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multimer
x * 63300, large subunit IlvB, plus x * 18700, small subunit IlvN, SDS-PAGE and calculated.
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x * 59200, calculated from amino acid sequence and SDS-PAGE
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x * 59200, calculated from amino acid sequence and SDS-PAGE
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x * 65000, recombinant enzyme, SDS-PAGE
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x * 63000, SDS-PAGE
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x * 60000, recombinant enzyme, SDS-PAGE
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x * 60200, calculated from amino acid sequence
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x * 9500 + x * 60000, isoenzyme I, SDS-PAGE
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x * 17500 + x * 61800, calculation from nucleotide sequence
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x * 11000 + x * 60000
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x * 16200 + x * 67200, SDS-PAGE
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x * 63700, recombinant His-tagged catalytic subunit, SDS-PAGE
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x * 58000, SDS-PAGE with urea
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x * 60000, SDS-PAGE
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x * 60000, SDS-PAGE
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3 major bands detected by SDS-PAGE: 26000 Da, 35000 Da and 46000 Da
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3 major bands detected by SDS-PAGE: 26000 Da, 35000 Da and 46000 Da
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x * 68000, about, wild-type and mutant enzyme variants, SDS-PAGE
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x * 68000, about, wild-type and mutant enzyme variants, SDS-PAGE
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x * 68000, SDS-PAGE
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?
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x * 48000, deduced from gene sequence
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x * 64000, mature enzyme, SDS-PAGE
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x * 62000, SDS-PAGE, catalytic subunit
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x * 62000, SDS-PAGE, catalytic subunit
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x * 65000, about, SDS-PAGE and MALDI-TOF spectrometry
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x * 15000 + x * 57000 + x * 58000, SDS-PAGE
dimer
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2 * 61000, SDS-PAGE
dimer
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2 * 63864, ion spray MS analysis
dimer
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1 * 59000-66000, catalytic subunit + 1 * 50000, above, regulatory subunit
dimer
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2 * 65000 and/or 66000, SDS-PAGE
dimer
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1 * 59000-66000, catalytic subunit + 1 * 50000, above, regulatory subunit
dimer
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2 * 60000, SDS-PAGE
dimer
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1 * 59000-66000, catalytic subunit + 1 * 10000-20000, above, regulatory subunit
dimer
1 * 59000-66000, catalytic subunit + 1 * 50000, above, regulatory subunit
dimer
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1 * 59000-66000, catalytic subunit + 1 * 50000, above, regulatory subunit
dimer
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2 * 64000, SDS-PAGE
dimer
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2 * 50000, SDS-PAGE, enzyme exists simultaneously as monomer, dimer and trimer
dimer
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2 * 50000, SDS-PAGE, enzyme exists simultaneously as monomer, dimer and trimer
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dimer
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the mobile loop comprising residues 567-582 on the C-terminus is involved in the binding/stabilization of the active dimer and thiamin diphosphate binding, overview
dimer
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1 * 59000-66000, catalytic subunit + 1 * 50000, above, regulatory subunit
dimer
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1 * 59000-66000, catalytic subunit + 1 * 10000-20000, above, regulatory subunit
dimer
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2 * 75000, SDS-PAGE
dimer
1 * 59000-66000, catalytic subunit + 1 * 34000, regulatory subunit
dimer
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1 * 59000-66000, catalytic subunit + 1 * 10000-20000, above, regulatory subunit
dimer
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2 * 64000, SDS-PAGE
dimer
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1 * 59000-66000, catalytic subunit + 1 * 10000-20000, above, regulatory subunit
dimer
2 * 20508, regulatory subunit, sequence calculation, 2 * 22210, regulatory subunit, SDS-PAGE
dimer
2 * 65497, catalytic subunit, sequence calculation, 2 * 66398, catalytic subunit, SDS-PAGE
dimer
1 * 65497, calculated, 1 * 66400, SDS-PAGE, plus 1 * 2058, calculated, 1 * 22200, SDS-PAGE, catalytic and regulatory subunit, respectively
dimer
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1 * 65497, calculated, 1 * 66400, SDS-PAGE, plus 1 * 2058, calculated, 1 * 22200, SDS-PAGE, catalytic and regulatory subunit, respectively
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heterotetramer
2 * 65497 + 2 * 20508, calculated from amino acid sequence
heterotetramer
2 * 66400 + 2 * 22200, SDS-PAGE
homodimer
