2013). On theSindex it has a DataRank of 1.8. It has been cited 50 times, with 39 citing works in its 1-hop citation network.
Abstract
SummaryGCN5‐type N‐acetyltransferases (GNATs) are enzymes that catalyse the transfer of the acetyl group from acetyl‐CoA to a primary amine. GNATs are conserved in all domains of life. Some members of this family of enzymes acetylate the side‐chain of specific lysine residues in proteins of diverse function. In bacteria, GNAT‐catalysed protein acetylation regulates carbon metabolism, RNA metabolism and transcriptional regulation. Metabolic regulation in Streptomyces species is of interest due to the role of these organisms in natural product synthesis. Here we identify SlPatA, a GNAT in Streptomyces lividans with unique domain organization, and a new acetylation target, namely acetoacetyl‐CoA synthetase (SlAacS). The latter has homologues in all domains of life. In vitro and in vivo evidence show that SlAacS is a bona fide acetoacetyl‐CoA synthetase. SlPatA acetylates SlAacS more efficiently than it does acetyl‐CoA synthetase, an enzyme known to be under acetylation control. SlPatA acetylates SlAacS at the active‐site residue Lys617 and acetylation inactivates SlAacS. Acetylated SlAacS was deacetylated by a sirtuin‐type protein deacetylase. SlAacS acetylation/deacetylation may represent a conserved mechanism for regulation of acetoacetyl‐CoA synthetase activity in all domains of life.
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FAIR Checklist
Context only (not used in score)- Has DOI
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DataRank Breakdown
Base Score Contribution
0.590
From this paper's citation signal
Citation Network Contribution
1.2
From 34 citing papers with measurable signal
Top 5 citers driving the network score
Ranked by citation count — the same ordering the engine uses when summing log1p(Cq) over citers.
- One-step inactivation of chromosomal genes in <i>Escherichia coli</i> K-12 using PCR productsProceedings of the National Academy of Sciences200015,089 citationsDataRank 1.4
- Lysine Acetylation Targets Protein Complexes and Co-Regulates Major Cellular FunctionsScience20094,020 citationsDataRank 1.2
- Structure and functions of the GNAT superfamily of acetyltransferasesArchives of Biochemistry and Biophysics2005632 citationsDataRank 12.9
- Reversible Acetylation and Inactivation of <i>Mycobacterium tuberculosis</i> Acetyl-CoA Synthetase Is Dependent on cAMPBiochemistry2011109 citationsDataRank 4.5
- System-wide Studies of N-Lysine Acetylation in Rhodopseudomonas palustris Reveal Substrate Specificity of Protein AcetyltransferasesJournal of Biological Chemistry201279 citationsDataRank 3.6
Why this DataRank?
DataRank blends this paper's own citation count with the influence of the papers that cite it. Here, roughly 33% comes from its base citations and 67% from the citation network (34 citing papers contributed measurable signal).
- Base score B(p)
- log1p(citation_count) — grows sub-linearly, so a paper with 1,000 citations is not 10× a paper with 100.
- Network N(p)
- Σ over citers of log1p(Cq) ÷ max(outdegreeq, 1). Being cited by a highly-cited paper with few references counts most.
- Damping factor d = 0.85
- DataRank = (1−d)·B(p) + d·N(p) — the two cards above are each already multiplied by their share.
- Self-citations excluded
- Citers sharing any OpenAlex author ID with this paper are filtered out before the network sum.
Citers are pulled from OpenAlex sorted by cited_by_count:descand capped per paper, so when the cap binds we keep the highest-signal references and the score is reproducible across reruns.
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