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Literature summary extracted from

  • Kiburu, I.N.; LaRonde-LeBlanc, N.
    Interaction of Rio1 kinase with toyocamycin reveals a conformational switch that controls oligomeric state and catalytic activity (2012), PLoS ONE, 7, e37371.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.11.1
-
 Archaeoglobus fulgidus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.11.1 X-ray crystal structure of toyocamycin bound to Rio1 at 2.0 A, toyocamycin binds in the ATP binding pocket of the protein Archaeoglobus fulgidus

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.11.1 ATP substrate inhibition. At ATP concentrations above 0.1 mM, kinase activity begins to drop until at 100 mM it becomes almost unmeasurable Archaeoglobus fulgidus
2.7.11.1 Toyocamycin toyocamycin binds in the ATP binding pocket of the protein more tightly than ATP/Mg2+ Archaeoglobus fulgidus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.11.1 0.0008
-
 ATP pH 8.0, 37°C Archaeoglobus fulgidus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.11.1 30100
-
 x * 30100, calculated from sequence, autophosphorylation by Rio1 reduces oligomer formation and promotes monomerization, resulting in the most active species. Interaction of Rio1 kinase with toyocamycin reveals a conformational switch that controls oligomeric state and catalytic activity Archaeoglobus fulgidus

Organism

EC Number Organism UniProt Comment Textmining
2.7.11.1 Archaeoglobus fulgidus O28471
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.11.1
-
 Archaeoglobus fulgidus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.11.1 ATP + a protein
-
 Archaeoglobus fulgidus ADP + a phosphoprotein
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.11.1 oligomer x * 30100, calculated from sequence, autophosphorylation by Rio1 reduces oligomer formation and promotes monomerization, resulting in the most active species. Interaction of Rio1 kinase with toyocamycin reveals a conformational switch that controls oligomeric state and catalytic activity Archaeoglobus fulgidus

Synonyms

EC Number Synonyms Comment Organism
2.7.11.1 afRio1 kinase
-
 Archaeoglobus fulgidus
2.7.11.1 Rio1 kinase
-
 Archaeoglobus fulgidus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.7.11.1 76
-
 Tm-value of unbound enzyme Archaeoglobus fulgidus
2.7.11.1 82
-
 Tm-value in presence of ATP and Mg2+ Archaeoglobus fulgidus
2.7.11.1 82
-
 Tm-value in presence of sangivamycin Archaeoglobus fulgidus
2.7.11.1 88
-
 Tm-value in presence of toyocamycin Archaeoglobus fulgidus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.7.11.1 0.0071
-
 ATP pH 8.0, 37°C Archaeoglobus fulgidus