PFKP

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Fosfofruktokinaza, trombocit

Identifikatori

Simboli

PFKP; ATP-PFK; PFK-C; PFK-P; PFKF

Vanjski ID

OMIM: 171840 MGI: 1891833 HomoloGene: 20579 GeneCards: PFKP Gene

EC broj

2.7.1.11

Ontologija gena
Molekulska funkcija	• 6-fosfofruktokinazna aktivnost • ATP vezivanje • vezivanje proteinskog kompleksa
Ćelijska komponenta	• nukleus • citosol • 6-fosfofruktokinazni kompleks
Biološki proces	• ugljenohidratni metabolički proces • fruktoza 6-fosfatni metabolički proces • glukozni metabolički proces

Pregled RNK izražavanja

podaci

Ortolozi

Vrsta

Čovek

Miš

Entrez

5214

56421

Ensembl

ENSG00000067057

ENSMUSG00000021196

UniProt

Q01813

Q9WUA3

Ref. Sekv. (iRNK)

NM_001242339

NM_001291071

Ref. Sekv. (protein)

NP_001229268

NP_001278000

Lokacija (UCSC)

Chr 10:
3.11 - 3.18 Mb

Chr 13:
6.58 - 6.65 Mb

PubMed pretraga

[1]

[2]

Fosfofruktokinaza, trombocit, takođe poznata kao PFKP je enzim koji je kod ljudi kodiran PFKP genom.^[1]

Funkcija

PFKP gen kodira trombocitnu izoformu fosfofruktokinaze (PFK) (ATP:D-fruktoza-6-fosfat-1-fosfotransferaza, EC 2.7.1.11). PFK katalizujue ireverzibilnu konverziju fruktoza 6-fosfata do fruktoza 1,6-bisfosfata i ključni je regulatorni enzim u glikolizi. PFKP gen, koji je mapiran na hromozomu 10p, je isto tako izražen u fibroblastima. Mišićna (PFKM) i jetrena (PFKL) izoforma fosfofruktokinaze su locirane na hromozomima 12q13 i 21q22, respektivno. Completni tetramerni fosfofruktokinazni enzim koji je prisutan u trombocitima može da bude formiran od podjedinica P4, P3L, i P2L2.^[2]^[1]

Reference

↑ ^1,0 ^1,1 „Entrez Gene: PFKP phosphofructokinase, platelet”.
↑ Vora S (April 1981). „Isozymes of human phosphofructokinase in blood cells and cultured cell lines: molecular and genetic evidence for a trigenic system”. Blood 57 (4): 724–32. PMID 6451249.

Literatura

Meienhofer MC, Lagrange JL, Cottreau D i dr.. (1979). „Phosphofructokinase in human blood cells”. Blood 54 (2): 389–400. PMID 156568.
Kahn A, Meienhofer MC, Cottreau D i dr.. (1979). „Phosphofructokinase (PFK) isozymes in man. I. Studies of adult human tissues”. Hum. Genet. 48 (1): 93–108. DOI:10.1007/bf00273280. PMID 156693.
Morrison N, Simpson C, Fothergill-Gilmore L i dr.. (1992). „Regional chromosomal assignment of the human platelet phosphofructokinase gene to 10p15”. Hum. Genet. 89 (1): 105–6. DOI:10.1007/BF00207053. PMID 1533608.
Simpson CJ, Fothergill-Gilmore LA (1991). „Isolation and sequence of a cDNA encoding human platelet phosphofructokinase”. Biochem. Biophys. Res. Commun. 180 (1): 197–203. DOI:10.1016/S0006-291X(05)81276-8. PMID 1834056.
Nakajima H, Noguchi T, Yamasaki T i dr.. (1987). „Cloning of human muscle phosphofructokinase cDNA”. FEBS Lett. 223 (1): 113–6. DOI:10.1016/0014-5793(87)80519-7. PMID 2822475.
Eto K, Sakura H, Yasuda K i dr.. (1994). „Cloning of a complete protein-coding sequence of human platelet-type phosphofructokinase isozyme from pancreatic islet”. Biochem. Biophys. Res. Commun. 198 (3): 990–8. DOI:10.1006/bbrc.1994.1141. PMID 8117307.
Bonaldo MF, Lennon G, Soares MB (1997). „Normalization and subtraction: two approaches to facilitate gene discovery”. Genome Res. 6 (9): 791–806. DOI:10.1101/gr.6.9.791. PMID 8889548.
Adam GC, Sorensen EJ, Cravatt BF (2003). „Trifunctional chemical probes for the consolidated detection and identification of enzyme activities from complex proteomes”. Mol. Cell Proteomics 1 (10): 828–35. DOI:10.1074/mcp.T200007-MCP200. PMID 12438565.
Strausberg RL, Feingold EA, Grouse LH i dr.. (2003). „Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences”. Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. DOI:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Ota T, Suzuki Y, Nishikawa T i dr.. (2004). „Complete sequencing and characterization of 21,243 full-length human cDNAs”. Nat. Genet. 36 (1): 40–5. DOI:10.1038/ng1285. PMID 14702039.
Navarro-Lérida I, Martínez Moreno M, Roncal F i dr.. (2004). „Proteomic identification of brain proteins that interact with dynein light chain LC8”. Proteomics 4 (2): 339–46. DOI:10.1002/pmic.200300528. PMID 14760703.
Beausoleil SA, Jedrychowski M, Schwartz D i dr.. (2004). „Large-scale characterization of HeLa cell nuclear phosphoproteins”. Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. DOI:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
Gerhard DS, Wagner L, Feingold EA i dr.. (2004). „The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)”. Genome Res. 14 (10B): 2121–7. DOI:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Rush J, Moritz A, Lee KA i dr.. (2005). „Immunoaffinity profiling of tyrosine phosphorylation in cancer cells”. Nat. Biotechnol. 23 (1): 94–101. DOI:10.1038/nbt1046. PMID 15592455.
Hannemann A, Jandrig B, Gaunitz F i dr.. (2005). „Characterization of the human P-type 6-phosphofructo-1-kinase gene promoter in neural cell lines”. Gene 345 (2): 237–47. DOI:10.1016/j.gene.2004.11.018. PMID 15716112.
Beausoleil SA, Villén J, Gerber SA i dr.. (2006). „A probability-based approach for high-throughput protein phosphorylation analysis and site localization”. Nat. Biotechnol. 24 (10): 1285–92. DOI:10.1038/nbt1240. PMID 16964243.
Ewing RM, Chu P, Elisma F i dr.. (2007). „Large-scale mapping of human protein–protein interactions by mass spectrometry”. Mol. Syst. Biol. 3 (1): 89. DOI:10.1038/msb4100134. PMC 1847948. PMID 17353931.
Martínez-Costa OH, Sánchez-Martínez C, Sánchez V, Aragón JJ (2007). „Chimeric phosphofructokinases involving exchange of the N- and C-terminal halves of mammalian isozymes: implications for ligand binding sites”. FEBS Lett. 581 (16): 3033–8. DOI:10.1016/j.febslet.2007.05.059. PMID 17544406.

