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ATP5O — CSN3
Text-mined interactions from Literome
Tek et al., Protein Sci 2002
:
Consistently, addition of the separated N-terminal domain does not reverse an inhibition of
ATPase activity of ClpBDeltaN in the
presence of
casein
Liu et al., J Mol Biol 2002
:
We observed, however, that three mutations, T7A, D103A, and E109A, reduced the
casein induced
activation of the ClpB
ATPase
Beinker et al., J Biol Chem 2002
:
In contrast casein binding and
stimulation of the
ATPase activity by
kappa-casein were affected
Yamada-Inagawa et al., J Biol Chem 2003
:
The
ATPase activity of the mutants was no longer
stimulated by
casein , whereas that of the three Phe228 mutants, but not the G230A mutant, remained sigma32-stimulatable
Vineyard et al., Biochemistry 2006
:
As the model peptide substrate [ S2 ; YRGITCSGRQK ( Bz ) ] [ Thomas-Wohlever, J., and Lee, I. ( 2002 ) Biochemistry 41, 9418-9425 ] or the protein substrate
casein affects only the steady-state
ATPase activity of the low-affinity sites, we propose that Lon adopts a different form after its first turnover as an ATP dependent protease
Mizuno et al., FEBS J 2012
:
However, the extent of
casein induced stimulation of
ATPase , the rate of substrate threading and the efficiency of protein disaggregation of these mutants were all lower than those of the wild-type but similar to those of ClpBdN
Park et al., J Biol Chem 1993
:
Furthermore, ClpB79 is capable of inhibiting the
casein activated
ATPase activity of ClpB93 in a dose dependent manner but without any effect on its inherent ATPase activity
Seol et al., Biol Chem 1997
:
Furthermore, in the presence of NEM,
casein could
stimulate the
ATPase activities of ClpA/C47S and ClpA/C47A and protect from their degradation by ClpP, but not of the other ClpA proteins
Roudiak et al., Biochemistry 1998
:
By contrast, N-G91 and N-E226 retained basal
ATPase activities, but these activities were only
stimulated weakly by
alpha-casein