ArticleJournal of the American Chemical Society2012
Revelation of a catalytic calcium-binding site elucidates unusual metal dependence of a human apyrase.
Article in Journal of the American Chemical Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 23 citations in OpenAlex.
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- Born-Oppenheimer Ab Initio QM/MM Molecular Dynamics Simulations of Enzyme Reactions.Methods in enzymology · 2016Article
- Thiol versus hydroxamate as zinc binding group in HDAC inhibition: An ab initio QM/MM molecular dynamics study.Journal of computational chemistry · 2015Article
- Extracellular Streptomyces lividans vesicles: composition, biogenesis and antimicrobial activity.Microbial biotechnology · 2015Article
- Mechanistic insights into a classic wonder drug--aspirin.Journal of the American Chemical Society · 2015Article
- Catalytic mechanism of histone acetyltransferase p300: from the proton transfer to acetylation reaction.The journal of physical chemistry. B · 2014Article
- DNA cytosine methylation: structural and thermodynamic characterization of the epigenetic marking mechanism.Biochemistry · 2013Article
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Authors and funding
3 authors at 1 institution in 1 country.
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Abstract
Human soluble calcium-activated nucleotidase 1 (hSCAN-1) represents a new family of apyrase enzymes that catalyze the hydrolysis of nucleotide di- and triphosphates, thereby modulating extracellular purinergic and pyrimidinergic signaling. Among well-characterized phosphoryl transfer enzymes, hSCAN-1 is unique not only in its unusual calcium-dependent activation, but also in its novel phosphate-binding motif. Its catalytic site does not utilize backbone amide groups to bind phosphate, as in the common P-loop, but contains a large cluster of acidic ionizable side chains. By employing a state-of-the-art computational approach, we have revealed a previously uncharacterized catalytic calcium-binding site in hSCAN-1, which elucidates the unusual calcium-dependence of its apyrase activity. In a high-order coordination shell, the newly identified calcium ion organizes the active site residues to mediate nucleotide binding, to orient the nucleophilic water, and to facilitate the phosphoryl transfer reaction. From ab initio QM/MM molecular dynamics simulations with umbrella sampling, we have characterized a reverse protonation catalytic mechanism for hSCAN-1 and determined its free energy reaction profile. Our results are consistent with available experimental studies and provide new detailed insight into the structure-function relationship of this novel calcium-activated phosphoryl transfer enzyme.
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