The power of vanadate in crystallographic investigations of phosphoryl transfer enzymes

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

Metavanadate at the active site of the phosphatase VHZ.

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

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



Crystal structure of bovine low molecular weight phosphotyrosyl phosphatase complexed with the transition state analog vanadate.

Two studies are consistent with the conclusion that vanadate inhibits tyrosine phosphatases by acting as a transition state analog, and the structure of theVanadate complex may be expected to closely resemble the transition state for reactions catalyzed by protein tyrosining phosphatase enzymes.

Pentavalent Organo-Vanadates as Transition State Analogues for Phosphoryl Transfer Reactions.

Uridine 2',3'-cyclic vanadate is tested as a transition state analogue for RNase A, but only a marginal one, indicating that a pentavalent organo-vanadate cannot necessarily be the basis for a rigorous analysis of the transition state for a phosphoryl transfer reaction.

Is the PTPase-vanadate complex a true transition state analogue?

Vanadate is not a true transition state analogue for the PTPase reactions, and the complex would resemble an associative transition state, contrary to the previously determined dissociative structure of the transition state.

Inhibition of phosphate-metabolizing enzymes by oxovanadium(V) complexes.

Detailed studies ofVanadate-initiated inhibition of enzymes will expand the understanding of the various mechanisms of action of vanadate and its derivatives that have been briefly described here and will doubtless provide insight into other functions of this unique material.

The Pentacovalent Phosphorus Intermediate of a Phosphoryl Transfer Reaction

The atomic-resolution structure of a high-energy reaction intermediate stabilized in the active site of an enzyme is reported, revealing a stabilized pentacovalent phosphorane formed in the phosphoryl transfer from the C(1)O of glucose 1,6-(bis)phosphate to the nucleophilic Asp8 carboxylate.

A Model of the Transition State in the Alkaline Phosphatase Reaction*

This structural complex supports the in-line displacement mechanism of phosphomonoester hydrolysis by alkaline phosphatase and provides a model for the proposed transition state in the enzyme-catalyzed reaction.

X-ray structure of a vanadium-containing enzyme: chloroperoxidase from the fungus Curvularia inaequalis.

An amino acid sequence comparison with vanadium-containing bromoperoxidase from the seaweed Ascophyllum nodosum shows high similarities in the regions of the metal binding site, with all hydrogen vanadate(V) interacting residues conserved except for lysine-353, which is an asparagine.

The X-ray Crystal Structures of Yersinia Tyrosine Phosphatase with Bound Tungstate and Nitrate

X-ray crystal structures of the Yersinia tyrosine phosphatase in complex with tungstate and nitrate have been solved to 2.4-Å resolution and are consistent with a general acid-catalyzed, in-line displacement of the phosphate moiety to Cys403 on the enzyme, followed by attack by a nucleophilic water molecule to release orthophosphate.

Models for biological phosphoryl transfer.

Structure (1.3 Å) and Charge States of a Ribonuclease A−Uridine Vanadate Complex: Implications for the Phosphate Ester Hydrolysis Mechanism

A joint X-ray crystallographic (1.3 A resolution) and ab initio quantum mechanical analysis of a uridine vanadate−ribonuclease A complex (UV−RNase A) is undertaken to probe specific aspects of the