DNPH1 hydrolyses dGMP

Stable Identifier
Reaction [transition]
Homo sapiens
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2'-deoxynucleoside 5'-phosphate N-hydrolase 1 (DNPH1 aka c-Myc-responsive protein RCL) is a cytosolic protein which catalyses the cleavage of the N-glycosidic bond of deoxyribonucleoside 5'-monophosphates to yield deoxyribose 5-phosphate (2DORP) and a purine or pyrimidine base. Of the six 2'-deoxynucleoside 5'-monophosphates, DNPH1 has highest affinity for the purine deoxynucleotide dGMP (Amiable et al. 2013). The same affinity for purine deoxynucleotides over pyrimidine deoxynucleotides was observed for rat Dnph1 (Ghiorghi et al. 2007). DNPH1 is a potential target for anti-cancer therapies (Amiable et al. 2014) as it is involved in cellular proliferation and is up-regulated in several types of cancer.

Literature References
PubMed ID Title Journal Year
17234634 The c-Myc target gene Rcl (C6orf108) encodes a novel enzyme, deoxynucleoside 5'-monophosphate N-glycosidase

Ghiorghi, YK, Zeller, KI, Dang, CV, Kaminski, PA

J. Biol. Chem. 2007
25108359 6-(Hetero)Arylpurine nucleotides as inhibitors of the oncogenic target DNPH1: synthesis, structural studies and cytotoxic activities

Amiable, C, Paoletti, J, Haouz, A, Padilla, A, Labesse, G, Kaminski, PA, Pochet, S

Eur J Med Chem 2014
24260472 N (6)-substituted AMPs inhibit mammalian deoxynucleotide N-hydrolase DNPH1

Amiable, C, Pochet, S, Padilla, A, Labesse, G, Kaminski, PA

PLoS ONE 2013
Participant Of
Catalyst Activity
Catalyst Activity
deoxyribonucleoside 5'-monophosphate N-glycosidase activity of DNPH1 [cytosol]
Physical Entity
Orthologous Events
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