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the enzyme is a homodimer in solution, the crystal structure shows a homotetramer with one noncovalently bound FAD and one thiamine diphosphate per monomer
homodimer
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the enzyme is a homodimer in solution, the crystal structure shows a homotetramer with one noncovalently bound FAD and one thiamine diphosphate per monomer
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homodimer
x-ray crystallography
homotetramer
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homotetramer
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in the crystallized form
homotetramer
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in the crystallized form
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homotetramer
the enzyme is a homotetramer formed by dimers of dimers, each monomer is composed of three domains. The alpha-domain (up to N181) is connected by a random coil to the central beta-domain (P195 to A346). The C-terminal gamma-domain (from H376) is connected to the central beta-domain by an alpha-helix and a random coil linker, structure-function analysis of the enzyme, overview. The 12 C-terminal resolved residues of AlsS (D556-K567) fold into a short alpha-helix
homotetramer
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the enzyme is a homotetramer formed by dimers of dimers, each monomer is composed of three domains. The alpha-domain (up to N181) is connected by a random coil to the central beta-domain (P195 to A346). The C-terminal gamma-domain (from H376) is connected to the central beta-domain by an alpha-helix and a random coil linker, structure-function analysis of the enzyme, overview. The 12 C-terminal resolved residues of AlsS (D556-K567) fold into a short alpha-helix
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monomer
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1 * 50000, SDS-PAGE, enzyme exists simultaneously as monomer, dimer and trimer
monomer
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1 * 50000, SDS-PAGE, enzyme exists simultaneously as monomer, dimer and trimer
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oligomer
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x * 68300, recombinant His-tagged catalytic subunit, + x * 20400, recombinant His-tagged regulatory subunit, SDS-PAGE
oligomer
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x * 68300, recombinant His-tagged catalytic subunit, + x * 20400, recombinant His-tagged regulatory subunit, SDS-PAGE
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oligomer
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8 * 15000 + 8 * 60000, SDS-PAGE
tetramer
the enzyme consists of a large catalytic and a small regulatory subunit, two copies of which form the enzyme tetramer
tetramer
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4 * 65000, SDS-PAGE, both isoforms
tetramer
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4 * 58000, SDS-PAGE
tetramer
the enzyme consists of a large catalytic and a small regulatory subunit, two copies of which form the enzyme tetramer The catalytic subunit has a molecular weight of 60-70 kD, the regulator of 10-45 kD
tetramer
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the enzyme consists of a large catalytic and a small regulatory subunit, two copies of which form the enzyme tetramer The catalytic subunit has a molecular weight of 60-70 kD, the regulator of 10-45 kD
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tetramer
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the enzyme consists of a large catalytic and a small regulatory subunit, two copies of which form the enzyme tetramer
tetramer
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2 * 9800 + 2 * 59000, SDS-PAGE
tetramer
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the enzyme consists of a large catalytic and a small regulatory subunit, two copies of which form the enzyme tetramer
trimer
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3 * 60000, SDS-PAGE
trimer
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3 * 55000, SDS-PAGE
trimer
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3 * 50000, SDS-PAGE, enzyme exists simultaneously as monomer, dimer and trimer
trimer
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3 * 50000, SDS-PAGE, enzyme exists simultaneously as monomer, dimer and trimer
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trimer
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3 * 55000, SDS-PAGE
additional information
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the regulatory subunit possesses no AHAS activity but greatly stimulates the activity of the catalytic subunit, it is necessary for AHAS to be inhibited by branched-chain amino acids, structures of catalytic and regulatory subunits, sequence comparisons, overview
additional information
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the regulatory subunit possesses no AHAS activity but greatly stimulates the activity of the catalytic subunit, it is necessary for AHAS to be inhibited by branched-chain amino acids, structures of catalytic and regulatory subunits, sequence comparisons, overview
additional information
the catabolic enzyme form lacks a regulatory subunit
additional information
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the catabolic enzyme form lacks a regulatory subunit
additional information
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enzymes in the AHAS family generally consist of regulatory and catalytic subunits, subunit composition, dimeric structure analysis of the regulatory subunit of isozyme AHAS III, overview
additional information
