New AMP‐forming acid:CoA ligases from <i>Streptomyces lividans</i>, some of which are posttranslationally regulated by reversible lysine acetylation

Burckhardt, Rachel M.; VanDrisse, Chelsey M.; Tucker, Alex C.; Escalante‐Semerena, Jorge C.

doi:10.1111/mmi.14414

Cited by 6 publications

(3 citation statements)

References 47 publications

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“…This lysine is highly conserved in all aryl-CoA ligases and throughout the acyl-CoA and fatty acid acyl-CoA ligases. The lysine residue is the target of acetylation as a posttranslational regulation mechanism ( 66 , 67 ). Reversible lysine acylation in prokaryotes is a relatively new field of study.…”

Section: Structural Features and Conserved Residues Of Aryl-coa Ligasesmentioning

confidence: 99%

Aryl Coenzyme A Ligases, a Subfamily of the Adenylate-Forming Enzyme Superfamily

Arnold

Kaplieva-Dudek

Heker

2021

Appl Environ Microbiol

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Aryl-CoA ligases belong to class I of the adenylate-forming enzyme superfamily (ANL superfamily) and catalyze the formation of thioester bonds between aromatic compounds and Coenzyme A (CoA) and occur in nearly all forms of life. These ligases are involved in various metabolic pathways degrading benzene, toluene, ethylbenzene, and xylene (BTEX) or polycyclic aromatic hydrocarbons (PAHs). They are often necessary to produce the central intermediate benzoyl-CoA that occurs in various anaerobic pathways. The substrate specificity is very diverse between enzymes within the same class, while the dependency on Mg 2+ , ATP and CoA as well as oxygen insensitivity are characteristics shared by the whole enzyme-class. Some organisms employ the same aryl-CoA ligase when growing aerobically and anaerobically, while others induce different enzymes depending on the environmental conditions. Aryl-CoA ligases can be divided into two major groups, benzoate:CoA ligase-like enzymes and phenylacetate:CoA ligase-like enzymes. They are widely distributed between the phylogenetic clades of the ANL superfamily and show closer relations within the subfamilies than to other aryl-CoA ligases. This, together with residual CoA-ligase activity in various other enzymes of the ANL superfamily, leads to the conclusion that CoA ligases might be the ancestral proteins from which all other ANL superfamily enzymes developed.

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Section: Structural Features and Conserved Residues Of Aryl-coa Ligasesmentioning

confidence: 99%

Aryl Coenzyme A Ligases, a Subfamily of the Adenylate-Forming Enzyme Superfamily

Arnold

Kaplieva-Dudek

Heker

2021

Appl Environ Microbiol

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“…For mammalian cytosolic and mitochondrial AMP-forming enzymes, AceS1 and AceS2, a regulation via lysine acetylation has been found 43 . The acetylation of AMP-forming acetyl-CoA synthetases is enzymatically catalysed by acetyltransferases and can be reversed by classical Zn 2+ -dependent enzymes and by NAD + -dependent sirtuins both, in prokaryotes and eukaryotes 14 , 34 , 35 , 43 , 55 , 60 , 115 . So far acetylation of AMP-forming acetyl-CoA synthetases was exclusively shown to be catalysed by GCN5-related N-acetyltransferases suggesting that the observed Pta activity might be realized also in other systems 21 , 34 , 60 , 80 , 116 .…”

Section: Discussionmentioning

confidence: 99%

Acetyl-CoA synthetase activity is enzymatically regulated by lysine acetylation using acetyl-CoA or acetyl-phosphate as donor molecule

Qin,

Graf,

Striska

et al. 2024

Nat Commun

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The AMP-forming acetyl-CoA synthetase is regulated by lysine acetylation both in bacteria and eukaryotes. However, the underlying mechanism is poorly understood. The Bacillus subtilis acetyltransferase AcuA and the AMP-forming acetyl-CoA synthetase AcsA form an AcuA•AcsA complex, dissociating upon lysine acetylation of AcsA by AcuA. Crystal structures of AcsA from Chloroflexota bacterium in the apo form and in complex with acetyl-adenosine-5′-monophosphate (acetyl-AMP) support the flexible C-terminal domain adopting different conformations. AlphaFold2 predictions suggest binding of AcuA stabilizes AcsA in an undescribed conformation. We show the AcuA•AcsA complex dissociates upon acetyl-coenzyme A (acetyl-CoA) dependent acetylation of AcsA by AcuA. We discover an intrinsic phosphotransacetylase activity enabling AcuA•AcsA generating acetyl-CoA from acetyl-phosphate (AcP) and coenzyme A (CoA) used by AcuA to acetylate and inactivate AcsA. Here, we provide mechanistic insights into the regulation of AMP-forming acetyl-CoA synthetases by lysine acetylation and discover an intrinsic phosphotransacetylase allowing modulation of its activity based on AcP and CoA levels.

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“…The S. lividans is involved in post-translational modification by acylation at lysine residue of active site for production of CoA ligases and many organic acids (Burckhardt et al, 2020). The cyclic antimicrobial peptide receptor protein and novel lipopeptide daptomycin are produced by S. roseosporus (Wu et al, 2021).…”

Section: Introductionmentioning

confidence: 99%

Promising bioactive metabolites of mangrove inhabitant Streptomyces tauricus and prostate cancer PC3 cell inhibition by antimicrobial peptides

Karthik,

Kalyani,

Krishnappa

et al. 2023

Front. Microbiol.

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Streptomyces is a group of microbes known for antibiotic production and has contributed to more than 70% of present commercially available antibiotics. These antibiotics are important in the management, protection, and treatment of chronic illnesses. In the present study, the isolated S. tauricus strain from mangrove soil in Mangalore, India (GenBank accession number: MW785875) was subjected for differential cultural characterization, phenotype involving brown pigmentation, filamentous mycelia, and ash-colored spore production was observed using field emission scanning electron microscopy (FESEM) analysis revealing filamentous mycelia possessing a straight spore chain. Spores were visualized as elongated, rod-shaped, smooth surfaces with curved edges. After optimized growth conditions for S. tauricus on starch-casein agar medium, the GC/MS analysis of S. tauricus intracellular extract detected bioactive compounds reported for pharmacological applications. Analyzed using the NIST library, most of the bioactive compounds identified in intracellular extract had molecular weights of less than 1 kDa. On the PC3 cell line, the Sephadex G-10 partially purified eluted peak protein fraction demonstrated significant anticancer activity. The LCMS analysis revealed the presence of Tryprostatin B, Fumonisin B1, Microcystin LR, and Surfactin C with molecular weights below 1 kDa. This study found that small molecular weight microbial compounds are more effective in a variety of biological applications.

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New AMP‐forming acid:CoA ligases from Streptomyces lividans, some of which are posttranslationally regulated by reversible lysine acetylation

Cited by 6 publications

References 47 publications

Aryl Coenzyme A Ligases, a Subfamily of the Adenylate-Forming Enzyme Superfamily

Aryl Coenzyme A Ligases, a Subfamily of the Adenylate-Forming Enzyme Superfamily

Acetyl-CoA synthetase activity is enzymatically regulated by lysine acetylation using acetyl-CoA or acetyl-phosphate as donor molecule

Promising bioactive metabolites of mangrove inhabitant Streptomyces tauricus and prostate cancer PC3 cell inhibition by antimicrobial peptides

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