| Name | monoamine oxidase |
|---|---|
| Synonyms | Adrenalin oxidase; Amine oxidase; Amine oxidase [flavin containing] B; MAO B; MAOB; Monoamine oxidase; Monoamine oxidase B; Monoamine oxidase type B… |
| Name | acrolein |
|---|---|
| CAS | 2-propenal |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 2332060 | Lea RG, Daya S, Clark DA: Identification of low molecular weight immunosuppressor molecules in human in vitro fertilization supernatants predictive of implantation as a polyamine--possibly Fertil Steril. 1990 May;53(5):875-81. becomes toxic when oxidized by monoamine oxidase to dialdehyde or acrolein. |
32(0,1,1,2) | Details |
| 17362887 | Wood PL, Khan MA, Moskal JR: The concept of load" in neurodegenerative mechanisms: cytotoxicity of the polyamine degradation products peroxide, acrolein, 3-acetamidopropanal and in a retinal ganglion cell line. Brain Res. 2007 May 11;1145:150-6. Epub 2007 Mar 23. The major aldehydes produced by polyamine oxidase and amine oxidases include the 2-alkenal acrolein, the acetoamidoaldehyde 3-acetamidopropanal (3-AAP) and the aminoaldehydes (3-AP) and (4-AB). |
6(0,0,1,1) | Details |
| 8130014 | Houen G, Bock K, Jensen AL: HPLC and NMR investigation of the serum amine oxidase catalyzed oxidation of polyamines. Acta Chem Scand. 1994 Jan;48(1):52-60. These findings were further substantiated by analysis of the reaction products by ion-exchange chromatography and by analysis of the products formed by oxidation of polyamines by the cofactor of Cu amine oxidases, 6-hydroxydopa. is unstable and can give rise to acrolein by beta-elimination. |
32(0,1,1,2) | Details |
| 16225993 | Toninello A, Pietrangeli P, De Marchi U, Salvi M, Mondovi B: Amine oxidases in apoptosis and cancer. Biochim Biophys Acta. 2006 Jan;1765(1):1-13. Epub 2005 Sep 29. The oxidation products of biogenic amines appears to be also carcinogenic, while acrolein, produced from the oxidation of and should be a key compound both carcinogenic and cytotoxic. |
7(0,0,0,7) | Details |
| 7646554 | Meier T, Issels RD: Degradation of 2-(3-aminopropylamino)-ethanethiol (WR-1065) by Cu-dependent amine oxidases and influence on status of Chinese hamster ovary cells. Biochem Pharmacol. 1995 Aug 8;50(4):489-96. Analysis of the degradation products of WR-1065 demonstrates the formation of acrolein and H2O2. |
5(0,0,0,5) | Details |
| 4055794 | Silverman RB, Hiebert CK, Vazquez ML: Inactivation of monoamine oxidase by allylamine does not result in flavin attachment. J Biol Chem. 1985 Nov 25;260(27):14648-52. [1-3H] Allylamine was synthesized by boro [3H] hydride reduction of acrolein followed by direct conversion of the [1-3H] allyl to N-allylphthalimide with triphenylphosphine, diethylazodicarboxylate, and phthalimide. Inactivation of beef liver mitochondrial monoamine oxidase with [1-3H] allylamine led to incorporation of 1-6 eq of inactivator/active site depending upon the length of incubation time. |
3(0,0,0,3) | Details |
| 1540641 | Williams CH, Lawson J, Backwell FR: Inhibition and inactivation of monoamine oxidase by 3-amino-1-phenyl-prop-1-enes. Biochim Biophys Acta. 1992 Feb 26;1119(2):111-7. |
2(0,0,0,2) | Details |
| 4084537 | Yamasaki RB, Silverman RB: Mechanism for reactivation of N-cyclopropylbenzylamine-inactivated monoamine oxidase by amines. Biochemistry. 1985 Nov 5;24(23):6543-50. One involves initial Schiff base formation with the active site adduct produced by N-CBA inactivation of MAO followed by base-catalyzed beta-elimination to the imine of acrolein. |
2(0,0,0,2) | Details |
