PMID-sentid Pub_year Sent_text compound_name comp_offset prot_official_name organism prot_offset 28199662-4 2017 In Arabidopsis, five PAOs are present, among which AtPAO5 catalyzes the back-conversion of Spm, Therm-Spm, and N1-acetyl-Spm to spermidine. N'-acetylspermine 111-124 polyamine oxidase 5 Arabidopsis thaliana 51-57 21067138-1 2010 The flavoprotein oxidase Fms1 from Saccharomyces cerevisiae catalyzes the oxidation of spermine and N(1)-acetylspermine to yield spermidine and 3-aminopropanal or N-acetyl-3-aminopropanal. N'-acetylspermine 100-119 polyamine oxidase Saccharomyces cerevisiae S288C 25-29 24550437-5 2014 It is also shown that AtPAO5 oxidizes the polyamines spermine, thermospermine, and N(1)-acetylspermine, the latter being the best in vitro substrate of the recombinant enzyme. N'-acetylspermine 83-102 polyamine oxidase 5 Arabidopsis thaliana 22-28 22642831-1 2012 The flavoprotein oxidase Fms1 from Saccharomyces cerevisiae catalyzes the oxidation of spermine and N(1)-acetylspermine to spermidine and 3-aminopropanal or N-acetyl-3-aminopropanal. N'-acetylspermine 100-119 polyamine oxidase Saccharomyces cerevisiae S288C 25-29 15791459-3 2005 hPAO oxidizes N(1)-acetylspermidine (K(m)=2.1 microM, K(cat)=15.0 s(-1)) and has very high affinity for N(1)-acetylspermine (K(m)=0.85 microM, K(cat)=31.7 s(-1)). N'-acetylspermine 104-123 spermine oxidase Homo sapiens 0-4 17362887-5 2007 Our data with 3-AAP, a product of N-acetylspermine and N-acetylspermidine metabolism, indicate that the aldehyde function of aminoaldehydes is insufficient to express toxicity since the free amino group of aminoaldehydes is also required to gain access to lysosomes where their cytotoxic actions are expressed via leakage of cathepsins that compromise mitochondrial integrity. N'-acetylspermine 34-50 serpin family F member 2 Homo sapiens 16-19 12727196-3 2003 Purified PAOh1/SMO oxidizes both spermine (K(m)=1.6 microM) and N(1)-acetylspermine (K(m)=51 microM), but does not oxidize spermidine. N'-acetylspermine 64-83 spermine oxidase Homo sapiens 9-14 15096507-6 2004 SSAT products N(1)-acetylspermidine, N(1)-acetylspermine, and N(1),N(12)-diacetylspermine accumulated intracellularly and extracellularly. N'-acetylspermine 37-56 spermidine/spermine N1-acetyltransferase 1 Homo sapiens 0-4 12803540-4 2003 When transiently transfected into HEK-293 cells, SSAT-1 decreased spermidine and spermine pools by approximately 30%, while, at the same time, significantly increasing putrescine, N (1)-acetylspermidine, N (1)-acetylspermine and N (1), N (12)-diacetylspermine pools. N'-acetylspermine 204-224 spermidine/spermine N1-acetyltransferase 1 Homo sapiens 49-55 12803540-8 2003 By substituting candidate substrates in the enzyme assay, we determined that SSAT-1 shows the substrate preference norspermidine=spermidine>>spermine> N (1)-acetylspermine>putrescine, whereas SSAT-2 shows the preference norspermidine>spermidine=spermine>> N (1)-acetylspermine=putrescine. N'-acetylspermine 160-180 spermidine/spermine N1-acetyltransferase 1 Homo sapiens 77-83 12803540-8 2003 By substituting candidate substrates in the enzyme assay, we determined that SSAT-1 shows the substrate preference norspermidine=spermidine>>spermine> N (1)-acetylspermine>putrescine, whereas SSAT-2 shows the preference norspermidine>spermidine=spermine>> N (1)-acetylspermine=putrescine. N'-acetylspermine 277-297 spermidine/spermine N1-acetyltransferase 1 Homo sapiens 77-83 12660232-10 2003 It was demonstrated definitively that PAO oxidizes N1-acetylspermine to spermidine and 3-acetamidopropanal and that it also oxidizes N1-acetylspermidine to putrescine and 3-acetamidopropanal. N'-acetylspermine 51-68 polyamine oxidase (exo-N4-amino) Mus musculus 38-41 12727196-3 2003 Purified PAOh1/SMO oxidizes both spermine (K(m)=1.6 microM) and N(1)-acetylspermine (K(m)=51 microM), but does not oxidize spermidine. N'-acetylspermine 64-83 smoothened, frizzled class receptor Homo sapiens 15-18 12670477-2 2003 Biochemical characterization of Fms1 shows that it can oxidize spermine, N(1)-acetylspermine, N(1)-acetylspermidine, and N(8)-acetylspermidine, but not spermidine. N'-acetylspermine 73-92 polyamine oxidase Saccharomyces cerevisiae S288C 32-36 12477380-8 2003 Lysates of human PAO cDNA-transfected HEK-293 cells, but not vector-transfected cells, rapidly oxidized N1-acetylspermine to spermidine. N'-acetylspermine 104-121 polyamine oxidase Homo sapiens 17-20 12477380-10 2003 This ranking is identical to that reported for purified PAO and distinctly different from the recently identified spermine oxidase (SMO), which prefers spermine over N1-acetylspermine. N'-acetylspermine 166-183 polyamine oxidase Homo sapiens 56-59 12477380-10 2003 This ranking is identical to that reported for purified PAO and distinctly different from the recently identified spermine oxidase (SMO), which prefers spermine over N1-acetylspermine. N'-acetylspermine 166-183 spermine oxidase Homo sapiens 114-130 12477380-10 2003 This ranking is identical to that reported for purified PAO and distinctly different from the recently