NT5E:Zn2+ hydrolyses NAD+

Stable Identifier
Reaction [transition]
Homo sapiens
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5'-nucleotidase (NT5E, CD73) is able to hydrolyse extracellular nucleotides into membrane permeable nucleosides. It displays a broad specificity, acting on mono- or di-nucleotide nicotinamides and different adenosine phosphates, with maximal activity on 5'-adenosine monophosphate. Human NT5E can hydrolyse both NAD+ and NMN, suggesting a role in NAD metabolism (Garavaglia et al. 2012). NT5E is a glycolipid-anchored plasma membrane enzyme (Misumi et al. 1990) that is active in dimeric form and requires one zinc ion per subunit (Zimmermann 1992).

Literature References
PubMed ID Title Journal Year
1637327 5'-nucleotidase: molecular structure and functional aspects

Zimmermann, H

Biochem J 1992
2129526 Primary structure of human placental 5'-nucleotidase and identification of the glycolipid anchor in the mature form

Ogata, S, Ikehara, Y, Misumi, Y, Hirose, S, Ohkubo, K

Eur J Biochem 1990
21933152 The high-resolution crystal structure of periplasmic Haemophilus influenzae NAD nucleotidase reveals a novel enzymatic function of human CD73 related to NAD metabolism

Sturla, L, Canella, L, Garavaglia, S, Mannino, E, Rizzi, M, Allegrone, G, Millo, E, Bruzzone, S, De Flora, A, Cassani, C

Biochem. J. 2012
Catalyst Activity

5'-nucleotidase activity of NT5E:Zn2+ dimer [plasma membrane]

Orthologous Events
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