The power of vanadate in crystallographic investigations of phosphoryl transfer enzymes

@article{Davies2004ThePO,
  title={The power of vanadate in crystallographic investigations of phosphoryl transfer enzymes},
  author={Douglas R. Davies and Wim G. J. Hol},
  journal={FEBS Letters},
  year={2004},
  volume={577}
}

Metavanadate at the active site of the phosphatase VHZ.

TLDR
A mechanism is proposed to explain the formation of metavanadate in the active site from a dimeric vanadate species that previous crystallographic evidence has shown to be able to bind to the active sites of phosphatases related to VHZ, and the results show that the interaction ofVanadate with biological systems is not solely reliant upon the prior formation of a particular inhibitory form in solution.

Shared traits on the reaction coordinates of ribonuclease and an RNA enzyme.

The catalytic scaffold of the haloalkanoic acid dehalogenase enzyme superfamily acts as a mold for the trigonal bipyramidal transition state

TLDR
It is proposed that core residues in the large enzyme family, the haloalkanoic acid dehalogenase enzyme superfamily (HADSF) form a “mold” in which the trigonal bipyramidal transition states formed during phosphoryl transfer are stabilized by electrostatic forces.

Tungstate as a Transition State Analog for Catalysis by Alkaline Phosphatase.

Crystal Structure of the Vanadate-Inhibited Ca(2+)-ATPase.

Trigonal Bipyramidal or Square Pyramidal Coordination Geometry? Investigating the Most Potent Geometry for Vanadium Phosphatase Inhibitors

The five-coordinate geometry is an important factor in phosphoryl group transfer, particularly for phosphate ester hydrolysis. In the following review we analyze the five-coordinate geometries for a
...

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TLDR
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TLDR
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TLDR
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