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decamer
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10 * 57000, isozyme PK2, SDS-PAGE
dimer or tetramer
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PKM2 can switch between a highly active tetrameric and an inactive dimeric form
hexamer
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3 * 58000 + 3 64000, SDS-PAGE
monomer
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1 * 210000, isozyme PKp, SDS-PAGE
octamer
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4 * 60000 + 4 * 57000, gel filtration
trimer
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M2-PK showing ProTalpha kinase activity is a trimeric association and possesses no observable pyruvate kinase activity
?
x * 61940, deduced from gene sequence
?
x * 58000, recombinant detagged enzyme, SDS-PAGE
?
x * 54000, recombinant enzyme, SDS-PAGE
?
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x * 54000, recombinant enzyme, SDS-PAGE
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?
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x * 54000, recombinant enzyme, SDS-PAGE
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?
x * 50000, SDS-PAGE, x * 49800, calculated
?
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x * 50000, SDS-PAGE, x * 49800, calculated
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?
x * 62570, deduced from gene sequence
dimer
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dimer
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predominant enzyme form
dimer
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nearly inactive dimeric form
dimer
dimeric PKM2 is regarded as an inactive form of tetrameric pyruvate kinase, but the enzymatic activity of the PKM2 dimer is determined in presence of metabolite SAICAR
dimer
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nearly inactive dimeric form
dimer
2 * 55400, SDS-PAGE, predominantly a dimer, but also some tetramer
dimer
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2 * 57000, SDS-PAGE
homodimer
2 * 36000, recombinant enzyme, SDS-PAGE
homodimer
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2 * 29495, MALDI-TOF spectrometry
homohexamer
6 * 67572, sequence calculation
homohexamer
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6 * 67572, sequence calculation
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homohexamer
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6 * 67572, sequence calculation
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homohexamer
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6 * 67572, sequence calculation
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homohexamer
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6 * 67572, sequence calculation
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homohexamer
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6 * 67572, sequence calculation
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homohexamer
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6 * 67572, sequence calculation
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homotetramer
-
-
homotetramer
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4 * 56000, gel filtration
homotetramer
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x-ray crystallography
homotetramer
enzyme structure in complex with ATP, oxalate, and fructose-2,6-bishosphate, overview
homotetramer
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crystal structure
homotetramer
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secondary and tertiary structure of muscle isozyme homotetramer and the four monomers with three tryptophans Trp157, Trp481, and Trp514, and bound Mg2+ and K+ per monomer, each monomer consists of the N-terminal domain, domain A, domain B, and domain C, overview
homotetramer
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structure of muscle isozyme homotetramer and of the four monomers with Y-interface and Z-interface, each monomer consists of the N-terminal domain, domain A, domain B, and domain C, overview
homotetramer
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4 * 80000, SDS-PAGE
homotetramer
4 * 55000, PYK-I, SDS-PAGE
homotetramer
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4 * 56000, gel filtration
homotetramer
4 * 65100, about, full-length enzyme, sequence calculation, 4 * 53100, about, C-terminally truncated enzyme mutant, sequence calculation
homotetramer
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4 * 50000-60000
homotetramer
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4 * 50000-60000
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homotetramer
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4 * 65100, about, full-length enzyme, sequence calculation, 4 * 53100, about, C-terminally truncated enzyme mutant, sequence calculation
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homotetramer
4 * 50000, recombinant His-tagged VcIIPK, SDS-PAGE, 4 * 54914, recombinant His-tagged VcIIPK, mass spectrometry, 4 * 52333, VcIIPK, sequence calculation
homotetramer
4 * 50000, recombinant His-tagged VcIPK, SDS-PAGE, 4 * 53138, recombinant His-tagged VcIPK, mass spectrometry, 4 * 50439, VcIPK, sequence calculation
homotetramer
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4 * 50000, recombinant His-tagged VcIIPK, SDS-PAGE, 4 * 54914, recombinant His-tagged VcIIPK, mass spectrometry, 4 * 52333, VcIIPK, sequence calculation
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homotetramer
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4 * 50000, recombinant His-tagged VcIPK, SDS-PAGE, 4 * 53138, recombinant His-tagged VcIPK, mass spectrometry, 4 * 50439, VcIPK, sequence calculation
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homotetramer
