منابع مشابه
Kinesin ATPase: rate-limiting ADP release.
The ATPase rate of kinesin isolated from bovine brain by the method of S.A. Kuznetsov and V.I. Gelfand [(1986) Proc. Natl. Acad. Sci. USA 83, 8530-8534)] is stimulated 1000-fold by interaction with tubulin (turnover rate per 120-kDa peptide increases from approximately equal to 0.009 sec-1 to 9 sec-1). The tubulin-stimulated reaction exhibits no extra incorporation of water-derived oxygens over...
متن کاملA Transition Path Ensemble Study Reveals a Linchpin Role for Mg2+ during Rate-Limiting ADP Release from Protein Kinase A†
Protein kinases are key regulators of diverse signaling networks critical for growth and development. Protein kinase A (PKA) is an important kinase prototype that phosphorylates protein targets at Ser and Thr residues by converting ATP to ADP. Mg(2+) ions play a crucial role in regulating phosphoryl transfer and can limit overall enzyme turnover by affecting ADP release. However, the mechanism ...
متن کاملProduct release is not the rate-limiting step during cytochalasin B-induced ATPase activity of monomeric actin.
Under conditions where cytochalasin B induces ATPase activity of monomeric actin (0.3 mM MgCl2, 1 mM EGTA, 30 microns cytochalasin B, 1 mM ATP) the rate constant of the exchange of actin-bound epsilon-ATP for free ATP is about 4-6 times faster than steady state ATPase activity. When a stoichiometric ATP-actin complex is extracted with PCA (single turnover experiment) the apparent rate constant ...
متن کاملATPase mechanism of Eg5 in the absence of microtubules: insight into microtubule activation and allosteric inhibition by monastrol.
The ATPase mechanism of kinesin superfamily members in the absence of microtubules remains largely uncharacterized. We have adopted a strategy to purify monomeric human Eg5 (HsKSP/Kinesin-5) in the nucleotide-free state (apoEg5) in order to perform a detailed transient state kinetic analysis. We have used steady-state and presteady-state kinetics to define the minimal ATPase mechanism for apoEg...
متن کاملKinesin-2 KIF3AB exhibits novel ATPase characteristics.
KIF3AB is an N-terminal processive kinesin-2 family member best known for its role in intraflagellar transport. There has been significant interest in KIF3AB in defining the key principles that underlie the processivity of KIF3AB in comparison with homodimeric processive kinesins. To define the ATPase mechanism and coordination of KIF3A and KIF3B stepping, a presteady-state kinetic analysis was...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1988
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.85.17.6314