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EC Tree
The taxonomic range for the selected organisms is: Mus musculus The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
pgk, phosphoglycerate kinase, pgk-1, 3-phosphoglycerate kinase, phosphoglycerate kinase 1, pgk-2, phosphoglycerate kinase-1, phosphoglycerokinase, phosphoglycerate kinase 2, 3-pgk,
more
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phosphoglycerate kinase 2
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3-phosphoglycerate kinase
3-phosphoglycerate phosphokinase
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3-phosphoglyceric acid kinase
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3-phosphoglyceric acid phosphokinase
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3-phosphoglyceric kinase
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ATP-3-phospho-D-glycerate-1-phosphotransferase
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ATP:D-3-phosphoglycerate 1-phosphotransferase
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glycerate 3-phosphate kinase
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glycerophosphate kinase
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kinase (phosphorylating), phosphoglycerate
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phosphoglycerate kinase 1
phosphoglycerate kinase 2
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phosphoglyceric acid kinase
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phosphoglyceric kinase
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phosphoglycerokinase
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X chromosome-linked phosphoglycerate kinase-1
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3-phosphoglycerate kinase
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3-phosphoglycerate kinase
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PGK1
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phosphoglycerate kinase 1
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phosphoglycerate kinase 1
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phospho group transfer
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-, -, -, -, -, -, -, -, -, -, -, -, -, -, -
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ATP:3-phospho-D-glycerate 1-phosphotransferase
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ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
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r
3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl 1-phosphate
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-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
CTP + 3-phospho-D-glycerate
CDP + 1,3-diphosphoglycerate
dATP + 3-phospho-D-glycerate
dADP + 1,3-diphosphoglycerate
dGTP + 3-phospho-D-glycerate
dGDP + 1,3-diphosphoglycerate
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
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-
-
-
?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
additional information
?
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ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
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r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
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r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
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r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
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r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
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r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
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-
-
?
CTP + 3-phospho-D-glycerate
CDP + 1,3-diphosphoglycerate
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no activity
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-
?
CTP + 3-phospho-D-glycerate
CDP + 1,3-diphosphoglycerate
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low activity
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-
?
CTP + 3-phospho-D-glycerate
CDP + 1,3-diphosphoglycerate
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1% of the activity with ATP
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-
?
dATP + 3-phospho-D-glycerate
dADP + 1,3-diphosphoglycerate
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-
?
dATP + 3-phospho-D-glycerate
dADP + 1,3-diphosphoglycerate
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isozymes PGK2A, PGK2B, and PGK1 show low activity, isozyme PGK2C shows 119% of the activity with ATP
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?
dGTP + 3-phospho-D-glycerate
dGDP + 1,3-diphosphoglycerate
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?
dGTP + 3-phospho-D-glycerate
dGDP + 1,3-diphosphoglycerate
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isozyme PGK2C with lower activity, all other isozymes show slightly lower activity compared to ATP
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?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
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?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
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60% of the activity with ATP
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-
?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
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?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
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1% of the activity with ATP
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?
additional information
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the only analog of 3-phospho-D-glycerate that can replace the substrate is an artificial 3-phospho-D-glycerate in which the phosphate group-O-PO3H2 is replaced by the phosphomethyl group-CH2-PO3H2, i.e. 2-hydroxy-4-phospho-DL-butyric acid
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additional information
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nucleotide substrate specificity
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additional information
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no activity with dTTP
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?
additional information
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Pgk1 plays some functional roles in the development of tooth germ and other embryonic organs by forming protein complex with glyceraldehyde-3-phosphate dehydrogenase
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?
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ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
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r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
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?
