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  2. DnaG - Wikipedia

    en.wikipedia.org/wiki/DnaG

    The E. Coli DnaG primase is a 581 residue monomeric protein with three functional domains, according to proteolysis studies. There is an N-terminal Zinc-binding domain (residues 1–110) where a zinc ion is tetrahedrally coordinated between one histidine and three cysteine residues, which plays a role in recognizing sequence specific DNA binding sites.

  3. DNA polymerase I - Wikipedia

    en.wikipedia.org/wiki/DNA_polymerase_I

    DNA polymerase I (or Pol I) is an enzyme that participates in the process of prokaryotic DNA replication. Discovered by Arthur Kornberg in 1956, [1] it was the first known DNA polymerase (and the first known of any kind of polymerase). It was initially characterized in E. coli and is ubiquitous in prokaryotes.

  4. Primase - Wikipedia

    en.wikipedia.org/wiki/Primase

    There are two main types of primase: DnaG found in most bacteria, and the AEP (Archaeo-Eukaryote Primase) superfamily found in archaean and eukaryotic primases. While bacterial primases (DnaG-type) are composed of a single protein unit (a monomer) and synthesize RNA primers, AEP primases are usually composed of two different primase units (a heterodimer) and synthesize two-part primers with ...

  5. Primer (molecular biology) - Wikipedia

    en.wikipedia.org/wiki/Primer_(molecular_biology)

    The second way to cleave a RNA primer is by degrading the RNA strand using a RNase, in eukaryotes it’s known as the RNase H2. This enzyme degrades most of the annealed RNA primer, except the nucleotides close to the 5’ end of the primer. Thus, the remaining nucleotides are displayed into a flap that is cleaved off using FEN-1.

  6. Nitrous-oxide reductase - Wikipedia

    en.wikipedia.org/wiki/Nitrous-oxide_reductase

    Nitrous-oxide reductase is a homodimer that is located in the bacterial periplasm. X-ray structures of the enzymes from Pseudomonas nautica and Paracoccus denitrificans have revealed that each subunit (MW=65 kDa) is organized into two domains. [7]

  7. Heme oxygenase - Wikipedia

    en.wikipedia.org/wiki/Heme_oxygenase

    A critical role of the prokaryotic HMOX systems is to facilitate acquisition of nutritional iron from a eukaryotic host. [20] Some heme-degrading prokaryotic enzymes produce products such as formaldehyde rather than CO. As an example, certain pathogens such as Escherichia coli O157:H7 can express the non-CO producing ChuW isoform. Many ...

  8. Oxidative phosphorylation - Wikipedia

    en.wikipedia.org/wiki/Oxidative_phosphorylation

    In eukaryotes, five main protein complexes are involved, whereas in prokaryotes many different enzymes are present, using a variety of electron donors and acceptors. The energy transferred by electrons flowing through this electron transport chain is used to transport protons across the inner mitochondrial membrane , in a process called ...

  9. DNA polymerase - Wikipedia

    en.wikipedia.org/wiki/DNA_polymerase

    Processivity is a characteristic of enzymes that function on polymeric substrates. In the case of DNA polymerase, the degree of processivity refers to the average number of nucleotides added each time the enzyme binds a template. The average DNA polymerase requires about one second locating and binding a primer/template junction.