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4 * 50000, recombinant His-tagged VcIIPK, SDS-PAGE, 4 * 54914, recombinant His-tagged VcIIPK, mass spectrometry, 4 * 52333, VcIIPK, sequence calculation
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homotetramer
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4 * 50000, recombinant His-tagged VcIPK, SDS-PAGE, 4 * 53138, recombinant His-tagged VcIPK, mass spectrometry, 4 * 50439, VcIPK, sequence calculation
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tetramer
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4 * 70000
tetramer
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4 * 51000, SDS-PAGE
tetramer
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4 * 49000, SDS-PAGE
tetramer
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4 * 49000, SDS-PAGE
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tetramer
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4 * 65000, SDS-PAGE
tetramer
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4 * 52000, L-type isozyme
tetramer
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4 * 56000, SDS-PAGE
tetramer
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x * 55000 + 4-x * 57000, SDS-PAGE
tetramer
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4 * 58000, SDS-PAGE
tetramer
Busycotypus canaliculatum
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4 * 72600, PK-anoxic, SDS-PAGE
tetramer
Busycotypus canaliculatum
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4 * 71000, PK-aerobic, SDS-PAGE
tetramer
Busycotypus canaliculatum
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4 * 64400, PK-aerobic, SDS-PAGE
tetramer
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4 * 57000, SDS-PAGE
tetramer
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4 * 58000, SDS-PAGE
tetramer
three-dimensional structure determination and analysis, structure comparisons, overview. Each CpPyK monomer consists of four domains: N (residues 23-32), A (residues 42-112 and 212-389), B (residues 113-211) and C (residues 390-526). The A-domain constitutes the central part of the molecule and forms a parallel (alphaa/beta)8 barrel. The B-domain contains nine beta strands that form an antiparallel beta-barrel. The active site is located at the interface of the A and B domains, and residues from both domains participate in substrate binding. The C-domain is composed of five beta strands surrounded by five alpha-helices. The allosteric site for binding the effector molecule is located in the C-domain. The A domains of the two monomers A and B form the major interface
tetramer
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4 * 50000, SDS-PAGE
tetramer
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4 * 66000, tetrameric in low ionic strength buffer
tetramer
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4 * 51000, isozyme PK I, SDS-PAGE
tetramer
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4 * 56000, isozyme PK II, SDS-PAGE
tetramer
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4 * 62000-64000, SDS-PAGE
tetramer
crystallization data
tetramer
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4 * 73000, SDS-PAGE
tetramer
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4 * 73000, SDS-PAGE
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tetramer
4 * 62000, SDS-PAGE
tetramer
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4 * 60000, L-type isozyme, SDS-PAGE
tetramer
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2 * 60000 + 2 * 57000-58000, most important of the "aged" isozymes, PKR2, SDS-PAGE, derived from erythroblast homotetramer by partial proteolysis and transformation into various active heterotetrameric forms with two partially proteolyzed subunits
tetramer
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x-ray crystallography
tetramer
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associated within the glycolytic enzyme complex
tetramer
binding of fructose 1,6-bisphosphate tetramerizes the enzyme, whereas its release causes dissociation to dimer
tetramer
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highly active tetrameric form
tetramer
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4 * 59000, SDS-PAGE
tetramer
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4 * 54400, isozyme PK1, SDS-PAGE
tetramer
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4 * 58000, SDS-PAGE, isozyme PK5
tetramer
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4 * 59500, K4-type isozyme, SDS-PAGE
tetramer
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4 * 58600, M4-type isozyme, SDS-PAGE
tetramer
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highly active tetrameric form
tetramer
Musa cavendishii
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4 * 57000, SDS-PAGE
tetramer
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4* 57540, SDS-PAGE
tetramer
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4* 57540, SDS-PAGE
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tetramer
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4 * 48000, SDS-PAGE
tetramer
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S-type isozyme, SDS-PAGE
tetramer
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4 * 62000-66000, SDS-PAGE
tetramer
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2 * 56000 + 2 * 57000, SDS-PAGE
tetramer
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x * 56000 + x * 57000, SDS-PAGE
tetramer
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4 * 50000-52000, SDS-PAGE
tetramer
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4 * 54000, isozyme I, SDS-PAGE
tetramer
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4 * 47000, isozyme II, SDS-PAGE
tetramer
2 * 55400, SDS-PAGE, predominantly a dimer, but also some tetramer
tetramer
4 * 51300, SDS-PAGE
tetramer
