PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 497352-0 1979 Theoretical drug design: 6-azauridine-5"-phosphate--its X-ray crystal structure, potential energy maps, and mechanism of inhibition of orotidine-5"-phosphate decarboxylase. 6-azauridine-5'-monophosphate 25-50 uridine monophosphate synthetase Homo sapiens 135-171 3680222-7 1987 Preliminary characterization of the human placental UMP synthase showed it to be similar to UMP synthase from the Ehrlich ascites carcinoma in subunit molecular weight, native molecular weight, isozyme pattern (although not absolute pI values), pH optima of enzymatic activities, and kinetic constants for orotidine 5"-monophosphate (Km) and 6-azauridine 5"-monophosphate (Ki) at the decarboxylase site. 6-azauridine-5'-monophosphate 342-371 uridine monophosphate synthetase Homo sapiens 52-64 7006681-0 1980 Inhibition of orotidine-5"-phosphate decarboxylase by 1-(5"-phospho-beta-d-ribofuranosyl)barbituric acid, 6-azauridine 5"-phosphate, and uridine 5"-phosphate. 6-azauridine-5'-monophosphate 106-131 uridine monophosphate synthetase Homo sapiens 14-50 2475503-7 1989 These data suggest that the detrimental deficiency of this one patient results from a structurally altered UMP synthase that is probably present in low steady-state amounts due to proteolysis and that this labile protein can be stabilized against heat denaturation and proteolytic degradation by 6-aza-UMP. 6-azauridine-5'-monophosphate 296-305 uridine monophosphate synthetase Homo sapiens 107-119