IntEnz

EC 3.6.1.58 - 8-oxo-dGDP phosphatase

IntEnz Enzyme Nomenclature
EC 3.6.1.58

Names

Reactions

• 32063 [IUBMB]
  8-oxo-dGDP

  8-oxo-dGDP

  Name origin: UniProt - CHECKED (C)

  CHEBI:63715

  Formula: C10H12N5O11P2
  Charge: -3

  ChEBI compound status: CHECKED (C)

  

  +

  H₂O

  H2O

  Name origin: UniProt - CHECKED (C)

  CHEBI:15377

  Formula: H2O
  Charge: 0

  ChEBI compound status: CHECKED (C)

  

  =

  8-oxo-dGMP

  8-oxo-dGMP

  Name origin: UniProt - CHECKED (C)

  CHEBI:63224

  Formula: C10H12N5O8P
  Charge: -2

  ChEBI compound status: CHECKED (C)

  

  +

  H⁺

  H(+)

  Name origin: UniProt - CHECKED (C)

  CHEBI:15378

  Formula: H
  Charge: 1

  ChEBI compound status: CHECKED (C)

  

  +

  phosphate

  phosphate

  Name origin: UniProt - CHECKED (C)

  CHEBI:43474

  Formula: HO4P
  Charge: -2

  ChEBI compound status: CHECKED (C)

  
• 62356 [IUBMB]
  8-oxo-GDP

  8-oxo-GDP

  Name origin: UniProt - CHECKED (C)

  CHEBI:143554

  Formula: C10H12N5O12P2
  Charge: -3

  ChEBI compound status: SUBMITTED (S)

  

  +

  H₂O

  H2O

  Name origin: UniProt - CHECKED (C)

  CHEBI:15377

  Formula: H2O
  Charge: 0

  ChEBI compound status: CHECKED (C)

  

  =

  8-oxo-GMP

  8-oxo-GMP

  Name origin: UniProt - CHECKED (C)

  CHEBI:145694

  Formula: C10H12N5O9P
  Charge: -2

  ChEBI compound status: SUBMITTED (S)

  

  +

  H⁺

  H(+)

  Name origin: UniProt - CHECKED (C)

  CHEBI:15378

  Formula: H
  Charge: 1

  ChEBI compound status: CHECKED (C)

  

  +

  phosphate

  phosphate

  Name origin: UniProt - CHECKED (C)

  CHEBI:43474

  Formula: HO4P
  Charge: -2

  ChEBI compound status: CHECKED (C)

  

Comments:

The enzyme catalyses the hydrolysis of both 8-oxo-dGDP and 8-oxo-GDP thereby preventing translational errors caused by oxidative damage. The preferred in vivo substrate is not known. The enzyme does not degrade 8-oxo-dGTP and 8-oxo-GTP to the monophosphates (cf. EC 3.6.1.55, 8-oxo-dGTP diphosphatase) [1,2]. Ribonucleotide diphosphates and deoxyribonucleotide diphosphates are hydrolysed with broad specificity. The bifunctional enzyme NUDT5 also hydrolyses ADP-ribose to AMP and D-ribose 5-phosphate (cf. EC 3.6.1.13, ADP-ribose diphosphatase) [4]. The human enzyme NUDT18 also hydrolyses 8-oxo-dADP and 2-hydroxy-dADP, the latter at a slower rate [6].

Links to other databases

References

1. Ishibashi, T., Hayakawa, H., Ito, R., Miyazawa, M., Yamagata, Y., Sekiguchi, M.
   Mammalian enzymes for preventing transcriptional errors caused by oxidative damage.
   Nucleic Acids Res. 33 : 3779-3784 (2005). [PMID: 16002790]
2. Ishibashi, T., Hayakawa, H., Sekiguchi, M.
   A novel mechanism for preventing mutations caused by oxidation of guanine nucleotides.
   EMBO Rep. 4 : 479-483 (2003). [PMID: 12717453]
3. Kamiya, H., Hori, M., Arimori, T., Sekiguchi, M., Yamagata, Y., Harashima, H.
   NUDT5 hydrolyzes oxidized deoxyribonucleoside diphosphates with broad substrate specificity.
   DNA Repair (Amst.) 8 : 1250-1254 (2009). [PMID: 19699693]
4. Ito, R., Sekiguchi, M., Setoyama, D., Nakatsu, Y., Yamagata, Y., Hayakawa, H.
   Cleavage of oxidized guanine nucleotide and ADP sugar by human NUDT5 protein.
   J. Biochem. 149 : 731-738 (2011). [PMID: 21389046]
5. Zha, M., Zhong, C., Peng, Y., Hu, H., Ding, J.
   Crystal structures of human NUDT5 reveal insights into the structural basis of the substrate specificity.
   J. Mol. Biol. 364 : 1021-1033 (2006). [PMID: 17052728]

[EC 3.6.1.58 created 2012]