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ATP
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ATP
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required as phosphate donor
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divalent cation
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Mg2+ or Mn2+
Mn2+
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0.8 mM Mg2+ and 0.5 mM Mn2+ are optimal
Mg2+
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Mg2+
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0.8 m Mg2+ and 0.5 mM Mn2+ are optimal
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2,3-diphosphoglycerate
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competitive to 3-phospho-D-glycerate and MgATP2-
5,5'-dithiobis(2-nitrobenzoic acid)
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ADP
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inhibitory in forward reaction
citrate
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40% inhibition at 50 mM
additional information
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no effect by glucose 6-phosphate, fructose 6-phosphate, fructose 1,6-phosphate, pyruvate, phosphoenolpyruvate and lactate
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additional information
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the KH-type splicing regulatory protein, KSRP, serves as a decay-promoting factor for Pgk2 mRNA in male germ cells. KSRP binds to to a 93-nt sequence (the F1 region) of the 3'-UTR of the Pgk2 mRNA and destabilizes Pgk2 mRNA constructs in testis extracts and in transfected cells. Destabilization of Pgk2 mRNA occurs when t-KSRP and the Pgk2 mRNA-stabilizing protein, polypyrimidine tract binding protein 2 (PTBP2), are present together in complexes bound to the 3'-UTR of Pgk2 mRNA
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additional information
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no effect by glucose 6-phosphate, fructose 6-phosphate, fructose 1,6-phosphate, pyruvate, phosphoenolpyruvate and lactate
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0.028 - 0.2
3-phospho-D-glycerate
additional information
additional information
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0.028
3-phospho-D-glycerate
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isozyme PGK2C
0.15
3-phospho-D-glycerate
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isozyme PGK2B, ADP, isoenzyme PGK2A
0.2
3-phospho-D-glycerate
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pH 6.9, 25°C
0.2
3-phospho-D-glycerate
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isoenzyme PGK2A
0.039
ADP
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isozyme PGK2C
0.038
ATP
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isoenzyme PGK2C
0.22
ATP
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isoenzyme PGK1
0.37
ATP
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ATP in form of MgATP2-
additional information
additional information
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kinetics
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additional information
additional information
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Km values at different pH-values
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additional information
additional information
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kinetics for 3-phospho-D-glycerate are biphasic
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additional information
additional information
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pH-dependence of Km values for the substrates in forward and reverse reaction, 2 isozymes
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2.3 - 3.8
2,3-diphosphoglycerate
2.3
2,3-diphosphoglycerate
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versus MgATP2-
3.8
2,3-diphosphoglycerate
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versus 3-phospho-D-glycerate
0.08
ADP
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pH 6.5, 25°C, versus ATP
0.175
ADP
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pH 6.5, 25°C, versus 3-phospho-D-glycerate
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260 - 450
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purified isozyme PGKB
430
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purified isozyme PGK2B
450
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purified isozyme PGK2A
600
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purified testis enzyme
8.5
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purified isozyme PGK2C
500
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purified isozyme PGKA
500
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purified isozyme PGK1
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5.4 - 8
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30% activity at pH 5.4, 60% activity at pH 8.0
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25 - 40
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activity of both isozymes in either reaction direction increases steadily with increasing temperature within this range
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UniProt
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phosphoglycerate kinase 2 is a sperm-specific isoform
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exclusively expressed in spermatids
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from intraperitoneal cavity
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ovary
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there is no significant difference in cell proliferation between parental Lewis lung carcinoma (LLC-1) and LLC-1 transduced with PGK-1. Overexpression of PGK-1 in LLC-1 reduces the COX-2 expression, and, in turn, affects prostaglandin E2, cell invasion, angiogenesis, and the immune functions, and finally inhibit the tumor progression
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2fold higher level than in testis
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in early meiosis
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isozyme PGK2
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of the mouse lower first molar. Strong expression of Pgk1 mRNA in the odontogenic epithelial cells and surrounding mesenchymal cells of the tooth germ from embryonic day 10.5 to embryonic day 18.0
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additional information
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isozyme PGK1 is found in all somatic tissues
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of testis, PTBP2 is a trans-acting factor that helps to stabilize Pgk2 mRNA in male mouse germ cells
