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heteromer
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GAPDH-AnBn heteromer of GapA and GapB subunits
heterotetramer
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A2B2-GAPDH, light conformation, B subunits are almost identical to A subunits, expect for the presence of a C-terminal extension containing a pair of cysteines, which is the target of TRX regulation
multimer
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A8B8-GAPDH, dark conformation, B subunits are almost identical to A subunits, expect for the presence of a C-terminal extension containing a pair of cysteines, which is the target of TRX regulation
octamer
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8 * 43000, pentalenolactone-insensitive enzyme, gel filtration
?
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x * 37600, calculated and SDS-PAGE
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Q81X74, YP_027084
x * 40000, SDS-PAGE
?
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x * 35500 + x * 37000, SDS-PAGE
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x * 35000, high speed equilibrium sedimentation after treatment with 5 M guanidine hydrochloride containing 0.01 M dithiothreitol
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x * 36446, calculated from amino acid sequence
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x * 36446, calculated, x * 38000, SDS-PAGE
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x * 14000, SDS-PAGE, probably truncated form, x * 37000, native enzyme, SDS-PAGE, x * 43000, recombinant His-tagged enzyme, SDS-PAGE
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x * 35470, apo-form of GADPH isozyme uracil-DNA glycosylase, mass spectrometry
?
x * 75000, about, recombinant enzyme, SDS-PAGE, x * 45000-50000, native enzyme, SDS-PAGE
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x * 75000, about, recombinant enzyme, SDS-PAGE, x * 45000-50000, native enzyme, SDS-PAGE
?
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x * 75000, about, recombinant enzyme, SDS-PAGE, x * 45000-50000, native enzyme, SDS-PAGE
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?
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x * 36000, about, sequence determination and analysis
?
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x * 36000, about, sequence determination and analysis
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?
x * 27000 + x * 37000 + x * 51000, SDS-PAGE
?
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x * 27000 + x * 37000 + x * 51000, SDS-PAGE
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?
x * 35914, calculated from sequence
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x * 36100, calculated
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?
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x * 14000 + x * 37000, SDS-PAGE
?
x * 37600, calculated, x * 37500, SDS-PAGE
?
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x * 37600, calculated, x * 37500, SDS-PAGE
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dimer
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x-ray crystallography
dimer
2 * 37000, about, sequence calculation, ligands bound
dimer
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1 * 58000 + 1 * 61000, enzyme form E6.6, SDS-PAGE
dimer
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the final crystallographic model consists of a dimer
homodimer
2 * 36200, recombinant enzyme, SDS-PAGE
homodimer
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2 * 36200, recombinant enzyme, SDS-PAGE
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homodimer
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2 * 36200, recombinant enzyme, SDS-PAGE
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homodimer
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2 * 36200, recombinant enzyme, SDS-PAGE
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homodimer
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2 * 36200, recombinant enzyme, SDS-PAGE
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homotetramer
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homotetramer
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GAPDH-A4, homotetramer GapA subunits
homotetramer
4 * 36000, SDS-PAGE
homotetramer
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4 * 37000, SDS-PAGE
homotetramer
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4 * 36500, non-denaturing PAGE
homotetramer
x-ray crystallography
homotetramer
4 * 37000, recombinant His-tagged enzyme, SDS-PAGE
homotetramer
4 * 38000, SDS-PAGE
homotetramer
4 * 40000, N-terminally truncated enzyme after trypsin treatment, SDS-PAGE
homotetramer
4 * 37672, MALDI-TOF mass spectrometry
homotetramer
4 * 37000, about, SDS-PAGE
homotetramer
4 * 37000, about, SDS-PAGE
homotetramer
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4 * 37000, about
homotetramer
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4 * 37000, SDS-PAGE
homotetramer
4 * 36000, SDS-PAGE
homotetramer
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4 * 36000, SDS-PAGE
