The stereochemical course of phosphoric residue transfer during the myosin ATPase reaction

J Biol Chem. 1980 Sep 25;255(18):8629-32.

Abstract

When adenosine 5'-(3-thiotriphosphate), stereospecifically labeled in the gamma position with 18O, was hydrolyzed in the presence of myosin subfragment 1 in 17O-enriched water, the product inorganic [16O,17O,18O]thiophosphate was chiral. The configuration of this product showed that the hydrolysis proceeds with inversion at the transferred phosphoric residue. This result suggests a direct, in-line hydrolysis mechanism for the ATPase.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenosine Triphosphatases / metabolism*
  • Adenosine Triphosphate / analogs & derivatives
  • Animals
  • Isomerism
  • Isotope Labeling
  • Kinetics
  • Magnetic Resonance Spectroscopy
  • Molecular Conformation
  • Muscles / enzymology
  • Myosins / metabolism*
  • Oxygen Isotopes
  • Rabbits
  • Thionucleotides

Substances

  • Oxygen Isotopes
  • Thionucleotides
  • adenosine 5'-O-(3-thiotriphosphate)
  • Adenosine Triphosphate
  • Adenosine Triphosphatases
  • Myosins