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structure-based molecular modeling and crystal structure analysis, overview
tetramer
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4 * 44000, SDS-PAGE
tetramer
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4 * 44000, SDS-PAGE
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tetramer
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4 * 59000, SDS-PAGE
tetramer
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4 * 63000, SDS-PAGE
tetramer
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4 * 62000, liver enzyme, SDS-PAGE
tetramer
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4 * 60000, SDS-PAGE, M1 isozyme
tetramer
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4 * 66000, SDS-PAGE
tetramer
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4 * 57000, SDS-PAGE
tetramer
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4 * 49000, SDS-PAGE
tetramer
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4 * 51000, native enzyme, SDS-PAGE
tetramer
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4 * 56000, recombinant enzyme, SDS-PAGE
tetramer
4 * 57000, SDS-PAGE
tetramer
each monomer is composed of four domains: A, B, C and N, structure, overview. The central A domain, residues I59-G124 and V224-C393, is composed of an (alpha/beta)8 barrel. The B-domain, P125-P223, is composed of only beta-strands and random coils. The catalytic site is located at the interface of these two domains, where residues in domain A interact with PEP and ADP and residues from the B domain contact ADP and Mg2+. The C domain, residues V394-E531, is composed of alpha and beta structural elements. It contains the effector binding/allosteric site. The N-terminal domain includes the first fifty amino acids of the protein and is a helix-loop-helix motif, however in the TgPK1 only a single helix is observed
tetramer
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4 * 50500, PykF, SDS-PAGE, circular dichroism spectroscopy, and gel filtration, 4 * 51500, PykA, SDS-PAGE, circular dichroism spectroscopy, and gel filtration
tetramer
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4 * 50500, PykF, SDS-PAGE, circular dichroism spectroscopy, and gel filtration, 4 * 51500, PykA, SDS-PAGE, circular dichroism spectroscopy, and gel filtration
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additional information
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structure overview
additional information
Antarctic fish
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structure overview
additional information
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structure overview
additional information
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structure overview
additional information
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the isozymes are thought to be homotetramers, but hybrid isozymes result in vivo if a cell synthesizes 2 or more subunits simultaneously and in vitro after denaturation/renaturation of isozymic mixtures
additional information
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overview
additional information
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overview
additional information
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structure overview
additional information
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structure overview
additional information
a long extra N-terminal sequence of 120 amino acids makes Pyk2 (67.6 kDa) larger than other typical bacterial Pyks (51 kDa), most other Pyk2s are homotetramers, enzyme structure comparisons
additional information
a long extra N-terminal sequence of 120 amino acids makes Pyk2 (67.6 kDa) larger than other typical bacterial Pyks (51 kDa), most other Pyk2s are homotetramers, enzyme structure comparisons
additional information
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a long extra N-terminal sequence of 120 amino acids makes Pyk2 (67.6 kDa) larger than other typical bacterial Pyks (51 kDa), most other Pyk2s are homotetramers, enzyme structure comparisons
additional information
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a long extra N-terminal sequence of 120 amino acids makes Pyk2 (67.6 kDa) larger than other typical bacterial Pyks (51 kDa), most other Pyk2s are homotetramers, enzyme structure comparisons
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additional information
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a long extra N-terminal sequence of 120 amino acids makes Pyk2 (67.6 kDa) larger than other typical bacterial Pyks (51 kDa), most other Pyk2s are homotetramers, enzyme structure comparisons
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additional information
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a long extra N-terminal sequence of 120 amino acids makes Pyk2 (67.6 kDa) larger than other typical bacterial Pyks (51 kDa), most other Pyk2s are homotetramers, enzyme structure comparisons
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additional information
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a long extra N-terminal sequence of 120 amino acids makes Pyk2 (67.6 kDa) larger than other typical bacterial Pyks (51 kDa), most other Pyk2s are homotetramers, enzyme structure comparisons
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additional information
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a long extra N-terminal sequence of 120 amino acids makes Pyk2 (67.6 kDa) larger than other typical bacterial Pyks (51 kDa), most other Pyk2s are homotetramers, enzyme structure comparisons
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additional information
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a long extra N-terminal sequence of 120 amino acids makes Pyk2 (67.6 kDa) larger than other typical bacterial Pyks (51 kDa), most other Pyk2s are homotetramers, enzyme structure comparisons
