Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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.
    View publication on PubMedView publication on EuropePMC

Activating Compound

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

Protein Variants

EC Number Protein Variants Comment Organism
5.6.2.4 C261A mutant with a disrupted zinc-binding site. One mol of the C261A mutant contains 0.03 atoms Bacillus cereus
5.6.2.4 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

EC Number Metals/Ions Comment Organism Structure
5.6.2.4 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

EC Number Organism UniProt Comment Textmining
5.6.2.4 Bacillus cereus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.6.2.4 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

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

Synonyms

EC Number Synonyms Comment Organism
5.6.2.4 BcMCM
-
 Bacillus cereus