EC 3.1.3.108 - Nocturnin

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IntEnz Enzyme Nomenclature
EC 3.1.3.108

Names

Accepted name:
nocturnin
Other name:
nocturnin (curled)
Systematic name:
NADPH 2'-phosphohydrolase

Reactions

Comments:

The mammalian mitochondrial enzyme is a rhythmically expressed protein that regulates metabolism under the control of circadian clock. It has a slight preference for NADPH over NADP+. The archaeal enzyme, identified in Methanocaldococcus jannaschii, is bifunctional acting as NAD kinase (EC 2.7.1.23) and NADP phosphatase with a slight preference for NADP+ over NADPH.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB

References

  1. Kawai, S., Murata, K.
    Structure and function of NAD kinase and NADP phosphatase: key enzymes that regulate the intracellular balance of NAD(H) and NADP(H).
    Biosci. Biotechnol. Biochem. 72 : 919-930 (2008). [PMID: 18391451]
  2. Abshire, E. T., Chasseur, J., Bohn, J. A., Del Rizzo, P. A., Freddolino, P. L., Goldstrohm, A. C., Trievel, R. C.
    The structure of human Nocturnin reveals a conserved ribonuclease domain that represses target transcript translation and abundance in cells.
    Nucleic Acids Res. 46 : 6257-6270 (2018). [PMID: 29860338]
  3. Estrella, M. A., Du, J., Korennykh, A.
    Crystal Structure of Human Nocturnin Catalytic Domain.
    Sci Rep 8 : 16294 (2018). [PMID: 30389976]
  4. Estrella, M. A., Du, J., Chen, L., Rath, S., Prangley, E., Chitrakar, A., Aoki, T., Schedl, P., Rabinowitz, J., Korennykh, A.
    The metabolites NADP+ and NADPH are the targets of the circadian protein Nocturnin (Curled).
    Nat Commun 10 : 2367 (2019). [PMID: 31147539]

[EC 3.1.3.108 created 2020]