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dimer or hexamer
x * 57000, recombinant enzyme, SDS-PAGE
trimer
and dimer and hexamer, 3 * 60000, SDS-PAGE
?
-
x * 52600, recombinant His6-tagged BceC, SDS-PAGE
?
-
x * 52600, recombinant His6-tagged BceC, SDS-PAGE
-
?
x * 56300, calculated, x * 60000, SDS-PAGE
?
-
x * 56300, calculated, x * 60000, SDS-PAGE
-
?
-
x * 62869, calculated from sequence
?
x * 53100, deduced from gene sequence
?
Saccharum spp.
-
x * 52000, SDS-PAGE
?
-
x * 48500, SDS-PAGE and calculated for His-tagged protein
?
x * 48500, recombinant His6-tagged enzyme, SDS-PaGE, x * 47200, native enzyme, SDS-PAGE
?
-
x * 48500, recombinant His6-tagged enzyme, SDS-PaGE, x * 47200, native enzyme, SDS-PAGE
-
?
x * 48200, about, sequence calculation
?
-
x * 48200, about, sequence calculation
-
?
x * 42000, SDS-PAGE, x * 43400, calculated
?
-
x * 42000, SDS-PAGE, x * 43400, calculated
-
dimer
-
2 * 44000, SDS-PAGE
dimer
-
2 * 47000, SDS-PAGE
dimer
2 * 47000, about, SDS-PAGE
dimer
-
2 * 47000, about, SDS-PAGE
-
dimer
-
2 * 57000, mutant A222Q/S233G and part of wild-type, SDS-PAGE
dimer
and trimer and hexamer, 2 * 60000, SDS-PAGE
dodecamer
12 * 47000, about, SDS-PAGE
dodecamer
-
12 * 47000, about, SDS-PAGE
-
dodecamer
12 * 47000, about, SDS-PAGE
dodecamer
-
12 * 47000, about, SDS-PAGE
-
hexamer
-
6 * 52000, at pH 5.5-7.8, equilibrium measurement under native and denaturing conditions
hexamer
-
6 * 52000, gel filtration
hexamer
-
6 * 50000, SDS-PAGE
hexamer
6 * 57000, SDS-PAGE
hexamer
6 x 57000, SDS-PAGE
hexamer
-
6* 57000, wild-type, plus some dimer and monomer, SDS-PAGE
hexamer
and dimer and trimer, 6 * 60000, SDS-PAGE
homodimer
recombinant form of Ugd(BCAL2946)
homodimer
recombinant form of Ugd(BCAM0855)
monomer
-
1 * 55000, SDS-PAGE
monomer
-
1 * 57000, SDS-PAGE, minor part of wild-type, major part is hexamer
monomer
1 * 50000, SDS-PAGE
monomer
-
1 * 45500, SDS-PAGE
tetramer
-
-
tetramer
-
4 * 70000, gel filtration after treatment with SDS
additional information
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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
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
additional information
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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
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
-
additional information
sequence and structure comparison of UDP-glucose dehydrogenase AglM from Haloferax volcanii and VNG1048G from Halobacterium salinarum, homology modelling, overview
additional information
-
sequence and structure comparison of UDP-glucose dehydrogenase AglM from Haloferax volcanii and VNG1048G from Halobacterium salinarum, homology modelling, overview
additional information
-
sequence and structure comparison of UDP-glucose dehydrogenase AglM from Haloferax volcanii and VNG1048G from Halobacterium salinarum, homology modelling, overview
-
additional information
identification of amino acids I7 through T19 as NAD+ binding-site by photoaffinity labeling with nicotinamide 2-azidoadenosine dinucleotide
additional information
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identification of amino acids I7 through T19 as NAD+ binding-site by photoaffinity labeling with nicotinamide 2-azidoadenosine dinucleotide
additional information
significant amount of dimeric and monomeric species can be detected
additional information
-
significant amount of dimeric and monomeric species can be detected
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
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
additional information
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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
-