identified spermine oxidase (SMO), which prefers spermine over N1-acetylspermine. N'-acetylspermine 166-183 spermine oxidase Homo sapiens 132-135 10917567-9 2000 Hydrogen peroxide and the aldehydes 3-aminopropanal and 3-acetamidopropanal, the products of polyamine oxidase-catalyzed splitting of spermine and N1-acetylspermine, contribute little to spermine cytotoxicity. N'-acetylspermine 147-164 polyamine oxidase Homo sapiens 93-110 10320741-2 1999 Pretreatment with the polyamine oxidase inhibitor MDL72527 caused an accumulation of N1-acetylspermidine and N1-acetylspermine in normal rats. N'-acetylspermine 109-126 polyamine oxidase Rattus norvegicus 22-39 10348665-7 1999 Two compounds, N8-acetyl spermidine and N1-acetyl spermine, were found to protect cells from low K+-induced apoptosis, which has been shown to be p53-independent. N'-acetylspermine 40-58 Wistar clone pR53P1 p53 pseudogene Rattus norvegicus 146-149 9831361-3 1998 METHODS: Polyamine oxidase activity was fluorimetrically measured using N1-acetylspermine as substrate. N'-acetylspermine 72-89 polyamine oxidase Rattus norvegicus 9-26 7554238-2 1995 Pretreatment of 7-day-old rats with the polyamine oxidase inhibitor, MDL 72527, induced a similar accumulation of N-acetylspermidine and N-acetylspermine in control and kainate-treated animals. N'-acetylspermine 137-153 polyamine oxidase Rattus norvegicus 40-57 7560898-8 1995 At the light microscopic level, final reaction product specifically generated by polyamine oxidase activity was found exclusively in a granular form in hepatocytes, epithelial cells of proximal tubules of the kidney, and epithelial cells of duodenal villi with N1-acetylspermidine or N1-acetylspermine as substrates. N'-acetylspermine 284-301 polyamine oxidase Rattus norvegicus 81-98 1989509-5 1991 Purified SSAT had a specific activity of 285 mumol/min/mg for spermidine and Km values of 5.9 microM for acetylcoenzyme A, 55 microM for spermidine, 5 microM for spermine, 36 microM for N1-acetylspermine, 1.6 microM for norspermidine, and 4 microM for norspermine. N'-acetylspermine 186-203 spermidine/spermine N1-acetyltransferase 1 Homo sapiens 9-13 1510731-3 1992 A second enzyme of polyamine back-conversion, murine polyamine oxidase (PAO), was found to be competitively inhibited by pentamidine, with a Ki of 7.6 microM when N-acetylspermine was the substrate. N'-acetylspermine 163-179 polyamine oxidase (exo-N4-amino) Mus musculus 53-70 1510731-3 1992 A second enzyme of polyamine back-conversion, murine polyamine oxidase (PAO), was found to be competitively inhibited by pentamidine, with a Ki of 7.6 microM when N-acetylspermine was the substrate. N'-acetylspermine 163-179 polyamine oxidase (exo-N4-amino) Mus musculus 72-75 1957880-1 1991 The activity of polyamine oxidase in human pregnancy serum was measured by our new specific method with radioisotopic N1-acetylspermine as substrate. N'-acetylspermine 118-135 polyamine oxidase Homo sapiens 16-33 35453845-5 2022 Results: The metabolites N1-acetylspermine (ASP), N8-acetylspermidine (ASD) and N1,N12-diacetylspermine (DAS) were detected at significantly different concentrations in the urine of HNC patients as compared to healthy controls. N'-acetylspermine 25-42 assembly factor for spindle microtubules Homo sapiens 44-47 2221348-1 1990 A new radioisotopic assay for polyamine oxidase with N1-acetylspermine as substrate is presented. N'-acetylspermine 53-70 polyamine oxidase Homo sapiens 30-47 2334396-7 1990 When polyamine oxidase activity in the treated cells was blocked, increases in N1-acetylspermidine and N1-acetylspermine were much greater, and the formation of putrescine was prevented. N'-acetylspermine 103-120 peroxisomal N(1)-acetyl-spermine/spermidine oxidase Cricetulus griseus 5-22 1366693-9 1990 N1-Acetylspermine, which is a good substrate for mammalian PAO, acts as a non-competitive inhibitor for the plant enzyme. N'-acetylspermine 0-17 polyamine oxidase Homo sapiens 59-62 6803078-1 1981 The acetyl derivatives of polyamines, N1-acetylspermine (N1-AcSPM) and N1-acetylspermidine (N1-AcSPD), are in vitro better substrates of tissue polyamine oxidase than the corresponding non-acetylated polyamines. N'-acetylspermine 38-55 polyamine oxidase Rattus norvegicus 144-161 3342402-4 1988 We studied the effects of putrescine, spermidine, 2 lower homologues of spermidine, N1- and N8-acetyl spermidines, spermine, and N1-acetyl spermine on the sedimentation profile and DNA binding of progesterone receptor from rabbit uterus. N'-acetylspermine 129-147 progesterone receptor Oryctolagus cuniculus 196-217 6803078-7 1981 These findings support the concept that N1-acetylspermine and N1-acetylspermidine are natural substrates of tissue polyamine oxidase and suggest poor membrane permeability of monoacetylputrescine (AcPUT) and N1, N12-diacetylspermine. N'-acetylspermine 40-57 polyamine oxidase Rattus norvegicus 115-132 7040832-4 1981 The reaction products N1-acetylspermine and N1-acetylspermidine are substrates of the cytoplasmic polyamine oxidase. N'-acetylspermine 22-39 polyamine oxidase Homo sapiens 98-115