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Literature summary for 3.1.5.B1 extracted from

  • Zhu, C.F.; Wei, W.; Peng, X.; Dong, Y.H.; Gong, Y.; Yu, X.F.
    The mechanism of substrate-controlled allosteric regulation of SAMHD1 activated by GTP (2015), Acta Crystallogr. Sect. D, 71, 516-524 .
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
dNTP both GTP and dNTP are required for tetramer activation of the enzyme. SAMHD1 activation is regulated by the concentration of dNTP Homo sapiens
GTP both GTP and dNTP are required for tetramer activation of the enzyme Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
-
Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
structures of the catalytic core of SAMHD1 in complex with different combinations of GTP and dNTPs. SAMHD1 contains two activator-binding sites in the allosteric pocket. The primary activator GTP binds to one site and the substrate dNTP (dATP, dCTP, dUTP or dTTP) occupies the other. Both GTP and dNTP are required for tetramer activation of the enzyme. In the absence of substrate binding, SAMHD1 adopts an inactive dimer conformation even when complexed with GTP Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q9Y3Z3
-
-

Synonyms

Synonyms Comment Organism
SAMHD1
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Homo sapiens