Proton-pumping pyrophosphatase

Last updated
Inorganic H+ pyrophosphatase
Identifiers
Symbol H_PPase
Pfam PF03030
InterPro IPR004131
TCDB 3.A.10
OPM superfamily 390
OPM protein 4a01

Two types of inorganic diphosphatase, very different in terms of both amino acid sequence and structure, have been characterised to date: soluble and transmembrane proton-pumping pyrophosphatases (sPPases and H(+)-PPases, respectively). sPPases are ubiquitous proteins that hydrolyse pyrophosphate to release heat, whereas H+-PPases, so far unidentified in animal and fungal cells, couple the energy of PPi hydrolysis to proton movement across biological membranes. [1] [2] The latter type is represented by this group of proteins. H+-PPases are also called vacuolar-type inorganic pyrophosphatases (V-PPase) or pyrophosphate-energised vacuolar membrane proton pumps. [3] In plants, vacuoles contain two enzymes for acidifying the interior of the vacuole, the V-ATPase and the V-PPase (V is for vacuolar). [2]

Inorganic diphosphatase

In enzymology, an inorganic diphosphatase (EC 3.6.1.1) is an enzyme that catalyzes the chemical reaction

Protein biological molecule consisting of chains of amino acid residues

Proteins are large biomolecules, or macromolecules, consisting of one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific three-dimensional structure that determines its activity.

Pyrophosphate salt or ester of diphosphoric acid

In chemistry, a pyrophosphate are phosphorus oxyanions that contain a P-O-P linkage. A number of pyrophosphate salts exist, such as Na2H2P2O7, as well as the normal pyrophosphates. Often pyrophosphates are called diphosphates. The parent pyrophosphates are derived from partial or complete neutralization of pyrophosphoric acid. Important salts are disodium pyrophosphate and tetrasodium pyrophosphate. The pyrophosphate bond, as found in ATP, is very important in biochemistry.

Two distinct biochemical subclasses of H+-PPases have been characterised to date: K +-stimulated and K+-insensitive. [1] [3]

Biochemistry study of chemical processes in living organisms

Biochemistry, sometimes called biological chemistry, is the study of chemical processes within and relating to living organisms. Biochemical processes give rise to the complexity of life.

Potassium Chemical element with atomic number 19

Potassium is a chemical element with symbol K and atomic number 19. Potassium is a silvery-white metal that is soft enough to be cut with a knife, with little force. Potassium metal reacts rapidly with atmospheric oxygen to form flaky white potassium peroxide in only seconds of exposure. It was first isolated from potash, the ashes of plants, from which its name derives. In the periodic table, potassium is one of the alkali metals, all of which have a single outer-shell valence electron that is easily removed to create an ion with a positive charge, a cation, that combines with anions to form salts. Potassium in nature occurs only in ionic salts. Elemental potassium reacts vigorously with water, generating sufficient heat to ignite hydrogen emitted in the reaction, and burning with a lilac-colored flame. It is found dissolved in sea water, and occurs in many minerals such as orthoclase, a common constituent of granites and other igneous rocks.

Related Research Articles

A proton pump is an integral membrane protein that builds up a proton gradient across a biological membrane. Proton pumps catalyze the following reaction:

Inorganic pyrophosphatase

Pyrophosphatase is an enzyme that catalyzes the conversion of one molecule of pyrophosphate to two phosphate ions. This is a highly exergonic reaction, and therefore can be coupled to unfavorable biochemical transformations in order to drive these transformations to completion. The functionality of this enzyme plays a critical role in lipid metabolism, calcium absorption and bone formation, and DNA synthesis, as well as other biochemical transformations.

ATP synthase subunit C

ATPase, subunit C of Fo/Vo complex is the main transmembrane subunit of V-type, A-type and F-type ATP synthases.

ATP6V1E1 protein-coding gene in the species Homo sapiens

V-type proton ATPase subunit E 1 is an enzyme that in humans is encoded by the ATP6V1E1 gene.

