Any feedback?
Please rate this page
(search_result.php)
(0/150)

BRENDA support

Refine search

Search Subunits

show results
Don't show organism specific information (fast!)
Search organism in taxonomic tree (slow, choose "exact" as search mode, e.g. "mammalia" for rat,human,monkey,...)
(Not possible to combine with the first option)
Refine your search

Search term:

<< < Results 31 - 40 of 43 > >>
download as CSV
download all results as CSV
EC Number Subunits Commentary Reference
Show all pathways known for 1.1.1.22Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.22monomer 1 * 50000, SDS-PAGE 721871
Show all pathways known for 1.1.1.22Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.22monomer 1 * 55000, SDS-PAGE 657082
Show all pathways known for 1.1.1.22Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.22monomer 1 * 57000, SDS-PAGE, minor part of wild-type, major part is hexamer 687474
Show all pathways known for 1.1.1.22Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.22More 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
Show all pathways known for 1.1.1.22Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.22More identification of amino acids I7 through T19 as NAD+ binding-site by photoaffinity labeling with nicotinamide 2-azidoadenosine dinucleotide 656240
Show all pathways known for 1.1.1.22Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.22More sequence and structure comparison of UDP-glucose dehydrogenase AglM from Haloferax volcanii and VNG1048G from Halobacterium salinarum, homology modelling, overview -, 740935
Show all pathways known for 1.1.1.22Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.22More significant amount of dimeric and monomeric species can be detected 656220
Show all pathways known for 1.1.1.22Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.22More 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
Show all pathways known for 1.1.1.22Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.22More 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
Show all pathways known for 1.1.1.22Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.22More 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
<< < Results 31 - 40 of 43 > >>
download as CSV
download all results as CSV