2.2.1.6 ? 3 major bands detected by SDS-PAGE: 26000 Da, 35000 Da and 46000 Da -, 395919 2.2.1.6 ? x * 11000 + x * 60000 395917 2.2.1.6 ? x * 15000 + x * 57000 + x * 58000, SDS-PAGE 395908 2.2.1.6 ? x * 16200 + x * 67200, SDS-PAGE 395904 2.2.1.6 ? x * 17500 + x * 61800, calculation from nucleotide sequence 395901 2.2.1.6 ? x * 20000, SDS-PAGE 719375 2.2.1.6 ? x * 48000, deduced from gene sequence 660189 2.2.1.6 ? x * 58000, SDS-PAGE with urea 395910 2.2.1.6 ? x * 59200, calculated from amino acid sequence and SDS-PAGE -, 758259 2.2.1.6 ? x * 60000, recombinant enzyme, SDS-PAGE 733744 2.2.1.6 ? x * 60000, SDS-PAGE -, 733547, 733744, 733987 2.2.1.6 ? x * 60200, calculated from amino acid sequence 733744 2.2.1.6 ? x * 62000, SDS-PAGE 395922 2.2.1.6 ? x * 62000, SDS-PAGE, catalytic subunit -, 719329 2.2.1.6 ? x * 63000, SDS-PAGE -, 756209 2.2.1.6 ? x * 63700, recombinant His-tagged catalytic subunit, SDS-PAGE 695852 2.2.1.6 ? x * 64000, mature enzyme, SDS-PAGE 758092 2.2.1.6 ? x * 65000, about, SDS-PAGE and MALDI-TOF spectrometry 676713 2.2.1.6 ? x * 65000, recombinant enzyme, SDS-PAGE 697061 2.2.1.6 ? x * 65000, SDS-PAGE 719117 2.2.1.6 ? x * 68000, about, wild-type and mutant enzyme variants, SDS-PAGE -, 733745 2.2.1.6 ? x * 68000, SDS-PAGE -, 719375, 733745, 733747, 756075 2.2.1.6 ? x * 74000, SDS-PAGE 755711 2.2.1.6 ? x * 9500 + x * 60000, isoenzyme I, SDS-PAGE 395881 2.2.1.6 dimer 1 * 59000-66000, catalytic subunit + 1 * 10000-20000, above, regulatory subunit 700782 2.2.1.6 dimer 1 * 59000-66000, catalytic subunit + 1 * 34000, regulatory subunit 700782 2.2.1.6 dimer 1 * 59000-66000, catalytic subunit + 1 * 50000, above, regulatory subunit 700782 2.2.1.6 dimer 1 * 65497, calculated, 1 * 66400, SDS-PAGE, plus 1 * 2058, calculated, 1 * 22200, SDS-PAGE, catalytic and regulatory subunit, respectively -, 733241 2.2.1.6 dimer 2 * 20508, regulatory subunit, sequence calculation, 2 * 22210, regulatory subunit, SDS-PAGE 733241 2.2.1.6 dimer 2 * 50000, SDS-PAGE, enzyme exists simultaneously as monomer, dimer and trimer -, 658566 2.2.1.6 dimer 2 * 60000, SDS-PAGE 395885 2.2.1.6 dimer 2 * 61000, SDS-PAGE 395902 2.2.1.6 dimer 2 * 63864, ion spray MS analysis 395902 2.2.1.6 dimer 2 * 64000, SDS-PAGE 395912, 395916 2.2.1.6 dimer 2 * 65000 and/or 66000, SDS-PAGE 395907 2.2.1.6 dimer 2 * 65497, catalytic subunit, sequence calculation, 2 * 66398, catalytic subunit, SDS-PAGE 733241 2.2.1.6 dimer 2 * 75000, SDS-PAGE 395915 2.2.1.6 dimer 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 672868 2.2.1.6 heterotetramer 2 * 65497 + 2 * 20508, calculated from amino acid sequence 733241 2.2.1.6 heterotetramer 2 * 66400 + 2 * 22200, SDS-PAGE 733241 2.2.1.6 homodimer - 756700 2.2.1.6 homodimer the enzyme is a homodimer in solution, the crystal structure shows a homotetramer with one noncovalently bound FAD and one thiamine diphosphate per monomer -, 733657 2.2.1.6 homodimer x-ray crystallography 756475 2.2.1.6 homotetramer - -, 733089, 735039, 756700 2.2.1.6 homotetramer in the crystallized form -, 733657 2.2.1.6 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 -, 733658 2.2.1.6 monomer 1 * 50000, SDS-PAGE, enzyme exists simultaneously as monomer, dimer and trimer -, 658566 2.2.1.6 additional information 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 697349 2.2.1.6 additional information 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 675377 2.2.1.6 additional information heterotetrameric enzyme composed of a small, regulatory and a large, catalytic subunit 671854 2.2.1.6 additional information 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 696357 2.2.1.6 additional information N-terminal sequence analysis -, 658566 2.2.1.6 additional information 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 673213 2.2.1.6 additional information the catabolic enzyme form lacks a regulatory subunit 733987 2.2.1.6 additional information the enzyme consists of a catalytic and a regulatory subunit 733241 2.2.1.6 additional information the enzyme consists of two diffrent types of subunits, a catalytic one and a regulatory one -, 672867 2.2.1.6 additional information the enzyme has a catalytic subunit and a regulatory subunit, encoded by two different genes -, 734734 2.2.1.6 additional information the enzyme is comprised of two subunits: a large catalytic subunit and asmall regulatory one -, 733747 2.2.1.6 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 700782 2.2.1.6 multimer x * 63300, large subunit IlvB, plus x * 18700, small subunit IlvN, SDS-PAGE and calculated. 736351 2.2.1.6 oligomer 8 * 15000 + 8 * 60000, SDS-PAGE 395893 2.2.1.6 oligomer x * 68300, recombinant His-tagged catalytic subunit, + x * 20400, recombinant His-tagged regulatory subunit, SDS-PAGE -, 673626 2.2.1.6 tetramer 2 * 9800 + 2 * 59000, SDS-PAGE 395879 2.2.1.6 tetramer 4 * 58000, SDS-PAGE 395897 2.2.1.6 tetramer 4 * 65000, SDS-PAGE, both isoforms 659100 2.2.1.6 tetramer the enzyme consists of a large catalytic and a small regulatory subunit, two copies of which form the enzyme tetramer 733685 2.2.1.6 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 -, 733685 2.2.1.6 trimer 3 * 50000, SDS-PAGE, enzyme exists simultaneously as monomer, dimer and trimer -, 658566 2.2.1.6 trimer 3 * 55000, SDS-PAGE 395918, 657572 2.2.1.6 trimer 3 * 60000, SDS-PAGE 660559