H+‐PPases: a tightly membrane‐bound family

@article{Baltscheffsky1999HPPasesAT,
  title={H+‐PPases: a tightly membrane‐bound family},
  author={Margareta Baltscheffsky and Anders Schultz and Herrick Baltscheffsky},
  journal={FEBS Letters},
  year={1999},
  volume={457}
}
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129 Citations
Highly Influential Citations
8
Background Citations
44
Methods Citations
4
Results Citations
1

129 Citations

Vacuolar H(+)-pyrophosphatase.

  • M. Maeshima
  • Biology, Chemistry
    Biochimica et biophysica acta
  • 2000

Proton/sodium pumping pyrophosphatases: the last of the primary ion pumps.

Plant proton pumping pyrophosphatase: the potential for its pyrophosphate synthesis activity to modulate plant growth.

This work proposes a model where the PPi synthase activity of H+ -PPases maintains thePPi pool when cells adopt PPi-dependent glycolysis during high energy demands and/or low oxygen environments.

A thermostable K+‐stimulated vacuolar‐type pyrophosphatase from the hyperthermophilic bacterium Thermotoga maritima

Pyrophosphate-Fueled Na+ and H+ Transport in Prokaryotes

The determination of the three-dimensional structures of H+- and Na+-pyrophosphatases has been another recent breakthrough in the studies of these cation pumps.

Identification of Essential Lysines Involved in Substrate Binding of Vacuolar H+-Pyrophosphatase*

Proteolytic evidence demonstrated that Lys-250 is the primary target of trypsin and confirmed its crucial role in H+-PPase hydrolysis, and functional roles of these lysines were examined.

Bioinformatics Insights on Plant Vacuolar Proton Pyrophosphatase: A Proton Pump Involved in Salt Tolerance

This chapter provides an overview on bioinformatics approaches used to understand the 3D structure, motifs, function, and working model of VPPases.

Functional roles of arginine residues in mung bean vacuolar H+-pyrophosphatase.

Membrane-Bound Pyrophosphatases

A concise summary of the current structural and functional understanding of M-PPases is given, with an emphasis on describing the role of the metal ions in the enzymatic function of these proteins.

Elucidating the Role of Conserved Glutamates in H+-pyrophosphatase of Rhodospirillum rubrum*

Substitution of Glu197, Glu202, and Glu649 resulted in decreased binding affinity for the substrate analogues aminomethylenediph phosphonate and methylenediphosphonate, indicating that these residues are involved in substrate binding as ligands for bridging metal ions.
...

References

SHOWING 1-10 OF 59 REFERENCES

Vacuolar H(+)-translocating pyrophosphatases: a new category of ion translocase.

Isolation and Characterization of cDNAs Encoding the Vacuolar H+-Pyrophosphatase of Beta vulgaris

Two cDNA species isolated from Beta are concluded to encode variants, possibly isoforms, of the enzyme, and the recent demonstration of the sufficiency of the substrate-binding polypeptide, alone, for all of the known catalytic functions of the V-PPase is demonstrated.

Molecular cloning of cDNA for vacuolar membrane proton-translocating inorganic pyrophosphatase in Hordeum vulgare.

A cDNA clone for the vacuolar membrane proton-translocating inorganic pyrophosphatase from barley roots was obtained by immunoscreening and the deduced amino acid sequence revealed 85.8% homology.

Reconstitution of highly purified proton‐translocating pyrophosphatase from Rhodospirillum rubrum

Reversibility of H+-ATPase and H+-Pyrophosphatase in Tonoplast Vesicles from Maize Coleoptiles and Seeds

Comparison of the two H + pumps showed that the H + -ATPase was more active than H -PPase in coleoptile tonoplast vesicles, whereas in seed vesicle activity was clearly dominant, which may reflect the physiological significance of these enzymes in different tissues at different stages of development and/or differentiation.

Molecular cloning and sequence of cDNA encoding the pyrophosphate-energized vacuolar membrane proton pump of Arabidopsis thaliana.

The cloning and sequence of cDNAs encoding the tonoplast H(+)-PPase of Arabidopsis thaliana are reported, and it is suggested that the H( +)- PPase has been cloned in its entirety.

Oligomeric structure of H(+)-translocating inorganic pyrophosphatase of plant vacuoles.

  • M. Maeshima
  • Biology
    Biochemical and biophysical research communications
  • 1990

Heterologous expression of plant vacuolar pyrophosphatase in yeast demonstrates sufficiency of the substrate-binding subunit for proton transport.

Heterologous expression of the cDNA (AVP) encoding the substrate-binding subunit of the vacuolar H(+)-pyrophosphatase from the vascular plant Arabidopsis thaliana in the yeast Saccharomyces cerevisiae results in the production of vacu polarly localized functional enzyme active in PPi-dependent H+ translocation.

A vacuolar H+-pyrophosphatase in Acetabularia acetabulum: molecular cloning and comparison with higher plants and a bacterium

The primary structure of the H+-PPase from total RNA using reverse-transcription and PCR tech- was compared with the enzymes in higher plants and in the niques andignments of the primary structure to that of similar photosynthetic bacterium, R. rubrum were revealed.

Chromatographic resolution of h-translocating pyrophosphatase from h-translocating ATPase of higher plant tonoplast.

Membrane vesicles derived from the tonoplast of Beta vulgaris L. possess two predominant phosphohydrolase activities: a Cl(-)-stimulated, NO(3) (-)-inhibited ATPase, and a K(+)-stimulated,…
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