CoChat
Sign Up
Cited by 98Microtubule and mitosis dynamicsATP Synthase and ATPases ResearchProtein Structure and Dynamics

Mechanism of Microtubule Kinesin ATPase

Ma, Y. Z., Taylor, Edwin W.·1995·Biochemistry
DOI 10.1021/bi00040a040
Open this paper in CoChat — free account

Abstract

A six-step mechanism is derived for the activation of kinesin K379 ATPase by microtubules. The data are fitted by the kinetic scheme [Formula see text] where T, D, and P refer to nucleotide triphosphate, nucleotide diphosphate, and inorganic phosphate, respectively; MtK refers to the complex of a K379 unit with the microtubule binding site. The initial binding and release steps, 1 and 6, are treated as rapid equilibria: k2 = 200 s-1, k3 = 100 s-1, k5 = 35-40 s-1, maximum steady-state rate = 25 s-1 (50 mM NaCl, 20 degrees C). k2 was obtained from the maximum rate of fluorescence enhancement with mant-ATP as substrate, k3 was obtained from the hydrolysis transient phase for ATP or mant-ATP, and k5 was obtained from the rate of decrease in fluorescence of mant-ADP in the reaction [Formula see text]. A large excess of ATP was present with the Mt to block rebinding of mant-ADP. The rate was measured as a function of microtubule concentration and extrapolated to give the maximum rate k5. The same method was used to obtain k5 for ADP by mixing K.ADP with microtubules plus excess mant-ATP. The enhancement of fluorescence for the binding of mant-ATP is followed by a decrease in fluorescence with a rate constant of 35-40 s-1. Since the decrease must occur after hydrolysis, it may be correlated with a step or steps leading to the low fluorescence MtK.D state. In the kinetic scheme, steps 4 and 5 both contribute to determining the maximum turnover rate. At higher ionic strengths or lower…

Integrity signals

Registry

Crossref · 10.1021/bi00040a040

Cites

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • ADP dissociates wild-type kinesin from the microtubule at a rate of ∼12 s−1.

    “ADP dissociates wild-type kinesin from the microtubule at a rate of ∼12 s−1 (17”

    From Stepping and Stretching (2003) · cites this paper as [31]

Cited by

Sorted by citations

Authors
Ma, Y. Z., & Taylor, E. W.
Affiliations
University of Chicago (US)
ORCID
Taylor, Edwin W.
Venue
Biochemistry
Publisher
American Chemical Society (ACS)
Published
1995-10-10
Volume
34
Issue
40
Pages
13242-13251
ISSN
  • 0006-2960 (ISSN-L)
  • 1520-4995
DOI
10.1021/bi00040a040
OpenAlex
W1990692957
Cited by
98
References
0
Citations by year
2025: 2 · 2022: 2 · 2021: 1 · 2020: 1 · 2019: 1 · 2017: 1 · 2016: 2 · 2015: 2 · 2014: 4 · 2013: 3 · 2012: 4
FWCI
3.23
Type
journal article
Language
en
Open access
closed
Locations
  • Biochemistry (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • National Institutes of Health (5p01hl020592-23)
  • National Heart, Lung, and Blood Institute (HL 20592)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords
kinesin, microtubule binding, ATP hydrolysis, enzyme kinetics, kinetic mechanism, dissociation constant, enzyme dimer
MeSH terms
Adenosine Diphosphate, Adenosine Triphosphate, Animals, Brain, Enzyme Activation, Humans, Kinetics, Microtubules, Osmolar Concentration, Peptide Fragments, Phosphates, Recombinant Proteins, Swine, Kinesins, In Vitro Techniques

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review