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x * 49300, catalytic subunit
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x * 72000 + x * 32000, denaturing SDS-PAGE
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x * 73000, calculation from nucleotide sequence
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x * 74200, amino acid sequence calculation
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x * 30548, calculation from nucleotide sequence
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unlike kidney enzyme, most of liver enzyme is in a reduced form which does not have disulfide linkage between heavy and light chain
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x * 90500, about, sequence calculation
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x * 90500, about, sequence calculation
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x * 78300, catalytic subunit
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x * 71400, catalytic subunit
dimer
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GCL reveals two redox-sensitive intramolecular disulfide bonds, CC1 and CC2, located at the homodimer interface that regulate plant GCL activity
dimer
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1 * 73000, about, heavy catalytic subunit, + 1 * 31000, about, light regulatory subunit, SDS-PAGE
dimer
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1 * 80000, about, catalytic subunit, + 1 * 28000, about, modifier subunit, SDS-PAGE
dimer
1 * 72800, heavy catalytic subunit, + 1 * 30700, light regulatory subunit, SDS-PAGE
dimer
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1 * 73000, about, catalytic subunit, + 1 * 31000, about, regulatory subunit, SDS-PAGE
dimer
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2 * 75000, recombinant wild-type and mutant enzymes, SDS-PAGE
dimer
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heavy and light subunit
dimer
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heterodimer of a catalytic subunit and a regulatory subunit, encoded by 2 genes
dimer
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1 * 73000, about, GCLC, + 1 * 31000, about, GCLM
dimer
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heterodimer consisting of subunits GCLC and GCLM
dimer
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the enzyme consists of a catalytic subunit GCLC and a modifier subunit GCLM
dimer
1 * 72700, heavy catalytic subunit, + 1 * 30500, light regulatory subunit, SDS-PAGE
dimer
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1 * 73000, about, catalytic subunit, + 1 * 31000, about, regulatory subunit, SDS-PAGE
dimer
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heterodimer, comprising a catalytic subunit (GCLC) and a regulatory subunit (GCLM). GCLC alone can catalyze the formation of L-gamma-glutamyl-L-cysteine, its binding with GCLM enhances the enzyme activity by lowering the Km for glutamate and ATP, and increasing the Ki for GSH inhibition
dimer
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1 * 73000, about, GCLC, + 1 * 31000, about, GCLM
dimer
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GCL is composed of catalytic GCLC and modifier GCLM subunits
dimer
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heterodimer consisting of catalytic and modifier subunits GCLC and GCLM
dimer
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2 * 34000, SDS-PAGE
dimer
the enzyme contains two intramolecular disulfide bridges, CC1 and CC2, amino acids contributing to the homodimer interface in GCL are highly conserved among plant GCLs, but not in related proteobacterial GCLs. NtGCL forms a homodimer under oxidizing conditions
dimer
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1 * 73000, about, heavy catalytic subunit, + 1 * 31000, about, light regulatory subunit, SDS-PAGE
dimer
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2 * 85000, SDS-PAGE
dimer
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2 *85000, SDS-PAGE
dimer
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1 * 66000 + 1 * 57000, SDS-PAGE
dimer
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1 * 75000 + 1 * 25000, denaturing PAGE in presence of 50 mM DTT
dimer
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1 * 75000 + 1 * 25000, nondenaturing PAGE in presence of 50 mM DTT
dimer
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1 * 74000 + 1 * 24000, SDS-PAGE. One enzyme species of MW 100000 Da detected by SDS-PAGE after cross-linking with dimethylsuberimidate
dimer
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1 * 73000 + 1 * 27700, PAGE in presence of 50 mM DTT
dimer
1 * 72600, heavy catalytic subunit, + 1 * 30600, light regulatory subunit, SDS-PAGE
dimer
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1 * 73000, about, catalytic subunit, + 1 * 31000, about, regulatory subunit, SDS-PAGE
dimer
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heavy and light subunit
dimer
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glutamatecysteine ligase is a heterodimer of a GCLC (GCL catalytic subunit) that possesses all of the enzymatic activity and a GCLM (GCL modifier subunit) that alters the Ki of GCLC for GSH. Differential regulation of glutamatecysteine ligase subunit expression and increased holoenzyme formation in response to cysteine deprivation
dimer
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1 * 73000, about, GCLC, + 1 * 31000, about, GCLM
dimer
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1 * 73000, about, heavy catalytic subunit, + 1 * 31000, about, light regulatory subunit, SDS-PAGE
dimer
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2 * 60000, SDS-PAGE
heterodimer
1 * 74760, catalytic subunit, + 1 * 28510, regulatory subunit, sequence calculation
heterodimer
enzyme GCL is a heterodimeric enzyme consisting of a catalytic subunit (GCLc) and a modulatory subunit (GCLm), which are encoded by two genes. The catalytic subunit GCLc performs all the enzymatic activity and its catalytic efficiency is increased by the covalent interaction with the regulatory subunit GCLm
