ホスホフルクトキナーゼ, phosphofructokinase, 6-phosphofructo-1-kinase
WordNet
- the 16th letter of the Roman alphabet (同)p
PrepTutorEJDIC
- parking
- phosphorusの化学記号
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/08/04 16:37:17」(JST)
[Wiki ja表示]
ホスホフルクトキナーゼ（Phosphofructokinase、PFK）は、フルクトース-6-リン酸に作用する酵素で、全部で2つのタイプがある。
- ホスホフルクトキナーゼ1(EC 2.7.1.11)…フルクトース-1,6-ビスリン酸に変換する。
- ホスホフルクトキナーゼ2(EC 2.7.1.105)…フルクトース-2,6-ビスリン酸に変換する。
関連項目
外部リンク
- MeSH Phosphofructokinases
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ホスホトランスフェラーゼ/キナーゼ (EC 2.7) |
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| 2.7.1 - OH アクセプター |
ヘキソ- - グルコ- - フルクト- - ガラクト- - ホスホフルクト- - チミジン - NAD+- - グリセロール- - パントテン酸- - メバロン酸- - ピルビン酸- - デオキシシチジン- - PFP - ジアシルグリセロール- - ブルトンチロシン - ホスホイノシチド-3 - スフィンゴシン
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| 2.7.2 - COOH アクセプター |
ホスホグリセリン酸 - アスパラギン酸
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| 2.7.3 - N アクセプター |
クレアチン
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| 2.7.4 - PO4 アクセプター |
ホスホメバロン酸 - アデニル酸 - ヌクレオシド二リン酸
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| 2.7.6 - P2O7トランスフェラーゼ |
リボース-リン酸ジホスホキナーゼ - チアミンピロホスホキナーゼ
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| 2.7.7 - ヌクレオチジル- |
インテグラーゼ - PNPアーゼ - ポリメラーゼ - RNアーゼ PH - UDP-グルコースピロホスホリラーゼ - ガラクトース-1-リン酸ウリジリルトランスフェラーゼ -ターミナルトランスフェラーゼ - RNAレプリカーゼ - リバーストランスクリプターゼ (テロメラーゼ) - トランスポザーゼ
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| 2.7.8 - 他のリン酸基 |
N-アセチルグルコサミン-1-リン酸トランスフェラーゼ
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| 2.7.10-11 - プロテイン |
チロシン - セリン/トレオニンプロテイン
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[Wiki en表示]
- "PFK" redirects here. PFK (Poulet Frit Kentucky) is also the name for KFC in Quebec. For the Polish hip-hop group, see Paktofonika.
| Phosphofructokinase |
| Identifiers |
| Symbol |
Ppfruckinase |
| Pfam |
PF00365 |
| InterPro |
IPR000023 |
| PROSITE |
PDOC00336 |
| Available protein structures: |
| Pfam |
structures |
| PDB |
RCSB PDB; PDBe; PDBj |
| PDBsum |
structure summary |
|
Phosphofructokinase is a kinase enzyme that phosphorylates fructose 6-phosphate in glycolysis.
The enzyme-catalysed transfer of a phosphoryl group from ATP is an important reaction in a wide variety of biological processes.[1] One enzyme that utilizes this reaction is phosphofructokinase (PFK), which catalyses the phosphorylation of fructose-6-phosphate to fructose-1,6- bisphosphate, a key regulatory step in the glycolytic pathway.[2][3] PFK exists as a homotetramer in bacteria and mammals (where each monomer possesses 2 similar domains) and as an octomer in yeast (where there are 4 alpha- (PFK1) and 4 beta-chains (PFK2), the latter, like the mammalian monomers, possessing 2 similar domains[3]). This protein may use the morpheein model of allosteric regulation.[4]
PFK is about 300 amino acids in length, and structural studies of the bacterial enzyme have shown it comprises two similar (alpha/beta) lobes: one involved in ATP binding and the other housing both the substrate-binding site and the allosteric site (a regulatory binding site distinct from the active site, but that affects enzyme activity). The identical tetramer subunits adopt 2 different conformations: in a 'closed' state, the bound magnesium ion bridges the phosphoryl groups of the enzyme products (ADP and fructose-1,6- bisphosphate); and in an 'open' state, the magnesium ion binds only the ADP,[5] as the 2 products are now further apart. These conformations are thought to be successive stages of a reaction pathway that requires subunit closure to bring the 2 molecules sufficiently close to react.[5]
Deficiency in PFK leads to glycogenosis type VII (Tarui's disease), an autosomal recessive disorder characterised by severe nausea, vomiting, muscle cramps and myoglobinuria in response to bursts of intense or vigorous exercise.[3] Sufferers are usually able to lead a reasonably ordinary life by learning to adjust activity levels.[3]
There are two types of the enzyme:
| Type |
Synonyms |
EC number |
Substrate |
Product |
Subunit genes |
| Phosphofructokinase 1 |
6-phosphofructokinase
phosphohexokinase |
EC 2.7.1.11 |
Fructose 6-phosphate |
Fructose-1,6-bisphosphate |
PFKL, PFKM, PFKP |
| Phosphofructokinase 2 |
6-phosphofructo-2-kinase |
EC 2.7.1.105 |
Fructose-2,6-bisphosphate |
PFKFB1, PFKFB2, PFKFB3, PFKFB4 |
See also
- Phosphofructokinase deficiency
References
- ^ Evans PR, Hellinga HW (1987). "Mutations in the active site of Escherichia coli phosphofructokinase". Nature 327 (6121): 437–439. doi:10.1038/327437a0. PMID 2953977.