ATP6V0C protein-coding gene in the species Homo sapiens

V-type proton ATPase 16 kDa proteolipid subunit is an enzyme that in humans is encoded by the ATP6V0C gene.

ATP6V1B2 protein-coding gene in the species Homo sapiens

V-type proton ATPase subunit B, brain isoform is an enzyme that in humans is encoded by the ATP6V1B2 gene.

ATP6V0A4 protein-coding gene in the species Homo sapiens

V-type proton ATPase 116 kDa subunit a isoform 4 is an enzyme that in humans is encoded by the ATP6V0A4 gene.

ATP6V1C1 protein-coding gene in the species Homo sapiens

V-type proton ATPase subunit C 1 is an enzyme that in humans is encoded by the ATP6V1C1 gene.

ATPase, H+ transporting, lysosomal V0 subunit a1 protein-coding gene in the species Homo sapiens

V-type proton ATPase 116 kDa subunit a isoform 1 is an enzyme that in humans is encoded by the ATP6V0A1 gene.

ATP6V1A protein-coding gene in the species Homo sapiens

V-type proton ATPase catalytic subunit A is an enzyme that in humans is encoded by the ATP6V1A gene.

ATP6V0D1 protein-coding gene in the species Homo sapiens

V-type proton ATPase subunit d 1 is an enzyme that in humans is encoded by the ATP6V0D1 gene.

ATP6V1G2 Protein-coding gene in Homo sapiens

V-type proton ATPase subunit G 2 is an enzyme that in humans is encoded by the ATP6V1G2 gene.

ATP6V1G1 protein-coding gene in the species Homo sapiens

V-type proton ATPase subunit G 1 is an enzyme that in humans is encoded by the ATP6V1G1 gene.

ATP6V1D protein-coding gene in the species Homo sapiens

V-type proton ATPase subunit D is an enzyme that in humans is encoded by the ATP6V1D gene.

ATP6V1G3 protein-coding gene in the species Homo sapiens

V-type proton ATPase subunit G 3 is an enzyme that in humans is encoded by the ATP6V1G3 gene.

ATP6V0B Protein-coding gene in Homo sapiens

V-type proton ATPase 21 kDa proteolipid subunit is an enzyme that in humans is encoded by the ATP6V0B gene.

ATP6V0E1 protein-coding gene in the species Homo sapiens

V-type proton ATPase subunit e 1 is an enzyme that in humans is encoded by the ATP6V0E1 gene.

ATP6V1E2 protein-coding gene in the species Homo sapiens

V-type proton ATPase subunit E 2 is an enzyme that in humans is encoded by the ATP6V1E2 gene.

Members of the H+, Na+-translocating Pyrophosphatase (M+-PPase) Family (TC# 3.A.10) are found in the vacuolar (tonoplast) membranes of higher plants, algae, and protozoa, and in both bacteria and archaea. They are therefore ancient enzymes.

References

  1. 1 2 Perez-Castineira JR, Lopez-Marques RL, Villalba JM, Losada M, Serrano A (December 2002). "Functional complementation of yeast cytosolic pyrophosphatase by bacterial and plant H+-translocating pyrophosphatases". Proc. Natl. Acad. Sci. U.S.A. 99 (25): 15914–9. doi:10.1073/pnas.242625399. hdl:11441/26079. PMC   138539 . PMID   12451180.
  2. 1 2 Baltscheffsky M, Schultz A, Baltscheffsky H (September 1999). "H+ -PPases: a tightly membrane-bound family". FEBS Lett. 457 (3): 527–33. doi:10.1016/S0014-5793(99)90617-8. PMID   10523139.
  3. 1 2 Perez-Castineira JR, Lopez-Marques RL, Losada M, Serrano A (May 2001). "A thermostable K(+)-stimulated vacuolar-type pyrophosphatase from the hyperthermophilic bacterium Thermotoga maritima". FEBS Lett. 496 (1): 6–11. doi:10.1016/S0014-5793(01)02390-0. PMID   11343697.
This article incorporates text from the public domain Pfam and InterPro: IPR004131