heterodimer
GCL is a heterodimeric enzyme, consisting of a catalytic subunit, (GCLc) and a modulatory subunit (GCLm) that are encoded by two distinct genes. GCLc constitutes all the enzymatic activity, but catalytic efficiency is increased substantially by covalent interaction with GCLm
heterodimer
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glutamate-cysteine ligase consists of a catalytic subunit (GCLC) and a modifier subunit (GCLM)
heterodimer
glutamate-cysteine ligase (GCL) is a heterodimer enzyme composed of a catalytic subunit (GCLC) and a modulator subunit (GCLM)
heterodimer
enzyme GCL is a heterodimeric enzyme consisting of a catalytic subunit (GCLc) and a modulatory subunit (GCLm), which are encoded by two genes
monomer
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proteobacterial GCLs remain monomeric under oxidizing and reducing conditions, overview
monomer
1 * 59900, catalytic unit
monomer
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x * 35000, mutant enzyme modifier subunit, SDS-PAGE
monomer
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1 * 56000, SDS-PAGE
monomer
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1 * 55000, SDS-PAGE
monomer
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1 * 55000, SDS-PAGE
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monomer
1 * 78100, catalytic unit
monomer
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1 * 60000, about
monomer
1 * 58000, SDS-PAGE, 1 * 57663, mass spectrometry and sequence calculation
monomer
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1 * 58000, SDS-PAGE, 1 * 57663, mass spectrometry and sequence calculation
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monomer
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bifunctional enzyme accounts for gamma-glutamylcysteine synthetase and glutathione synthetase activities
monomer
1 * 46000, recombinant enzyme, SDS-PAGE
monomer
1 * 77500, catalytic unit
monomer
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proteobacterial GCLs remain monomeric under oxidizing and reducing conditions, overview
additional information
glutamate-cysteine ligase (GCL) is a heterodimer enzyme composed of a catalytic subunit (GCLC) and a modifier subunit (GCLM)
additional information
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glutamate-cysteine ligase (GCL) is a heterodimer enzyme composed of a catalytic subunit (GCLC) and a modifier subunit (GCLM)
additional information
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quaternary structure
additional information
the enzyme contains two intramolecular disulfide bridges, CC1 and CC2, which both strongly impact on GCL activity in vitro, cysteines of CC2 involved in the monomer-dimer transition in GCL. Amino acids contributing to the homodimer interface in BjGCL are highly conserved among plant GCLs, but not in related proteobacterial GCLs
additional information
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the enzyme contains two intramolecular disulfide bridges, CC1 and CC2, which both strongly impact on GCL activity in vitro, cysteines of CC2 involved in the monomer-dimer transition in GCL. Amino acids contributing to the homodimer interface in BjGCL are highly conserved among plant GCLs, but not in related proteobacterial GCLs
additional information
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enzyme is build of 2 subunits, a modifier and a catalytic subunit, the modifier subunit DmGCLM possesses cysteine residues, Cyys213, Cys214, and Cys267, which can form covalent interactions with the catalytic subunit DmGCLC and modify its activity, the activity of the holoenzyme is enhanced compared to the catalytic subunit alone
additional information
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enzyme consists of 2 subunits, the heavy catalytic one and the light regulatory one
additional information
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enzyme consists of a catalytic GCLC and a modulatory GCLM subunit
additional information
quarternary structure, the heavy subunit monomer may be essentially nonfunctional under physiological conditions
additional information
quarternary structure, the heavy subunit monomer may be essentially nonfunctional under physiological conditions
additional information
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quarternary structure, the heavy subunit monomer may be essentially nonfunctional under physiological conditions
additional information
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reaction can be performed by the catalytic subunit alone, but presence of the regulatory subunit in the holoenzyme increases the activity
additional information
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reaction can be performed by the catalytic subunit alone, but presence of the regulatory subunit in the holoenzyme increases the activity and the specificity with L-2-aminobutyrate as substrate
additional information
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the holoenzyme consists of a heavy catalytic and a light modifier subunit, i.e. gamma-GCSH and gamma-GCSL, protein modeling
additional information
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the holoenzyme consists of a heavy catalytic and a light regulatory subunit, i.e. gamma-GCSh and gamma-GCSl
additional information
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GCL is a heterodimeric protein composed of catalytic GCLC and modifier GCLM subunits that are expressed from different genes, the catalytic subunit GCLC contains the active site responsible for the ATP-dependent bond formation between the amino group of cysteine and the gamma-carboxyl group of glutamate, the modifier subunit GCLM through direct interaction with GCLC acts to increase the catalytic efficiency of GCLC. GCL subunit protein structures, overview. GCLM is quite sensitive to aggregation in vitro in the absence of GCLC
additional information