Transferaze: fosfor-sadržavajuće grupe (EC 2.7)

2.7.1-2.7.4:
fosfotransferaze/kinaze
(PO₄)

2.7.1: OH- akceptor	Hekso- • Gluko- • Frukto- (Hepatička) • Galakto- • Fosfofrukto- (1, Jetra, Mišić, Trombocit, 2) • Riboflavin • Šikimat • Timidin (ADP-timidin) • NAD⁺ • Glicerol • Pantotenat • Mevalonat • Piruvat • Deoksicitidin • PFP • Diacilglocerol • Fosfoinozitid 3 (Klasa I PI 3, Klasa II PI 3) • Sfingozin • Glukoza-1,6-bisfosfat sintaza
2.7.2: COOH akceptor	Fosfoglicerat • Aspartat
2.7.3: N akceptor	Kreatin
2.7.4: PO₄ akceptor	Fosfomevalonat • Adenilat • Nukleozid-difosfat

2.7.6: difosfotransferaze
(P₂O₇)

Riboza-fosfat difosfokinaza • Tiaminska pirofosfokinaza

2.7.7: nukleotidiltransferaza
(PO₄-nukleozid)

Polimeraza

DNK polimeraza	DNK-usmerena DNK polimeraza: DNK polimeraza I • DNA polimeraza II • DNA polimeraza III holoenzim RNK-usmerena DNA polimeraza: Reverzna transkriptaza (Telomeraza) DNK nukleotidileksotransferaza/Terminalna deoksinukleotidil transferaza
RNK nukleotidiltransferaza	RNK polimeraza/DNK-usmerena RNK polimeraza: RNK polimeraza I • RNK polimeraza II • RNK polimeraza III • RNK polimeraza IV • Primaza • RNK-zavisna RNK polimeraza PNPaza

Fosforolitička
3' do 5' eksoribonukleaza

RNaza PH • PNPaze

Uridililtransferaza

Glukoza-1-fosfat uridililtransferaza • Galaktoza-1-fosfat uridililtransferaza

Guanililtransferaza

iRNK završavajući enzim

Druge

Rekombinaza (Integraza) • Transpozaza

2.7.8: razno

Fosfatidiltransferaze	CDP-diacilglicerol—glicerol-3-fosfat 3-fosfatidiltransferaza • CDP-diacilglicerol—serin O-fosfatidiltransferaza • CDP-diacilglicerol—inozitol 3-fosfatidiltransferaza • CDP-diacilglicerol—holin O-fosfatidiltransferaza
Glikozil-1-fosfotransferaza	N-acetilglukozamin-1-fosfat transferaza

2.7.10-2.7.13: proteinske kinaze
(PO₄; proteinski akceptor)

2.7.10: proteinske-tirozinske	vidi tirozinske kinaze
2.7.11: proteinske-serin/treonin	vidi serin/treonin-specifične proteinske kinaze
2.7.12: dualna specifičnost	vidi serin/treonin-specifične proteinske kinaze
2.7.13: protein-histidinske	Protein-histidinske pros-kinaze • Proteinske-histidinske tele-kinaze • Histidinske kinaze

B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6