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homotetramer
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4 * 36000, SDS-PAGE
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homotetramer
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4 * 50000, SDS-PAGE
homotetramer
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4 * 51000, native PAGE slab gels with varying acrylamide concentrations of 5-10% (w/v) in the absence of SDS
homotetramer
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4 * 50000, SDS-PAGE
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homotetramer
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4 * 51000, native PAGE slab gels with varying acrylamide concentrations of 5-10% (w/v) in the absence of SDS
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homotetramer
4 * 37000, SDS-PAGE
homotetramer
4 * 36636, wild-type enzyme, sequence calculation, 4 * 40000, about, recombinant N-terminally prolongated enzyme, SDS-PAGE, 4 * 40355, recombinant N-terminally prolongated enzyme, sequence calculation
homotetramer
4 * 37000, SDS-PAGE
homotetramer
SDS-PAGE and gel filtration
homotetramer
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4 * 37000, denaturing SDS-PAGE
homotetramer
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4 * 38500, non-denaturing PAGE
homotetramer
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GAPDH-A4, homotetramer GapA subunits
homotetramer
functional GAPDH is a homotetramer, with each monomer composed of two domains: the N-terminal coenzyme binding domain and the C-terminal catalytic domain. The catalytic domain contains the Ps and Pi sites, which bind the C(3) phosphate of the substrate and the inorganic phosphate ion, respectively, during the phosphorylation step carried out by the enzyme. The S-loop folds over in close proximity to the bound cofactor, modelling
homotetramer
x-ray crystallography
homotetramer
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x-ray crystallography
homotetramer
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x-ray crystallography
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homotetramer
a dimer of dimers, 4 * 44000, about, SDS-PAGE
homotetramer
4 * 36830, MALDI-TOF mass spectrometry
homotetramer
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4 * 36830, MALDI-TOF mass spectrometry
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homotetramer
4 * 37000, SDS-PAGE
monomer
1 * 36000, SDS-PAGE
monomer
1 * 45000, SDS-PAGE, isozyme uracil-DNA glycosylase, enzyme as adduct with AP DNA
monomer
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1 * 36000, SDS-PAGE
monomer
1 * 45000, SDS-PAGE, isozyme uracil-DNA glycosylase
monomer
1 * 38000, SDS-PAGE, 1 * 38760, mass spectrometry
tetramer
either treatment with psiGAPDH or direct phosphorylation of GAPDH by deltaPKC decreased GAPDH tetramerization, which corresponded to reduced GAPDH glycolytic activity in vitro and ex vivo
tetramer
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4 * 36000, SDS-PAGE
tetramer
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4 * 35000, SDS-PAGE
tetramer
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4 * 38500, SDS-PAGE
tetramer
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4 * 36000, SDS-PAGE
tetramer
either treatment with psiGAPDH or direct phosphorylation of GAPDH by deltaPKC decreased GAPDH tetramerization, which corresponded to reduced GAPDH glycolytic activity in vitro and ex vivo
tetramer
4 * 32400, engineered recombinant enzyme, SDS-PAGE, 4 * 35500, non-modified wild-type enzyme, SDS-PAGE
tetramer
each of the subunits can be divided into two domains: the N-terminal NAD+-binding domain and the C-terminal catalytic domain. The NAD+-binding domain is typically a Rossman fold containing eight beta-strands, namely beta1 (Lys3-Asn7), beta2 (Asp28-Asn33), beta3 (Val58-Phe60), beta4 (Ser64-Val67), beta5 (Lys70-Tyr75), beta6 (Ile92-Glu95), beta7 (Lys116-Ile119) and beta8 (Ile144-Ser146). The strands are connected by either helices or short loops. beta3 and beta5 are antiparallel to the other six parallel beta-strands. There are four alpha-helices in this domain: alpha1 (Gly10-Val23), alpha2 (Ser37-His47), alpha3 (Ser102-Ser106) and alpha4 (Gln107-Ala112). The catalytic domain contains eight mixed beta-sheets, beta9 (Ile168-Ala178), beta10 (Ile205-His207), beta11 (Leu226-Val231), beta12 (Ser239-Leu247), beta13 (Phe270-Thr273), beta14 (Ser289-Asp292), beta15 (Glu297-Val301) and beta16 (Leu304-Tyr313), and three long alpha-helices, alpha5 (Ser149-Gly167), alpha6 (Thr252-Thr264) and alpha7 (Gln317-Lys332). The catalytically active residues Cys150 and His177 are situated in alpha5 and beta9, respectively
tetramer
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4 * 37000, SDS-PAGE
tetramer
4 * 37000, about, sequence calculation and modeling
tetramer
either treatment with psiGAPDH or direct phosphorylation of GAPDH by deltaPKC decreased GAPDH tetramerization, which corresponded to reduced GAPDH glycolytic activity in vitro and ex vivo
tetramer
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4 * 36000, SDS-PAGE
