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heterohexamer
3 * 46328, GdhA, + 3 * 46112, GdhB, sequence calculation and SDS-PAGE
monomer
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at 25°C the enzyme is mostly represented by monomeric subunits at concentrations lower than 0.02 mg/ml, while oligomers are predominant at concentrations higher than 0.12 mg/ml
octamer
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8 * 61000, or aggregate of two tetramers, SDS-PAGE
oligomer
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at 25°C the enzyme is mostly represented by monomeric subunits at concentrations lower than 0.02 mg/ml, while oligomers are predominant at concentrations higher than 0.12 mg/ml
tetramer
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4 * 52000, SDS-PAGE
?
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x * 57000, SDS-PAGE
?
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x * 57000, SDS-PAGE
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?
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x * 57500, recombinant enzyme, SDS-PAGE
?
x * 47122, calculated from sequence
?
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x * 56000, enzymes from mitochondria and endoplasmic reticulum
?
x * 46078, calculated from sequence
?
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x * 46078, calculated from sequence
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dimer
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the GdhA-GdhB-Leu complex is crystallized as a heterohexamer composed of four GdhA subunits and two GdhB subunits. In this complex, six leucine molecules are bound at subunit interfaces identified as glutamate-binding sites in the GdhB-Glu complex
dimer
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the GdhA-GdhB-Leu complex is crystallized as a heterohexamer composed of four GdhA subunits and two GdhB subunits. In this complex, six leucine molecules are bound at subunit interfaces identified as glutamate-binding sites in the GdhB-Glu complex
hexamer
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6 * 54000, SDS-PAGE
hexamer
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6 * 48000, SDS-PAGE
hexamer
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6 * 49000, SDS-PAGE
hexamer
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4 * 44000 + 2 * 46000, isoenzyme GDH2, SDS-PAGE
hexamer
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isoenzyme GDH1, SDS-PAGE
hexamer
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6 * 56000, wild-type enzyme and mutant enzymes K333L, K337L, K344L, K346L, S445L and G446L
hexamer
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6 * 56500, hGDH1, SDS-PAGE
hexamer
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6 * 56500, hGDH2, SDS-PAGE
hexamer
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native gradient polyacryamide gel electrophoresis, 6 * 60000 Da
hexamer
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the GdhB-Glu complex is a hexamer that binds 12 glutamate molecules: six molecules are bound at the substrate-binding sites, and the remaining six are bound at subunit interfaces, each composed of three subunits
hexamer
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6 * 47300, recombinant enzyme, second peak in gel filtration corresponding to catalytically inactive monomer, SDS-PAGE
hexamer
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6 * 46000, SDS-PAGE
hexamer
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6 * 46000, recombinant enzyme, SDS-PAGE
hexamer
electrostatic interactions play a key role in the relevant stability of Pyrococcus furiosus hlutamate dehydrogenase quaternary assembly at low pH although there may be other contributions involved in the complex mechanism of subunit association required for protein function
hexamer
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6 * 48000, SDS-PAGE
hexamer
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6 * 46000, SDS-PAGE
hexamer
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6 * 45000, SDS-PAGE
hexamer
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6 * 44000, SDS-PAGE
hexamer
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6 * 50000, membrane-bound liver enzyme, SDS-PAGE
hexamer
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6 * 57000, SDS-PAGE
hexamer
6 * 47040, calculated from sequence, the natural enzyme was purified only as a hexameric form, whereas the recombinant enzyme was purified as both monomeric and hexameric forms. Only the enzyme in a hexameric form is active. Upon heat treatment (70°C for 15 min), the inactive monomeric form of the recombinant enzyme is at least partially associated with the hexameric form
hexamer
6 * 47300, SDS-PAGE, the natural enzyme was purified only as a hexameric form, whereas the recombinant enzyme was purified as both monomeric and hexameric forms. Only the enzyme in a hexameric form is active. Upon heat treatment (70°C for 15 min), the inactive monomeric form of the recombinant enzyme is at least partially associated with the hexameric form
hexamer
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the GdhB-Glu complex is a hexamer that binds 12 glutamate molecules: six molecules are bound at the substrate-binding sites, and the remaining six are bound at subunit interfaces, each composed of three subunits
hexamer
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6 * 53900, sedimentation equilibrium of enzyme treated with 6 M guanidinium and 0.5% 2-mercaptoethanol
hexamer
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6 * 40500, SDS-PAGE
hexamer
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6 * 59500, enzyme from both euthermic and hibernating animals
homohexamer
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homohexamer
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6 * 56000, SDS-PAGE
homohexamer
6 * 56000, about, dimer of trimers
homohexamer
dimer of trimers, the enzyme adopts a novel semi-closed conformation, which is an intermediate between known open and closed GDH1 conformations, differing from both. Structure-function analysis, overview. Each monomer consists of the glutamate-binding domain (residues 1-210), the NAD+-binding domain (residues 211-399), the antenna (residues 400-448), the pivot helix (residues 449-478) and the C-terminal alpha-helix (residues 479-501), which are very similar to the structural features of hGDH1. The antenna region is formed by the ascending and descending helix
homohexamer
method of determination not further specified
trimer
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6 * 56000, mutant enzyme H454Y
trimer
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analytical ultracentrifugation
trimer
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analytical ultracentrifugation
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additional information
gene products genes Gdh1, Gdh2 and Gdh3 are three different Gdh subunits that randomly associate to form a complex array of homo- and hetero-hexamers
additional information
gene products genes Gdh1, Gdh2 and Gdh3 are three different Gdh subunits that randomly associate to form a complex array of homo- and hetero-hexamers
additional information
gene products genes Gdh1, Gdh2 and Gdh3 are three different Gdh subunits that randomly associate to form a complex array of homo- and hetero-hexamers
additional information
structure overview
additional information
structure overview
additional information
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structure overview
additional information
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Thermus thermophilus, possesses GDH with a unique subunit configuration composed of two different subunits, GdhA, the regulatory subunit, and GdhB, the catalytic subunit, structure of the GdhA-GdhB-Leu complex, overview
additional information
sequence comparisons and GDH structure homology modeling studies, overview
additional information
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Thermus thermophilus, possesses GDH with a unique subunit configuration composed of two different subunits, GdhA, the regulatory subunit, and GdhB, the catalytic subunit, structure of the GdhA-GdhB-Leu complex, overview
additional information
GDH is composed of two heterologous subunits, GdhA and GdhB. GdhA and GdhB form a heterohexamer, in which GdhB acts as the catalytic subunit and GdhA acts as the regulatory subunit to sense leucine. In the heterocomplex, GdhB acts as the catalytic subunit, whereas GdhA lacks enzymatic activity and acts as the regulatory subunit for activation by leucine. TTC1249 (APRTh), which is annotated as adenine phosphoribosyltransferase but lacks the enzymatic activity, forms a ternary complex with the enzyme heterodimer. The ternary complex exhibits GDH activity that is activated by leucine, as observed for the GdhA-GdhB binary complex
additional information
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GDH is composed of two heterologous subunits, GdhA and GdhB. GdhA and GdhB form a heterohexamer, in which GdhB acts as the catalytic subunit and GdhA acts as the regulatory subunit to sense leucine. In the heterocomplex, GdhB acts as the catalytic subunit, whereas GdhA lacks enzymatic activity and acts as the regulatory subunit for activation by leucine. TTC1249 (APRTh), which is annotated as adenine phosphoribosyltransferase but lacks the enzymatic activity, forms a ternary complex with the enzyme heterodimer. The ternary complex exhibits GDH activity that is activated by leucine, as observed for the GdhA-GdhB binary complex