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Pgk2 mRNA accumulates in postmeiotic germ cells
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isozyme PGKA
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mature
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isozyme PGK2
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isozyme PGKB
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polypyrimidine tract binding protein 2 binds to PGK2 mRNA in the testis
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PTBP2 is a trans-acting factor that helps to stabilize Pgk2 mRNA in male mouse germ cells
brenda
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similar levels of Pgk2 mRNA transcription in nuclei isolated from the testes of prepuberal (17 day old) and adult mice
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malfunction
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targeted disruption of Pgk2 by homologous recombination eliminates PGK activity in sperm and testis, and severely impairs male fertility, but does not block spermatogenesis. Mating behavior, reproductive organ weights (testis, excurrent ducts, and seminal vesicles), testis histology, sperm counts, and sperm ultrastructure are indistinguishable between Pgk2(-/-) and wild-type mice. Sperm motility and ATP levels are markedly reduced in males lacking PGK2. Pgk2(-/-) males sire occasional pups. Alternative pathways that bypass the PGK step of glycolysis exist. One of these bypass enzymes, acylphosphatase, is active in mouse sperm, perhaps contributing to phenotypic differences between mice lacking GAPDHS or PGK2
physiological function
Pgk1/EGFP expression in ovaries is effective in protecting the fecundity of the partial ovaries after ovary allotransplantation
physiological function
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PGK2 is not required for completion of spermatogenesis, but is essential for sperm motility and male fertility
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PGK2_MOUSE
417
0
44853
Swiss-Prot
other Location (Reliability: 2 )
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45000
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gel filtration
45000
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isozymes PGKA and PGKB
47000
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gel filtration
47000
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isoenzymes PGK1, PGK2A, PGK2B, PGK2C
47000
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1 * 47000, isozymes PGKA and PGKB, SDS-PAGE
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monomer
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monomer
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1 * 47000, SDS-PAGE
monomer
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1 * 47000, isozymes PGKA and PGKB, SDS-PAGE
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crystallized in three forms: as the apoenzyme, as a complex with 3-phosphoglycerate, and as a complex with 3-phosphoglycerate and ATP. The crystal structures are solved to 2.7, 2.0, and 2.7 A resolutions, respectively
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4.7
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isozyme PGKB: loss of 70% activity after 45 min, isozyme PGKA: loss of 10% activity after 45 min
642268
9.6
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isozymes PGKA and PGKB: stable for at least 30 min
642268
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50
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pH 6.0, 10 min: 20% loss of activity, PGKA, 80% loss of activity PGKB
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bovine serum albumin and dithioerythritol stabilize in the enzyme assay
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optimal stabilization at 1 mM EDTA and 5 mM 2-mercaptoethanol
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as a precipitate in 3.3 M ammonium sulfate, stable for years
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876fold, to homogeneity
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99fold from muscle, 333fold from testis
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isoenzyme PGK1 and all 3 genetic variants of PGK2
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overexpression in Escherichia coli
129S6/SvEvTac genomic DNA fragments inserted into vector pUCBM21
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1872-bp Pgk1/EGFP DNA fragment excised by double digestion of MluI and DraIII, consisting of 519 bp of the Pgk1 promoter, 723 bp of the EGFP cDNA and 224 bp of the bovine growth hormone (BGH) poly-A tail from the vector pPgk1/EGFP. Microinjection into the pronucleus of in vitro-fertilized FVB/NCrl mouse eggs and re-implanted into pseudopregnant ICR females to generate transgenic mice. CHO-K1 cells transfected with pPgk1/EGFP
3'UTR of PGK2 subcloned into the three regions F1, F2 and F3
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in the cytoplasm of early meiotic spermatocytes, t-KSRP promotes the decay of Pgk2 mRNA
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Pgk2 mRNA is first detectable in early meiosis in spermatocytes and increases dramatically in spermatids. Decline of t-KSRP in late meiosis and increase of PTBP2 are concomitant with the increase in Pgk2 mRNA levels
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analysis
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in situ PCR is useful for detecting PGK-1 gene in paraffin-embedded sections under optimized conditions of both PCR cycle number and proteinase K concentration
additional information
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polypyrimidine tract binding protein 2 is a trans-acting factor that helps to stabilize PGK2 mRNA in male mouse germ cells, specifically binds to the F1 region of the PGK2 3'-UTR
medicine
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PGK-1 may be an important therapeutic target for pharmacological or gene therapy intervention in non-small cell lung carcinoma
medicine
transgenic mice ubiquitously expressing enhanced green fluorescent protein (EGFP) under the control of the phosphoglycerate kinase 1 promoter by allotransplantation of transgenic mice ovaries may be useful for studies assessing the use of gene therapy of bone marrow or nerve cells, as well as for tumorigenesis and organ transplantation studies
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Kuntz, G.W.K.; Krietsch, W.K.G.
Phosphoglycerate kinase from animal tissue
Methods Enzymol.
90
103-110
1982
Oryctolagus cuniculus, Equus caballus, Homo sapiens, Mus musculus, trout
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brenda
Lee, C.Y.
