1.1.1.22 ? ? * 40000, SDS-PAGE 286302 1.1.1.22 ? x * 42000, SDS-PAGE, x * 43400, calculated -, 725276 1.1.1.22 ? x * 43000, SDS-PAGE 666609 1.1.1.22 ? x * 48200, about, sequence calculation -, 739891 1.1.1.22 ? x * 48500, recombinant His6-tagged enzyme, SDS-PaGE, x * 47200, native enzyme, SDS-PAGE -, 739981 1.1.1.22 ? x * 48500, SDS-PAGE and calculated for His-tagged protein 684611 1.1.1.22 ? x * 52000, SDS-PAGE 654351 1.1.1.22 ? x * 52600, recombinant His6-tagged BceC, SDS-PAGE -, 710750 1.1.1.22 ? x * 53100, deduced from gene sequence 654831 1.1.1.22 ? x * 56300, calculated, x * 60000, SDS-PAGE -, 726412 1.1.1.22 ? x * 62869, calculated from sequence 762397 1.1.1.22 dimer 2 * 44000, SDS-PAGE 286305 1.1.1.22 dimer 2 * 47000, about, SDS-PAGE -, 740935 1.1.1.22 dimer 2 * 47000, SDS-PAGE 286292 1.1.1.22 dimer 2 * 57000, mutant A222Q/S233G and part of wild-type, SDS-PAGE 687474 1.1.1.22 dimer 54500, calculated 687559 1.1.1.22 dimer 57400, calculated 687559 1.1.1.22 dimer and trimer and hexamer, 2 * 60000, SDS-PAGE 760577 1.1.1.22 dimer or hexamer x * 57000, recombinant enzyme, SDS-PAGE 740715 1.1.1.22 dodecamer 12 * 47000, about, SDS-PAGE -, 740935 1.1.1.22 hexamer 6 * 50000, SDS-PAGE 725729 1.1.1.22 hexamer 6 * 52000, at pH 5.5-7.8, equilibrium measurement under native and denaturing conditions 286290 1.1.1.22 hexamer 6 * 52000, gel filtration 286306 1.1.1.22 hexamer 6 * 57000, SDS-PAGE 656240 1.1.1.22 hexamer 6 x 57000, SDS-PAGE 656220 1.1.1.22 hexamer 6* 57000, wild-type, plus some dimer and monomer, SDS-PAGE 687474 1.1.1.22 hexamer and dimer and trimer, 6 * 60000, SDS-PAGE 760577 1.1.1.22 homodimer recombinant form of Ugd(BCAL2946) 700059 1.1.1.22 homodimer recombinant form of Ugd(BCAM0855) 700059 1.1.1.22 monomer 1 * 45500, SDS-PAGE 286301 1.1.1.22 monomer 1 * 50000, SDS-PAGE 721871 1.1.1.22 monomer 1 * 55000, SDS-PAGE 657082 1.1.1.22 monomer 1 * 57000, SDS-PAGE, minor part of wild-type, major part is hexamer 687474 1.1.1.22 additional information examination of the dimer-dimer subunit interface reveals an extensive network of charge interactions and hydrogen bonding that coordinately stabilize the hexamer in the presence and absence of its cofactor or substrate, involving residue T325. The wild-type UGDH enzyme purifies in a hexamer-dimer equilibrium and transiently undergoes dynamic motion that exposes the dimer-dimer interface during catalysis. Only dynamic UGDH hexamers support robust cellular function, mutant dimeric species of UGDH have reduced activity in vitro and in supporting hyaluronan production by cultured cells. Molecular interactions at the subunit interface, overview. In the apo form Thr325 directly forms a hydrogen bond with Asp105 of the opposite subunit 740715 1.1.1.22 additional information identification of amino acids I7 through T19 as NAD+ binding-site by photoaffinity labeling with nicotinamide 2-azidoadenosine dinucleotide 656240 1.1.1.22 additional information sequence and structure comparison of UDP-glucose dehydrogenase AglM from Haloferax volcanii and VNG1048G from Halobacterium salinarum, homology modelling, overview -, 740935 1.1.1.22 additional information significant amount of dimeric and monomeric species can be detected 656220 1.1.1.22 additional information structural modelling of the enzyme in complex with NAD and uridine 5'-monophosphate, using structure of Ugd from Klebsiella pneumoniae in complex with UDPGA, PDB ID 3PJG, as template 740710 1.1.1.22 additional information the Rossmann structural motifs found in NAD+-dependent dehydrogenases can have a dual function working as a nucleotide cofactor binding domain and as a ribonuclease -, 739981 1.1.1.22 additional information the specific activity of the VNG1048G dodecamer at 2 M NaCl is only one sixth of that of UDP-glucose dehydrogenase AglM, while the dimer is inactive. The oligomeric status of VNG1048G is affected by lowered salinity. Sequence and structure comparison of UDP-glucose dehydrogenase AglM from Haloferax volcanii and VNG1048G from Halobacterium salinarum, homology modelling, overview -, 740935 1.1.1.22 tetramer - 670814 1.1.1.22 tetramer 4 * 70000, gel filtration after treatment with SDS 286295 1.1.1.22 trimer and dimer and hexamer, 3 * 60000, SDS-PAGE 760577