Literature summary for 5.6.2.4 extracted from

Samuels, M.; Gulati, G.; Shin, J.H.; Opara, R.; McSweeney, E.; Sekedat, M.; Long, S.; Kelman, Z.; Jeruzalmi, D.
A biochemically active MCM-like helicase in Bacillus cereus (2009), Nucleic Acids Res., 37, 4441-4452.

Search for more literature for 5.6.2.4

Activating Compound

Activating Compound	Comment	Organism	Structure
single-stranded DNA	stimulates activity	Bacillus cereus

Protein Variants

Protein Variants	Comment	Organism
C261A	mutant with a disrupted zinc-binding site. One mol of the C261A mutant contains 0.03 atoms	Bacillus cereus
K653A	mutation of the ATP-binding site reduces activity to about 30% of wild-type. This drop in ATPase activity corresponds to an abrogation of helicase activity observed in the same mutant	Bacillus cereus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	BcMCM amino-terminus can bind single-stranded DNA and harbors a zinc atom, BcMCM contains 0.11 zinc atoms per mole	Bacillus cereus

Organism

Organism	UniProt	Comment	Textmining
Bacillus cereus	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + H2O	BcMCM displays 3' to 5' helicase and ssDNA-stimulated ATPase activity. BcMCM is an active ATPase, and this activity is restricted to the MCM-AAA module	Bacillus cereus	ADP + phosphate	-	?

Subunits

Subunits	Comment	Organism
monomer	BcMCM is a monomer in solution but likely forms the functional oligomer in vivo	Bacillus cereus

Synonyms

Synonyms	Comment	Organism
BcMCM	-	Bacillus cereus

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)