The Enzyme Database

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Accepted name: DNA primase AEP
Reaction: (1) ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
(2) ssDNA + n dNTP = ssDNA/pppdN(pdN)n-1 hybrid + (n-1) diphosphate
Other name(s): archaeo-eukaryotic primase; AEP; PrimPol
Systematic name: (deoxy)nucleotide 5′-triphosphate:single-stranded DNA (deoxy)nucleotidyltransferase (DNA or DNA-RNA hybrid synthesizing)
Comments: The enzyme, which is found in eukaryota and archaea, catalyses the synthesis of short RNA or DNA sequences which are used as primers for EC, DNA-directed DNA polymerase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
1.  Desogus, G., Onesti, S., Brick, P., Rossi, M. and Pisani, F.M. Identification and characterization of a DNA primase from the hyperthermophilic archaeon Methanococcus jannaschii. Nucleic Acids Res. 27 (1999) 4444–4450. [PMID: 10536154]
2.  Arezi, B. and Kuchta, R.D. Eukaryotic DNA primase. Trends Biochem. Sci. 25 (2000) 572–576. [PMID: 11084371]
3.  Liu, L., Komori, K., Ishino, S., Bocquier, A.A., Cann, I.K., Kohda, D. and Ishino, Y. The archaeal DNA primase: biochemical characterization of the p41-p46 complex from Pyrococcus furiosus. J. Biol. Chem. 276 (2001) 45484–45490. [PMID: 11584001]
4.  Lao-Sirieix, S.H. and Bell, S.D. The heterodimeric primase of the hyperthermophilic archaeon Sulfolobus solfataricus possesses DNA and RNA primase, polymerase and 3′-terminal nucleotidyl transferase activities. J. Mol. Biol. 344 (2004) 1251–1263. [PMID: 15561142]
5.  Baranovskiy, A.G., Zhang, Y., Suwa, Y., Babayeva, N.D., Gu, J., Pavlov, Y.I. and Tahirov, T.H. Crystal structure of the human primase. J. Biol. Chem. 290 (2015) 5635–5646. [PMID: 25550159]
6.  Guilliam, T.A., Keen, B.A., Brissett, N.C. and Doherty, A.J. Primase-polymerases are a functionally diverse superfamily of replication and repair enzymes. Nucleic Acids Res. 43 (2015) 6651–6664. [PMID: 26109351]
[EC created 2018]

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