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pairs of catalytic subunits form an intimate dimer containing two active sites, each of which lies across a dimer interface and involves both monomers, the catalytic subunit of AHAS II is not active alone
additional information
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by mapping the 3D contour maps of CoMFA and CoMSIA models into the possible inhibitory active site in the crystal structure of catalytic subunit of yeast AHAS, a plausible binding model for AHAS, with best fit QSAR in the literature so far, is proposed
additional information
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isozyme AHAS I, catalytic subunit ilvB, regulatory subunit ilvN. AHAS II, catalytic subunit ilvG, regulatory subunit ilvM. Isozyme AHAS III, catalytic subunit ilvI, regulatory subunit ilvH. AHAS II regulatory subunit ilvM is able to activate the catalytic subunits of all three of the isozymes, and the truncated AHAS III regulatory subunits ilvH-DELTA80, ilvH-DELTA86 and ilvH-DELTA89 are able to activate the catalytic subunits of both AHAS I and AHAS III. Contrary to wild-type, none of the heterologously activated enzymes have any feedback sensitivity
additional information
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the regulatory subunit possesses no AHAS activity but greatly stimulates the activity of the catalytic subunit, it is necessary for AHAS to be inhibited by branched-chain amino acids, structures of catalytic and regulatory subunits, sequence comparisons, overview
additional information
the regulatory subunit possesses no AHAS activity but greatly stimulates the activity of the catalytic subunit, it is necessary for AHAS to be inhibited by branched-chain amino acids, structures of catalytic and regulatory subunits, sequence comparisons, overview
additional information
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the regulatory subunit possesses no AHAS activity but greatly stimulates the activity of the catalytic subunit, it is necessary for AHAS to be inhibited by branched-chain amino acids, structures of catalytic and regulatory subunits, sequence comparisons, overview
additional information
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N-terminal sequence analysis
additional information
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N-terminal sequence analysis
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additional information
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the enzyme consists of two diffrent types of subunits, a catalytic one and a regulatory one
additional information
the enzyme is comprised of two subunits: a large catalytic subunit and asmall regulatory one
additional information
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the enzyme consists of two diffrent types of subunits, a catalytic one and a regulatory one
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additional information
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the enzyme is comprised of two subunits: a large catalytic subunit and asmall regulatory one
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additional information
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the regulatory subunit possesses no AHAS activity but greatly stimulates the activity of the catalytic subunit, it is necessary for AHAS to be inhibited by branched-chain amino acids, structures of catalytic and regulatory subunits, sequence comparisons, overview
additional information
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the regulatory subunit possesses no AHAS activity but greatly stimulates the activity of the catalytic subunit, it is necessary for AHAS to be inhibited by branched-chain amino acids, structures of catalytic and regulatory subunits, sequence comparisons, overview
additional information
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the enzyme has a catalytic subunit and a regulatory subunit, encoded by two different genes
additional information
the enzyme has a catalytic subunit and a regulatory subunit, encoded by two different genes
additional information
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the enzyme has a catalytic subunit and a regulatory subunit, encoded by two different genes
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additional information
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heterotetrameric enzyme composed of a small, regulatory and a large, catalytic subunit
additional information
the regulatory subunit possesses no AHAS activity but greatly stimulates the activity of the catalytic subunit, it is necessary for AHAS to be inhibited by branched-chain amino acids, structures of catalytic and regulatory subunits, sequence comparisons, overview
additional information
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the regulatory subunit possesses no AHAS activity but greatly stimulates the activity of the catalytic subunit, it is necessary for AHAS to be inhibited by branched-chain amino acids, structures of catalytic and regulatory subunits, sequence comparisons, overview
additional information
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the regulatory subunit possesses no AHAS activity but greatly stimulates the activity of the catalytic subunit, it is necessary for AHAS to be inhibited by branched-chain amino acids, structures of catalytic and regulatory subunits, sequence comparisons, overview
additional information
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the enzyme consists of a catalytic and a regulatory subunit
additional information
the enzyme consists of a catalytic and a regulatory subunit
additional information
the enzyme consists of a catalytic and a regulatory subunit