Zobrazeno 1 - 3
of 3
pro vyhledávání: '"Kathrin Gasow"'
Autor:
Andrea Preusser-Kunze, Kathrin Gasow, Thomas Dierks, Bernhard Schmidt, Dirk Roeser, Kurt von Figura, Julia G. Wittmann, Markus G. Rudolph
Publikováno v:
Proceedings of the National Academy of Sciences. 103:81-86
The formylglycine (FGly)-generating enzyme (FGE) uses molecular oxygen to oxidize a conserved cysteine residue in all eukaryotic sulfatases to the catalytically active FGly. Sulfatases degrade and remodel sulfate esters, and inactivity of FGE results
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::36829f005204dc2c542efeabfeb85f1f
https://doi.org/10.1073/pnas.0507592102
https://doi.org/10.1073/pnas.0507592102
Autor:
Julia G. Wittmann, Daniel Heinrich, Ulf Diederichsen, Kathrin Gasow, Alexandra Frey, Markus G. Rudolph
Publikováno v:
Structure (London, England : 1993). 16(1)
SummaryUMP synthase (UMPS) catalyzes the last two steps of de novo pyrimidine nucleotide synthesis and is a potential cancer drug target. The C-terminal domain of UMPS is orotidine-5′-monophosphate decarboxylase (OMPD), a cofactor-less yet extremel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e4da2d26fc962db46e977f78247b82a3
https://pubmed.ncbi.nlm.nih.gov/18184586
https://pubmed.ncbi.nlm.nih.gov/18184586
Publikováno v:
Acta crystallographica. Section D, Biological crystallography. 61(Pt 8)
Sulfatases are a family of enzymes essential for the degradation of sulfate esters. Formylglycine is the key catalytic residue in the active site of sulfatases and is generated from a cysteine residue by FGE, the formylglycine-generating enzyme. Inac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4a67d9940ea0e9e261e384d4db4589b2
https://pubmed.ncbi.nlm.nih.gov/16041070
https://pubmed.ncbi.nlm.nih.gov/16041070