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additional information
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overview
additional information
secondary structure determination by circular dichroism spectrometry. Effect of pH on the tertiary structure, overview
additional information
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secondary structure determination by circular dichroism spectrometry. Effect of pH on the tertiary structure, overview
additional information
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structure overview
additional information
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structure overview
additional information
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structure overview
additional information
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M2 pyruvate kinase is a substrate of delta protein kinase C. delta Protein kinase C activation in vitro or in cells does not appear to alter the enzyme activity or polymerization of M2 pyruvate kinase
additional information
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M2-type enzyme directly interacts with promyelocytic leukemia tumor suppressor protein
additional information
the hepatitis C virus RNA-dependent RNA polymerase interacts with M2-type pyruvate kinase, but not with L-type pyruvate kinase
additional information
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in tumors, the dimeric form of M2-PK is predominant due to direct interaction with different oncoproteins and components of the protein kinase cascade, such as HPV-16 E7, the tyrosine kinases pp60v-src, BCR-ABL, ETV6-NTRK3, FGFR-1, FLT3 and JAK-2, the serine/threonine kinase A-Raf, cytoplasmic promyelocytic leukemia tumor suppressor protein as well as phosphotyrosine peptides
additional information
the dimeric isozyme PKM2 is inactive
additional information
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the dimeric isozyme PKM2 is inactive
additional information
although found to exist in different oligomeric forms in cells, like other pyruvate kinases, PKM2 is considered to have maximal pyruvate kinase activity as a tetramer. Prevalence of dimeric PKM2 in cancer
additional information
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although found to exist in different oligomeric forms in cells, like other pyruvate kinases, PKM2 is considered to have maximal pyruvate kinase activity as a tetramer. Prevalence of dimeric PKM2 in cancer
additional information
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structure overview
additional information
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structure overview
additional information
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overview
additional information
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structure overview
additional information
secondary structure analysis by circular dichroism spectroscopy revealing a content of 17% alpha-helix, 34% beta-sheet, and 49% turns in the enzyme
additional information
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secondary structure analysis by circular dichroism spectroscopy revealing a content of 17% alpha-helix, 34% beta-sheet, and 49% turns in the enzyme
additional information
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secondary structure analysis by circular dichroism spectroscopy revealing a content of 17% alpha-helix, 34% beta-sheet, and 49% turns in the enzyme
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additional information
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secondary structure analysis by circular dichroism spectroscopy revealing a content of 17% alpha-helix, 34% beta-sheet, and 49% turns in the enzyme
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additional information
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structure overview
additional information
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structure overview
additional information
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structure overview
additional information
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structure overview
additional information
structure-function analysis, overview
additional information
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structure-function analysis, overview
additional information
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structure overview
additional information
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overview
additional information
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structure overview
additional information
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structure overview
additional information
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overview
additional information
the C-terminal domain is not required for the tetramerization of the enzyme, homotetramerization also occurs in a truncated enzyme lacking the domain
additional information
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the C-terminal domain is not required for the tetramerization of the enzyme, homotetramerization also occurs in a truncated enzyme lacking the domain
additional information
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the C-terminal domain is not required for the tetramerization of the enzyme, homotetramerization also occurs in a truncated enzyme lacking the domain
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additional information
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structure overview
additional information
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structure overview
additional information
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structure overview