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2.7.7.B16: DNA primase

This is an abbreviated version!
For detailed information about DNA primase, go to the full flat file.

Word Map on EC 2.7.7.B16

Reaction

dNTP
+ n dNTP =
dN(pdN)n
 + n diphosphate

Synonyms

archaeal eukaryotic-type primase, DNA primase-polymerase, DnaG primase, Mjpri, Pabp41, Pabp46, pIT3 replication protein, PolpTN2, PriL, PriS, PriSL, PriX, Sso core primase, SsoPriSL

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.7 Nucleotidyltransferases
                2.7.7.B16 DNA primase

Subunits

Subunits on EC 2.7.7.B16 - DNA primase

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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterodimer
heterotrimer
Q9UWW1; Q97Z83; Q97ZS7
archaea encode a eukaryotic-type primase comprising a catalytic subunit, PriS, and a noncatalytic subunit, PriL and PriX. PriX is a diverged homologue of the C-terminal domain of PriL but lacks the iron-sulfur cluster. PriX, PriL and PriS form a stable heterotrimer (PriSLX). Both PriSX and PriSLX show far greater affinity for nucleotide substrates and are substantially more active in primer synthesis than the PriSL heterodimer. PriL, but not PriX, facilitates primer extension by PriS. The catalytic activity of PriS is modulated through concerted interactions with the two noncatalytic subunits in primer synthesis. PriX subunit residues 26-54 are in a flexible region. PriX residues 55-154 fold into a single domain containing 6 helices, which form a compact core stabilized by extensive hydrophobic interactions. The overall structure of the PriX protein is quite unique, sequence and three-dimensional structure comparisons, overview
additional information