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Literature summary extracted from

  • Zheng, Q.C.; Li, Z.S.; Sun, M.; Zhang, Y.; Sun, C.C.
    Homology modeling and substrate binding study of Nudix hydrolase Ndx1 from Thermos thermophilus HB8 (2005), Biochem. Biophys. Res. Commun., 333, 881-887.
    View publication on PubMed

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.6.1.61 Mg2+ homology modeling techniques shows that Ser38, Leu39 and Glu46, coordinate enzyme-bound Mg2+ ions in the complex of Ndx1 with P1,P6-bis(5'-adenosyl)hexaphosphate Thermus thermophilus

Organism

EC Number Organism UniProt Comment Textmining
3.6.1.61 Thermus thermophilus
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.1.61 additional information homology modeling techniques shows Glu46, Arg88, and Glu90 are three important determinant residues in binding as they have strong hydrogen bonding interactions and electrostatic interactions with P1,P6-bis(5'-adenosyl)hexaphosphate Thermus thermophilus ?
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