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Literature summary for 5.6.2.3 extracted from

  • LeBowitz, J.H.; McMacken, R.
    The Escherichia coli dnaB replication protein is a DNA helicase (1986), J. Biol. Chem., 261, 4738-4748 .
    View publication on PubMed
Search for more literature for 5.6.2.3

Inhibitors

Inhibitors Comment Organism Structure
additional information the enzyme is inhibited by prior coating of the single-stranded regions of the helicase substrate with the Escherichia coli single-stranded DNA-binding protein Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required. No detectable helicase activity is found in the absence of Mg2+ Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
duplex DNA the dnaB protein unwinds the DNA in a reaction that requires hydrolysis of a ribonucleoside triphosphate. The dnaB protein moves 5' to 3' along the strand to which it is bound. A preformed fork is required for the protein to invade and unwind duplex DNA Escherichia coli ?
-
 ?

Synonyms

Synonyms Comment Organism
dnaB replication protein
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP best cofactor Escherichia coli
CTP CTP is somewhat less active as cofactor compared to ATP Escherichia coli
GTP GTP is somewhat less active as cofactor compared to ATP Escherichia coli
additional information the nonhydrolyzable ATP analogue App(NH)p is not capable of serving as a nucleotide cofactor for DNA unwinding Escherichia coli
UTP UTP is significantly less active than ATP Escherichia coli

General Information

General Information Comment Organism
physiological function the dnaB protein is the primary replicative helicase of Escherichia coli and actively and processively migrates along the lagging strand template, serving both to unwind the DNA duplex in advance of the leading strand and to potentiate synthesis by the bacterial primase of RNA primers for the nascent (Okazaki) fragments of the lagging strand Escherichia coli