tetramer
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4 * 37000, SDS-PAGE
tetramer
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4 * 40000, SDS-PAGE
tetramer
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4 * 38000, cetyltrimethyl ammonium bromide PAGE
tetramer
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4 * 38000, cetyltrimethyl ammonium bromide PAGE
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tetramer
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4 * 36000, SDS-PAGE
tetramer
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4 * 29500, enzyme form E8.5, SDS-PAGE
tetramer
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x * 36000 + x * 38000, enzyme form E6.8, SDS-PAGE
tetramer
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4 * 33000, enzyme form E9.5, SDS-PAGE
tetramer
N-terminally truncated mutant, crystallization data
tetramer
either treatment with psiGAPDH or direct phosphorylation of GAPDH by deltaPKC decreased GAPDH tetramerization, which corresponded to reduced GAPDH glycolytic activity in vitro and ex vivo
tetramer
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determined by gel filtration
tetramer
either treatment with psiGAPDH or direct phosphorylation of GAPDH by deltaPKC decreased GAPDH tetramerization, which corresponded to reduced GAPDH glycolytic activity in vitro and ex vivo
tetramer
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sedimentation analysis
tetramer
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4 * 36000-37000, SDS-PAGE
tetramer
4 * 37000, SDS-PAGE
tetramer
either treatment with psiGAPDH or direct phosphorylation of GAPDH by deltaPKC decreased GAPDH tetramerization, which corresponded to reduced GAPDH glycolytic activity in vitro and ex vivo
tetramer
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either treatment with psiGAPDH or direct phosphorylation of GAPDH by deltaPKC decreased GAPDH tetramerization, which corresponded to reduced GAPDH glycolytic activity in vitro and ex vivo
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tetramer
4 * 41000, SDS-PAGE
tetramer
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4 * 37000, SDS-PAGE
tetramer
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4 * 35000, SDS-PAGE
tetramer
4 * 37000, dimer of dimer, SDS-PAGE
tetramer
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4 * 37000, dimer of dimer, SDS-PAGE
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tetramer
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4 * 37000, dimer of dimer, SDS-PAGE
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tetramer
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4 * 43000, pentalenolactone-sensitive enzyme, gel filtration
tetramer
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4 * 38000, SDS-PAGE
tetramer
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4 * 38000, glyoxysomal enzyme, SDS-PAGE
tetramer
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4 * 37000, SDS-PAGE
tetramer
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4 * 36000, SDS-PAGE
tetramer
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4 * 33500, SDS-PAGE
tetramer
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4 * 33700, SDS-PAGE
tetramer
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4 * 33700, SDS-PAGE
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tetramer
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4 * 38000, GAPDH I and GAPDH II, SDS-PAGE
tetramer
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4 * 38000, glyoxysomal enzyme, SDS-PAGE
tetramer
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4 * 33500, cytosolic enzyme, SDS-PAGE
tetramer
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4 * 36000, SDS-PAGE
tetramer
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4 * 36000, SDS-PAGE
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tetramer
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4 * 35000, SDS-PAGE
tetramer
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4 * 40000-42000, SDS-PAGE
additional information
enzyme can bind top a partial gene sequence of NADP-dependent malated dehydrogenase EC 1.2.1.37
additional information
enzyme can bind top a partial gene sequence of NADP-dependent malated dehydrogenase EC 1.2.1.37
additional information
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enzyme can bind top a partial gene sequence of NADP-dependent malated dehydrogenase EC 1.2.1.37
additional information
structure analysis, overview. Dual side-chain conformations are observed in Ser207 in subunits of O, Q, and R of the bGAPDH(NAD)3
additional information
purified recombinant FhGAPDH is a mixture of homodimers and tetramers, as judged by protein-protein crosslinking and analytical gel filtration. The addition of either NAD+ or glyceraldehyde 3-phosphate shifts this equilibrium towards a compact dimer, that is more stable than the unliganded one. Molecular modeling of FhGAPDH monomer, and of the enzyme as a tetramer, the quaternary structure is shown as a dimer of dimers arrangement, overview. Substrate binding induces conformational and oligomerisation changes in FhGAPDH, both glyceraldehyde 3-phosphate and NAD+ appear to favour the formation of dimers over tetramers
