H+-ATPase

• プロトンATPアーゼ

関

F0F1-ATPase、F1-ATPase、F1F0-ATPase、proton-translocating ATPase

• proton-translocating ATPase

WordNet

1. the 8th letter of the Roman alphabet (同)h

PrepTutorEJDIC

1. hydrogenの化学記号
2. 鉛筆の硬度 / 《俗》heroin

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2017/12/22 21:27:41」(JST)

wiki en

[Wiki en表示]

In the field of enzymology, a proton ATPase is an enzyme that catalyzes the following chemical reaction:

ATP + H
2O + H+
_in $\rightleftharpoons$ ADP + phosphate + H+
_out

The 3 substrates of this enzyme are ATP, H
2O, and H+
, whereas its 3 products are ADP, phosphate, and H+
.

Proton ATPases are divided into three groups as outlined below:

P-type proton ATPase

P-type ATPases form a covalent phosphorylated (hence the symbol ’P') intermediate as part of its reaction cycle. P-type ATPases undergo major conformational changes during the catalytic cycle. P-type ATPases are not evolutionary related to V- and F-type ATPases.

Plasma membrane H⁺-ATPase

Main article: Plasma membrane H+-ATPase

P-type proton ATPase (or plasma membrane H+
-ATPase) is found in the plasma membranes of eubacteria, archaea, protozoa, fungi and plants. Here it serves as a functional equivalent to the Na⁺/K⁺ ATPase of animal cells; i.e. it energizes the plasma membrane by forming an electrochemical gradient of protons (Na⁺ in animal cells), that in turn drives secondary active transport processes across the membrane. The plasma membrane H⁺-ATPase is a P3A ATPase with a single polypeptide of 70-100 kDa.

Gastric H⁺/K⁺ ATPase

Main article: Hydrogen potassium ATPase

Animals have a gastric hydrogen potassium ATPase or H⁺/K⁺ ATPase that belongs to the P-type ATPase family and functions as an electroneutral proton pump. This pump is found in the plasma membrane of cells in the gastric mucosa and functions to acidify the stomach. This enzyme is a P2C ATPase, characterized by having an supporting beta-subunit, and is closely related to the Na⁺/K⁺ ATPase.

V-type proton ATPase

Main article: V-ATPase

V-type proton ATPase (or V-ATPase) translocate protons into intracellular organelles other than mitochondria and chloroplasts, but in certain cell types they are also found in the plasma membrane. V-type ATPases acidify the lumen of the vacuole (hence the symbol 'V') of fungi and plants, and that of the lysosome in animal cells. Furthermore, they are found in endosomes, clathrin coated vesicles, hormone storage granules, secretory granules, Golgi vesicles and in the plasma membrane of a variety of animal cells. Like F-type ATPases, V-type ATPases are composed of multiple subunits and carry out rotary catalysis. The reaction cycle involves tight binding of ATP but proceeds without formation of a covalent phosphorylated intermediate. V-type ATPases are evolutionary related to F-type ATPases.

F-type proton ATPase

Main article: F-ATPase

F-type proton ATPase (or F-ATPase) typically operates as an ATP synthase that dissipates a proton gradient rather than generating one; i.e. protons flow in the reverse direction compared to V-type ATPases. In eubacteria, F-type ATPases are found in plasma membranes. In eukaryotes, they are found in the mitochondrial innner membranes and in chloroplast thylakoid membranes. Like V-type ATPases, F-type ATPases are composed of multiple subunits and carry out rotary catalysis. The reaction cycle involves tight binding of ATP but proceeds without formation of a covalent phosphorylated intermediate. F-type ATPases are evolutionary related to V-type ATPases.

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English Journal

• The multidrug transporter MATE1 sequesters OCs within an intracellular compartment that has no influence on OC secretion in renal proximal tubules.

• Martínez-Guerrero LJ1, Evans KK1, Dantzler WH1, Wright SH2.
• American journal of physiology. Renal physiology.Am J Physiol Renal Physiol.2016 Jan 1;310(1):F57-67. doi: 10.1152/ajprenal.00318.2015. Epub 2015 Nov 4.
• Secretion of organic cations (OCs) across renal proximal tubules (RPTs) involves basolateral OC transporter (OCT)2-mediated uptake from the blood followed by apical multidrug and toxin extruder (MATE)1/2-mediated efflux into the tubule filtrate. Whereas OCT2 supports electrogenic OC uniport, MATE is
• PMID 26538438

• An emerging role for gasotransmitters in the control of breathing and ionic regulation in fish.

• Perry S1, Kumai Y2, Porteus CS2,3, Tzaneva V2, Kwong RW2.
• Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology.J Comp Physiol B.2015 Dec 11. [Epub ahead of print]
• Three gases comprising nitric oxide, carbon monoxide and hydrogen sulphide, collectively are termed gasotransmitters. The gasotransmitters control several physiological functions in fish by acting as intracellular signaling molecules. Hydrogen sulphide, first implicated in vasomotor control in fish,
• PMID 26660653

• miR156 modulates rhizosphere acidification in response to phosphate limitation in Arabidopsis.

• Lei KJ1,2, Lin YM1, An GY3.
• Journal of plant research.J Plant Res.2015 Dec 11. [Epub ahead of print]
• Rhizosphere acidification is a general response to Pi deficiency, especially in dicotyledonous plants. However, the signaling pathway underlying this process is still unclear. Here, we demonstrate that miR156 is induced in the shoots and roots of wild type Arabidopsis plants during Pi starvation. Th
• PMID 26659856

Japanese Journal

• Screening and analysis of rhizosphere acidification deficiency mutants in Arabidopsis thaliana under low phosphorus(Plant nutrition)

• Soil science and plant nutrition 61(3), 493-500, 2015-06
• NAID 110010031457

• Suture materials affect peri-implant bone healing and implant osseointegration

• Journal of Oral Science 57(3), 219-227, 2015
• NAID 130005099737

• P-22 病原真菌Candida glabrataのvacuolar H^+-ATPaseが酸化ストレス応答に及ぼす影響(基礎-2,一般演題(ポスター),基本を見直す)

• 日本医真菌学会総会プログラム抄録集 55(Supplement_1), 101, 2014-10
• NAID 110009897577

Related Links

• The Plasma Membrane H+-ATPase' - Plant Physiology

Plant Physiol. (1995) 108: 1-6. The Plasma Membrane H+-ATPase'. A Highly Regulated Enzyme with Multiple Physiological Functions. Baudouin Michelet and Marc Boutry*. Unité de Biochimie Physiologique, Université Catholique de Louvain ...

• V-ATPase - Wikipedia, the free encyclopedia

Vacuolar-type H+ -ATPase (V-ATPase) is a highly conserved evolutionarily ancient enzyme with remarkably diverse functions in eukaryotic organisms. V- ATPases acidify a wide array of intracellular organelles and pump protons across the ...

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「vacuolar H+-ATPase」

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• 液胞型プロトンATPアーゼ、液胞型プロトンATPase、液胞型プロトン・ンプ

関

V-ATPase、V-type ATPase、vacuolar ATPase、vacuolar proton-translocating ATPase

• vacuolar ATPase

「plasma membrane H+-ATPase」

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細胞膜プロトンATPアーゼ、細胞膜プロトンポンプ、形質膜プロトンポンプ、原形質膜プロトンポンプ

「H」

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• 食道裂孔
• ヒスチジン
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「ATPase」

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同

ATP hydrolase

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アデノシン三リン酸