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1997 Ma & Taylor JBC p717, kinetics of monomeric construct by Mind Map: 1997 Ma & Taylor JBC p717, kinetics of monomeric construct
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1997 Ma & Taylor JBC p717, kinetics of monomeric construct

Kinesin type

Human kinesin construct K332

expressed in E. coli, not sure how purified

Cited by me in

2011 Larry Kinetic Modeling Paper

Rates

MONOMERIC, unbound empty, bind ATP

MONOMERIC, unbound empty, bind ADP

MONOMERIC bound ATP hydrolysis 200/s

MONOMERIC bound ATP, release ATP

MONOMERIC bound ADP head unbinding 80/s (+/- 10/s) (kdis)

MONOMERIC bound ADP, release ADP 150 /s or 200 /s

MONOMERIC bound ADP-P, phosphate release

Monomeric Vmax 60 /s

Assay conditions

Temperature 20C

Otherwise methods seem to be described in Ma and Taylor 1995 Biochemistry 34 13233 and 13242

Citation

Ma, Y. Z., & Taylor, E. W. (1997). Kinetic Mechanism of a Monomeric Kinesin Construct. Journal of Biological Chemistry, 272(2), 717-723. doi:10.1074/jbc.272.2.717

Interesting

The nucleotide-free K332 was more stable than K379 which tends to aggregate with loss of binding activity

My assessment

A lot of these rate constants should be looked at as a reference for zero-force rate constants (i.e. one-head bound) of the dimeric construct. However, there are some caveats

companion paper

Ma & Taylor JBC 1997 p 724