additional information
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purified recombinant FhGAPDH is a mixture of homodimers and tetramers, as judged by protein-protein crosslinking and analytical gel filtration. The addition of either NAD+ or glyceraldehyde 3-phosphate shifts this equilibrium towards a compact dimer, that is more stable than the unliganded one. Molecular modeling of FhGAPDH monomer, and of the enzyme as a tetramer, the quaternary structure is shown as a dimer of dimers arrangement, overview. Substrate binding induces conformational and oligomerisation changes in FhGAPDH, both glyceraldehyde 3-phosphate and NAD+ appear to favour the formation of dimers over tetramers
additional information
dimers generated from the tetrameric enzyme are inactive but exhibit cooperativity in NAD+ binding
additional information
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dimers generated from the tetrameric enzyme are inactive but exhibit cooperativity in NAD+ binding
additional information
isolation of a truncated form of the protein from the excretory-secretory products of the parasite worms using C3-affinity chromatography, and identification by mass spectroscopy as glyceraldehyde-3-phosphate dehydrogenase, GAPDH
additional information
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isolation of a truncated form of the protein from the excretory-secretory products of the parasite worms using C3-affinity chromatography, and identification by mass spectroscopy as glyceraldehyde-3-phosphate dehydrogenase, GAPDH
additional information
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recombinant GAPDH binds directly with high affinity to a single-stranded oligonucleotide comprising three telomeric DNA repeats. Nucleotides T1, G5, and G6 of the TTAGGG repeat are essential for binding.The stoichiometry of the interaction is 2:1 DNA:GAPDH, and GAPDH appears to form a high-molecular-weight complex when bound to the oligonucleotide
additional information
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recombinant glyceraldehyde 3-phosphate dehydrogenase binds to hepatitis B virus regulatory element RNA in vitro and inhibits hepatitis B virus regulatory element function. Overexpression of glyceraldehyde 3-phosphate dehydrogenase depresses the expression of hepatitis B virus antigen
additional information
GAPDH is composed of two folding domains, an NAD+-binding domain (residues 2-150) and a catalytic domain (residues 155-312)
additional information
high-molecular-weight multimers of serum GAPDH, multiple protein bands (about 25, and 50-75 kDa) along with some proteins with weak signals in albumin-depleted serum samples, SDS-PAGE and mass spectrometry. The enzymatic function of serum GAPDH remained unaffected by the multimers
additional information
molecular docking simulation
additional information
the residues P164 (beta-turn), P326 (first position of alpha-helix), and the interdomain salt bridge D311-H124 are significant for the enhanced stability of GAPDS. The salt bridge D311-H124 enhances stability of the active site of GAPDS at the expense of the catalytic activity. The N-terminal domain is hidden inside the cytoskeleton structures and does not interact with the catalytic part of the enzyme
additional information
the residues P164 (beta-turn), P326 (first position of alpha-helix), and the interdomain salt bridge D311-H124 are significant for the enhanced stability of GAPDS. The salt bridge D311-H124 enhances stability of the active site of GAPDS at the expense of the catalytic activity. The N-terminal domain is hidden inside the cytoskeleton structures and does not interact with the catalytic part of the enzyme
additional information
three GAPDS-specific salt bridges, E96-H394 and D311-H124 connect the NAD+-binding and the catalytic domains within a single subunit, while E244-R320 is formed between two different subunits
additional information
three GAPDS-specific salt bridges, E96-H394 and D311-H124 connect the NAD+-binding and the catalytic domains within a single subunit, while E244-R320 is formed between two different subunits
additional information
human GAPDH identified by peptide mass fingerprinting and mass spectrometric analysis
additional information
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human GAPDH identified by peptide mass fingerprinting and mass spectrometric analysis
additional information
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peptide mapping, mass spectrometry, overview
additional information
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enzyme exists as an equilibrium mixture of different oligomeric states. Rapid equilibrium between monomer - dimer - tetramer, the tetramer is inactive
additional information