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upon oxidative stress, activation of GCL occurrs within min of treatment and without any change in GCL protein levels, and coincides with an increase in the proportion of GCL catalytic subunit in the holoenzyme form. Likewise, GCL modifier subunit shifts from the monomeric form to holoenzyme and higher molecular weight species. Neither GCL activation, nor the formation of holoenzyme, requires a covalent intermolecular disulfide bridge between GCL catalytic subunit and GCL modifier subunit
additional information
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the enzyme consists of a catalytic (GCLC) and a modifier (GCLM) subunit
additional information
the recombinant heavy subunit contains a 55 kDa insert which may function as the small subunit
additional information
quarternary structure
additional information
quarternary structure
additional information
quaternary structure
additional information
quaternary structure
additional information
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the dimeric enzyme is composed of a heavy, catalytic subunit and a light, regulatory subunit
additional information
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the holoenzyme consists of a heavy catalytic and a light regulatory subunit, i.e. gamma-GCSh and gamma-GCSl
additional information
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reaction is catalyzed by the catalytic subunit GCLC or by the holoenzyme (GCLholo), which comprises GCLC and the modifier subunit GCLM. GCLM decreases the Km for ATP by about 6fold and decreases the Km-value for glutamate and increases the Ki-value for feedback inhibition by GSH. GCLM increases by 4.4fold the turnover number for gamma-glutamylcysteine synthesis
additional information
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reaction is catalyzed by the catalytic subunit GCLC or by the holoenzyme (GCLholo), which comprises GCLC and the modifier subunit GCLM. GCLM decreases the Km for ATP by about 6fold and decreases the Km-value for glutamate and increases the Ki-value for feedback inhibition by GSH. GCLM increases by 4.4fold the turnover number for gamma-glutamylcysteine synthesis
additional information
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GCL is a heterodimeric protein composed of catalytic GCLC and modifier GCLM subunits that are expressed from different genes, the catalytic subunit GCLC contains the active site responsible for the ATP-dependent bond formation between the amino group of cysteine and the gamma-carboxyl group of glutamate, the modifier subunit GCLM through direct interaction with GCLC acts to increase the catalytic efficiency of GCLC. GCL subunit protein structures, overview. GCLM is quite sensitive to aggregation in vitro in the absence of GCLC
additional information
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the enzyme consists of a catalytic (GCLC) and a modifier (GCLM) subunit
additional information
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quarternary structure
additional information
three-dimensional model of rPhGshA II obtained by homology modelling, overview. The catalytic residue Cys 386 is located at the protein surface
additional information
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three-dimensional model of rPhGshA II obtained by homology modelling, overview. The catalytic residue Cys 386 is located at the protein surface
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additional information
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the light subunit has a regulatory function affecting the affinity for Glu and GSH
additional information
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the heavy subunit contains all of the structural requirements for enzymatic activity and also for feedback inhibition by glutathione
additional information
quarternary structure, the heavy subunit monomer may be essentially nonfunctional under physiological conditions
additional information
quarternary structure, the heavy subunit monomer may be essentially nonfunctional under physiological conditions
additional information
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the holoenzyme consists of a heavy catalytic and a light regulatory subunit, i.e. gamma-GCSh and gamma-GCSl
additional information
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GCL is a heterodimeric protein composed of catalytic GCLC and modifier GCLM subunits that are expressed from different genes, the catalytic subunit GCLC contains the active site responsible for the ATP-dependent bond formation between the amino group of cysteine and the gamma-carboxyl group of glutamate, the modifier subunit GCLM through direct interaction with GCLC acts to increase the catalytic efficiency of GCLC. GCL subunit protein structures, overview. GCLM is quite sensitive to aggregation in vitro in the absence of GCLC
additional information
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the enzyme consists of a catalytic (GCLC) and a modifier (GCLM) subunit
additional information
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the enzyme consists of a catalytic (GCLC) and a modifier (GCLM) subunit
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additional information
enzyme secondary structure analysis
additional information
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enzyme secondary structure analysis
additional information
secondary structure analysis, overview
additional information
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secondary structure analysis, overview
additional information
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enzyme secondary structure analysis
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additional information
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secondary structure analysis, overview
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additional information
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quaternary structure
additional information
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structure modeling
additional information
the recombinant heavy subunit contains a 55 kDa insert which may function as the small subunit