EC |
2.7.7.101 |
Accepted name: |
DNA primase DnaG |
Reaction: |
ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate |
Other name(s): |
DnaG |
Systematic name: |
nucleotide 5′-triphosphate:single-stranded DNA nucleotidyltransferase (DNA-RNA hybrid synthesizing) |
Comments: |
The enzyme catalyses the synthesis of short RNA sequences that are used as primers for EC 2.7.7.7, DNA-directed DNA polymerase. It is found in bacteria and archaea. The latter also have a second primase system (EC 2.7.7.102, DNA primase AEP). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Rowen, L. and Kornberg, A. Primase, the dnaG protein of Escherichia coli. An enzyme which starts DNA chains. J. Biol. Chem. 253 (1978) 758–764. [PMID: 340457] |
2. |
Ilyina, T.V., Gorbalenya, A.E. and Koonin, E.V. Organization and evolution of bacterial and bacteriophage primase-helicase systems. J. Mol. Evol. 34 (1992) 351–357. [PMID: 1569588] |
3. |
Frick, D.N. and Richardson, C.C. DNA primases. Annu. Rev. Biochem. 70 (2001) 39–80. [PMID: 11395402] |
4. |
Zuo, Z., Rodgers, C.J., Mikheikin, A.L. and Trakselis, M.A. Characterization of a functional DnaG-type primase in archaea: implications for a dual-primase system. J. Mol. Biol. 397 (2010) 664–676. [PMID: 20122937] |
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[EC 2.7.7.101 created 2018] |
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