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Literature summary for 3.6.1.15 extracted from

  • Shalaeva, D.N.; Cherepanov, D.A.; Galperin, M.Y.; Golovin, A.V.; Mulkidjanian, A.Y.
    Evolution of cation binding in the active sites of P-loop nucleoside triphosphatases in relation to the basic catalytic mechanism (2018), eLife, 7, e37373 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.6.1.15

Activating Compound

Activating Compound Comment Organism Structure
additional information activation mechanism, overview. Catalytic activity of P-loop NTPases typically depends upon their interaction with other proteins or domains of the same protein or RNA/DNA molecules, upon this interaction, activating Arg or Lys fingers are inserted into the catalytic site Escherichia coli
additional information activation mechanism, overview. Catalytic activity of P-loop NTPases typically depends upon their interaction with other proteins or domains of the same protein or RNA/DNA molecules, upon this interaction, activating Arg or Lys fingers are inserted into the catalytic site Arabidopsis thaliana

Metals/Ions

Metals/Ions Comment Organism Structure
K+ binding structure analysis, activates Escherichia coli
K+ binding structure analysis, activates Arabidopsis thaliana
Mg2+ dependent on, activates Escherichia coli
Mg2+ dependent on, activates Arabidopsis thaliana
additional information cation binding to Mg2+-NTP complexes in water, molecular dynamics simulations, overview. Cation binding induces eclipsed conformation of the phosphate chain. Activation of P-loop NTPases by monovalent cations Escherichia coli
additional information cation binding to Mg2+-NTP complexes in water, molecular dynamics simulations, overview. Cation binding induces eclipsed conformation of the phosphate chain. Activation of P-loop NTPases by monovalent cations Arabidopsis thaliana
Na+ binding structure analysis, activates Escherichia coli
Na+ binding structure analysis, activates Arabidopsis thaliana
NH4+ binding structure analysis, activates Escherichia coli
NH4+ binding structure analysis, activates Arabidopsis thaliana

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O Escherichia coli
-
 ADP + phosphate
-
 ?
ATP + H2O Arabidopsis thaliana
-
 ADP + phosphate
-
 ?
GTP + H2O Escherichia coli
-
 GDP + phosphate
-
 ?
GTP + H2O Arabidopsis thaliana
-
 GDP + phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana
-
-
-
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O
-
 Escherichia coli ADP + phosphate
-
 ?
ATP + H2O
-
 Arabidopsis thaliana ADP + phosphate
-
 ?
GTP + H2O
-
 Escherichia coli GDP + phosphate
-
 ?
GTP + H2O
-
 Arabidopsis thaliana GDP + phosphate
-
 ?
additional information substrate binding structures in presence of Mg2+, NMR structures, overview Escherichia coli ?
-
-
additional information substrate binding structures in presence of Mg2+, NMR structures, overview Arabidopsis thaliana ?
-
-

Synonyms

Synonyms Comment Organism
nucleoside triphosphatase
-
 Escherichia coli
nucleoside triphosphatase
-
 Arabidopsis thaliana
P-loop NTPase
-
 Escherichia coli
P-loop NTPase
-
 Arabidopsis thaliana

General Information

General Information Comment Organism
evolution evolution of cation binding in the active sites of P-loop nucleoside triphosphatases in relation to the basic catalytic mechanism, overview Escherichia coli
evolution evolution of cation binding in the active sites of P-loop nucleoside triphosphatases in relation to the basic catalytic mechanism, overview Arabidopsis thaliana
additional information combined comparative structure analysis with molecular dynamics simulations of Mg-ATP and Mg-GTP complexes in water and in the presence of potassium, sodium, or ammonium ions. In all analyzed structures of diverse P-loop NTPases, the conserved P-loop motif keeps the triphosphate chain of bound NTPs (or their analogues) in an extended, catalytically prone conformation, similar to that imposed on NTPs in water by potassium or ammonium ions. Mg-NTP complexes and their binding in the active sites of P-loop NTPases, substrate binding, structure overview. Catalytic activity of P-loop NTPases typically depends upon their interaction with other proteins or domains of the same protein or RNA/DNA molecules, upon this interaction, activating Arg or Lys fingers are inserted into the catalytic site. Some P-loop NTPases functionally depend not on Arg/Lys fingers, but on monovalent cations. Molecular dynamics simulations, overview Escherichia coli
additional information combined comparative structure analysis with molecular dynamics simulations of Mg-ATP and Mg-GTP complexes in water and in the presence of potassium, sodium, or ammonium ions. In all analyzed structures of diverse P-loop NTPases, the conserved P-loop motif keeps the triphosphate chain of bound NTPs (or their analogues) in an extended, catalytically prone conformation, similar to that imposed on NTPs in water by potassium or ammonium ions. Mg-NTP complexes and their binding in the active sites of P-loop NTPases, substrate binding, structure overview. Catalytic activity of P-loop NTPases typically depends upon their interaction with other proteins or domains of the same protein or RNA/DNA molecules, upon this interaction, activating Arg or Lys fingers are inserted into the catalytic site. Some P-loop NTPases functionally depend not on Arg/Lys fingers, but on monovalent cations. Molecular dynamics simulations, overview Arabidopsis thaliana