Literature summary for 3.6.4.13 extracted from

Talavera, M.A.; Matthews, E.E.; Eliason, W.K.; Sagi, I.; Wang, J.; Henn, A.; De La Cruz, E.M.
Hydrodynamic characterization of the DEAD-box RNA helicase DbpA (2005), J. Mol. Biol., 355, 697-707.

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Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Escherichia coli

Reaction

Reaction	Comment	Organism	Reaction ID
ATP + H2O = ADP + phosphate	models: DbpA functions as an active monomer that possesses two distinct RNA binding sites, one in the helicase core domain and the other in the carboxyl-terminal domain that recognizes 23 S rRNA and interacts specifically with hairpin 92 of the peptidyl transferase center	Escherichia coli	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + H2O	-	Escherichia coli	ADP + phosphate	-	?

Subunits

Subunits	Comment	Organism
monomer	DbpA is monomeric in solution up to a concentration of 25 mM and over the temperature range of 4°C to 22°C	Escherichia coli

Synonyms

Synonyms	Comment	Organism
DbpA	-	Escherichia coli
DEAD-box RNA helicase	-	Escherichia coli

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Release 2023.1 (January 2023)