3-Phosphoglycerate kinase isozymes and genetic variants from mouse
Methods Enzymol.
90
121-126
1982
Mus musculus
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brenda
Pegorado, B.; Lee, C.Y.
Purification and characterization of two isozymes of 3-phosphoglycerate kinase from the mouse
Biochim. Biophys. Acta
522
423-433
1978
Mus musculus, Mus musculus DBA/2J
brenda
Mukherjee, K.; Ghosh, S.; Ray, M.; Ray, S.
Purification and characterization of 3-phosphoglycerate kinase from Ehrlich ascites carcinoma cells
Indian J. Biochem. Biophys.
39
332-341
2002
Mus musculus
brenda
Xu, M.; Hecht, N.B.
Polypyrimidine tract binding protein 2 stabilizes phosphoglycerate kinase 2 mRNA in murine male germ cells by binding to its 3UTR
Biol. Reprod.
76
1025-1033
2007
Mus musculus
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Honda, J.Y.; Kobayashi, I.; Kiyoshima, T.; Yamaza, H.; Xie, M.; Takahashi, K.; Enoki, N.; Nagata, K.; Nakashima, A.; Sakai, H.
Glycolytic enzyme Pgk1 is strongly expressed in the developing tooth germ of the mouse lower first molar
Histol. Histopathol.
23
423-432
2008
Mus musculus
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Tang, S.J.; Ho, M.Y.; Cho, H.C.; Lin, Y.C.; Sun, G.H.; Chi, K.H.; Wang, Y.S.; Jhou, R.S.; Yang, W.; Sun, K.H.
Phosphoglycerate kinase 1-overexpressing lung cancer cells reduce cyclooxygenase 2 expression and promote anti-tumor immunity in vivo
Int. J. Cancer
123
2840-2848
2008
Mus musculus
brenda
Sawyer, G.M.; Monzingo, A.F.; Poteet, E.C.; OBrien, D.A.; Robertus, J.D.
X-ray analysis of phosphoglycerate kinase 2, a sperm-specific isoform from Mus musculus
Proteins
71
1134-1144
2008
Mus musculus (P09041), Mus musculus
brenda
Hishikawa, Y.; An, S.; Yamamoto-Fukuda, T.; Shibata, Y.; Koji, T.
Improvement of in situ PCR by optimization of PCR cycle number and proteinase k concentration: localization of x chromosome-linked phosphoglycerate kinase-1 gene in mouse reproductive organs
Acta Histochem. Cytochem.
42
15-21
2009
Mus musculus
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Danshina, P.V.; Geyer, C.B.; Dai, Q.; Goulding, E.H.; Willis, W.D.; Kitto, G.B.; McCarrey, J.R.; Eddy, E.M.; OBrien, D.A.
Phosphoglycerate kinase 2 (PGK2) is essential for sperm function and male fertility in mice
Biol. Reprod.
82
136-145
2010
Mus musculus
brenda
Xu, M.; McCarrey, J.R.; Hecht, N.B.
A cytoplasmic variant of the KH-type splicing regulatory protein serves as a decay-promoting factor for phosphoglycerate kinase 2 mRNA in murine male germ cells
Nucleic Acids Res.
36
7157-7167
2008
Mus musculus
brenda
Wu, H.; Chou, C.; Hung, Y.; Yu, C.
Allotransplantation of transgenic mouse ovaries expressing enhanced green fluorescent protein under the control of the murine phosphoglycerate kinase 1 promoter
Reprod. Domest. Anim.
45
90090-6
2010
Mus musculus (P09411), Mus musculus
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Mikawa, T.; Shibata, E.; Shimada, M.; Ito, K.; Ito, T.; Kanda, H.; Takubo, K.; Lleonart, M.E.; Inagaki, N.; Yokode, M.; Kondoh, H.
Phosphoglycerate mutase cooperates with Chk1 kinase to regulate glycolysis
iScience
23
101306
2020
Mus musculus (P09411)
brenda
Park, H.J.; Lee, W.Y.; Park, C.; Hong, K.H.; Kim, J.H.; Song, H.
Species-specific expression of phosphoglycerate kinase 2 (PGK2) in the developing porcine testis
Theriogenology
110
158-167
2018
Mus musculus (P09041), Mus musculus, Sus scrofa (Q6RI85), Sus scrofa
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