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non-native forms of GAPDH obtained by cold denaturation, oxidation of the enzyme, or its unfolding in guanidine hydrochloride efficiently bind to soluble amyloid-beta peptide (1-42) yielding a stable complex. Native tetrameric GAPDH does not interact with soluble amyloid-beta peptide (1-42), neither non-native forms of GAPDH interact with aggregated amyloid-beta peptide (1-42)
additional information
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the CgGAP protein consists of an N-terminal NAD+-binding domain and a central catalytic domain
additional information
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the CgGAP protein consists of an N-terminal NAD+-binding domain and a central catalytic domain
additional information
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the CgGAP protein consists of an N-terminal NAD+-binding domain and a central catalytic domain
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additional information
the 51 kDa enzyme form is present only in the soluble fraction of the cell extract
additional information
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the 51 kDa enzyme form is present only in the soluble fraction of the cell extract
additional information
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the 51 kDa enzyme form is present only in the soluble fraction of the cell extract
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additional information
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subunit interactions are involved in regulation of activity
additional information
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immobilized enzyme can exist as a trimer
additional information
quarternary structure analysis and comparisons, overview
additional information
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quarternary structure analysis and comparisons, overview
additional information
subunits of the dimers form the major interface P, overview. The second largest interface, the R interface, includes residues in the N-terminal domain that interact with NAD+ and loop residues 181-206 in the C-terminal domain of subunit pairs A, C and B, D. The smallest interface, the Q interface, shows limited interactions between residues in the ranges 43-53 and 274-291 of adjacent subunits A, D and B, C
additional information
the enzyme crystal structure contains an asymmetric mixed holo tetramer (four copies of the GAPDH molecule in one asymmetric unit that form a tetramer or two dimers, namely the A-B dimer and the C-D dimer), with two NAD+ ligands bound to two protomers. The asymmetric dimers A-B of both structures can be aligned nearly perfectly, while the asymmetric dimers C-D are in very different conformations because of the different NAD+ binding states of the molecules. The molecular interfaces within both tetramers are essentially the same. Overall, the two tetramers are in different conformations owing to the different ligand-binding states of the four promoters
additional information
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the enzyme crystal structure contains an asymmetric mixed holo tetramer (four copies of the GAPDH molecule in one asymmetric unit that form a tetramer or two dimers, namely the A-B dimer and the C-D dimer), with two NAD+ ligands bound to two protomers. The asymmetric dimers A-B of both structures can be aligned nearly perfectly, while the asymmetric dimers C-D are in very different conformations because of the different NAD+ binding states of the molecules. The molecular interfaces within both tetramers are essentially the same. Overall, the two tetramers are in different conformations owing to the different ligand-binding states of the four promoters
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additional information
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the enzyme crystal structure contains an asymmetric mixed holo tetramer (four copies of the GAPDH molecule in one asymmetric unit that form a tetramer or two dimers, namely the A-B dimer and the C-D dimer), with two NAD+ ligands bound to two protomers. The asymmetric dimers A-B of both structures can be aligned nearly perfectly, while the asymmetric dimers C-D are in very different conformations because of the different NAD+ binding states of the molecules. The molecular interfaces within both tetramers are essentially the same. Overall, the two tetramers are in different conformations owing to the different ligand-binding states of the four promoters
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additional information
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interaction of GAPDH with Porphyromonas gingivalis major fimbrae plays an important role in Porphyromonas gingivalis colonization. Amino acid residues 166 to 183 of Streptococcus oralis GAPDH exhibit the strongest binding activity toward rFimA, and the synthetic peptide corresponding to amino acid residues 166 to 183 of GAPDH, peptide DNFGVVEGLMTTIHAYTG inhibits Streptococcus oralis-Porphyromonas gingivalis biofilm formation in a dose-dependent manner. The peptide inhibits interbacterial biofilm formation by several oral streptococci and Porphyromonas gingivalis strains with different types of FimA
additional information
enzyme modeling