- ^ Wegener G, Krause U (2002). "Different modes of activating phosphofructokinase, a key regulatory enzyme of glycolysis, in working vertebrate muscle". Biochem. Soc. Trans. 30 (2): 264–270. doi:10.1042/bst0300264. PMID 12023862.
- ^ a b c d Raben N, Exelbert R, Spiegel R, Sherman JB, Nakajima H, Plotz P, Heinisch J (1995). "Functional expression of human mutant phosphofructokinase in yeast: genetic defects in French Canadian and Swiss patients with phosphofructokinase deficiency". Am. J. Hum. Genet. 56 (1): 131–141. PMC 1801305. PMID 7825568.
- ^ T. Selwood and E. K. Jaffe. (2011). "Dynamic dissociating homo-oligomers and the control of protein function.". Arch. Biochem. Biophys. 519 (2): 131–43. doi:10.1016/j.abb.2011.11.020. PMC 3298769. PMID 22182754.
- ^ a b Shirakihara Y, Evans PR (1988). "Crystal structure of the complex of phosphofructokinase from Escherichia coli with its reaction products". J. Mol. Biol. 204 (4): 973–994. doi:10.1016/0022-2836(88)90056-3. PMID 2975709.
External links
- Phosphofructokinases at the US National Library of Medicine Medical Subject Headings (MeSH)
This article incorporates text from the public domain Pfam and InterPro IPR000023
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Transferases: phosphorus-containing groups (EC 2.7)
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2.7.1-2.7.4:
phosphotransferase/kinase
(PO4) |
| 2.7.1: OH acceptor |
- Hexo-
- Gluco-
- Fructo-
- Galacto-
- Phosphofructo-
- 1
- Liver
- Muscle
- Platelet
- 2
- Riboflavin
- Shikimate
- Thymidine
- NAD+
- Glycerol
- Pantothenate
- Mevalonate
- Pyruvate
- Deoxycytidine
- PFP
- Diacylglycerol
- Phosphoinositide 3
- Class I PI 3
- Class II PI 3
- Sphingosine
- Glucose-1,6-bisphosphate synthase
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| 2.7.2: COOH acceptor |
- Phosphoglycerate
- Aspartate
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| 2.7.3: N acceptor |
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| 2.7.4: PO4 acceptor |
- Phosphomevalonate
- Adenylate
- Nucleoside-diphosphate
- Uridylate
- Guanylate
- Thiamine-diphosphate
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|
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2.7.6: diphosphotransferase
(P2O7) |
- Ribose-phosphate diphosphokinase
- Thiamine diphosphokinase
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2.7.7: nucleotidyltransferase
(PO4-nucleoside) |
| Polymerase |
| DNA polymerase |
- DNA-directed DNA polymerase
- I
- II
- III
- IV
- V
- RNA-directed DNA polymerase
- Reverse transcriptase
- Telomerase
- DNA nucleotidylexotransferase/Terminal deoxynucleotidyl transferase
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| RNA nucleotidyltransferase |
- RNA polymerase/DNA-directed RNA polymerase
- RNA polymerase I
- RNA polymerase II
- RNA polymerase III
- RNA polymerase IV
- Primase
- RNA-dependent RNA polymerase
- PNPase
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Phosphorolytic
3' to 5' exoribonuclease |
|
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| Uridylyltransferase |
- Glucose-1-phosphate uridylyltransferase
- Galactose-1-phosphate uridylyltransferase
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| Guanylyltransferase |
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| Other |
- Recombinase (Integrase)
- Transposase
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| 2.7.8: miscellaneous |
| Phosphatidyltransferases |
- CDP-diacylglycerol—glycerol-3-phosphate 3-phosphatidyltransferase
- CDP-diacylglycerol—serine O-phosphatidyltransferase
- CDP-diacylglycerol—inositol 3-phosphatidyltransferase
- CDP-diacylglycerol—choline O-phosphatidyltransferase
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| Glycosyl-1-phosphotransferase |
- N-acetylglucosamine-1-phosphate transferase
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2.7.10-2.7.13: protein kinase
(PO4; protein acceptor) |
| 2.7.10: protein-tyrosine |
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| 2.7.11: protein-serine/threonine |
- see serine/threonine-specific protein kinases
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| 2.7.12: protein-dual-specificity |
- see serine/threonine-specific protein kinases
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| 2.7.13: protein-histidine |
- Protein-histidine pros-kinase
- Protein-histidine tele-kinase
- Histidine kinase
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- B
- enzm
- 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 3.1
- 4.1
- 5.1
- 6.1-3
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Related Pictures
★リンクテーブル★
[★]
- 英
- phosphofructokinase, PFK
- 同
- ホスホフルクトキナーゼ1 phosphofructokinase-1
- 関
- ホスホフルクトキナーゼ2。解糖系
生体内での調節
乳酸アシドーシスにおいて
- 重炭酸Naの投与でアシドーシスを補正する場合、HCO3-はphosphofructokinaseの活性を亢進させるので、乳酸アシドーシスを悪化させることがある。
急性呼吸性アルカローシスにいて
- 血液のpHが上昇するとホスホフルクトキナーゼの活性が亢進するため、血液中のリン酸が細胞内に取り込まれる結果、低リン血症を来すことがある。
解糖系
臨床関連
[★]
- 英
- PFKM deficiency
- 関
- 糖原病VII型
[★]
- 英
- 6-phosphofructo-2-kinase
[★]
[★]
平行線維 parallel fiber parallel fibre