| 4084536 | Vazquez ML, Silverman RB: Revised mechanism for inactivation of mitochondrial monoamine oxidase by N-cyclopropylbenzylamine. Biochemistry. 1985 Nov 5;24(23):6538-43. Inactivation of MAO by N-[1-3H] CBA results in incorporation of about 3 equiv of tritium into the enzyme and release of [3H] acrolein. |
2(0,0,0,2) | Details |
| 2071588 | Ambroziak W, Pietruszko R: Human aldehyde dehydrogenase. J Biol Chem. 1991 Jul 15;266(20):13011-8. Isoelectric focusing of liver homogenates followed by development with various physiological substrates together with substrate specificity data suggest that aldehyde dehydrogenase (EC 1.2.1.3) is the only enzyme in the human liver capable of catalyzing dehydrogenation of aldehydes arising via monoamine, diamine, and plasma amine oxidases. All isozymes dehydrogenate naturally occurring aldehydes, 5-imidazoleacetaldehyde metabolite) and acrolein (product of beta-elimination of oxidized polyamines) with similar catalytic efficiency. |
1(0,0,0,1) | Details |
| 2728003 | Toraason M, Luken ME, Breitenstein M, Krueger JA, Biagini RE: Comparative toxicity of allylamine and acrolein in cultured myocytes and fibroblasts from neonatal rat heart. Toxicology. 1989 May 31;56(1):107-17. Semicarbazide, a benzylamine oxidase inhibitor, protected myocytes from allylamine toxicity, but clorgyline, a monoamine oxidase inhibitor, was ineffective. |
1(0,0,0,1) | Details |
| 17026969 | Wood PL, Khan MA, Moskal JR, Todd KG, Tanay VA, Baker G: load in ischemia-reperfusion brain injury: neuroprotection by neutralization of reactive aldehydes with phenelzine. Brain Res. 2006 Nov 29;1122(1):184-90. Epub 2006 Oct 5. In ongoing studies of the neuroprotective properties of monoamine oxidase inhibitors, we found that phenelzine provided robust neuroprotection in the gerbil model of transient forebrain ischemia, with drug administration delayed up to 3 h post reperfusion. Both aminoaldehydes and acrolein are generated from the metabolism of polyamines to by polyamine oxidase. |
1(0,0,0,1) | Details |
| 15953813 | Naoi M, Maruyama W, Shamoto-Nagai M, Yi H, Akao Y, Tanaka M: Oxidative stress in mitochondria: decision to survival and death of neurons in neurodegenerative disorders. Mol Neurobiol. 2005;31(1-3):81-93. In mitochondria, oxidative phosphorylation and enzymatic oxidation of biogenic amines by monoamine oxidase produce reactive and species, which are proposed to cause neuronal cell death in neurodegenerative disorders, including Parkinson's and Alzheimer's disease. Rotenone induced mitochondrial dysfunction and accumulation and aggregation of proteins modified with acrolein, an product of lipid peroxidation in the cells. |
1(0,0,0,1) | Details |
| 8920635 | Lyles GA: Mammalian plasma and tissue-bound semicarbazide-sensitive amine oxidases: biochemical, pharmacological and toxicological aspects. Int J Biochem Cell Biol. 1996 Mar;28(3):259-74. Vascular SSAO can metabolize the xenobiotic allylamine, to the cytotoxic acrolein and this has been linked to the ability of allylamine administration to produce cardiovascular lesions in experimental animals, sometimes mimicking features of atherosclerotic disease. A variety of compounds have now been identified as relatively selective inhibitors to distinguish the SSAOs from other amine oxidases, in order to investigate the properties of SSAOs and their potential role in biogenic and xenobiotic amine metabolism in vivo. |
1(0,0,0,1) | Details |
| 9503571 | Pino R, Lyles GA: [Effect of activity of semicarbazide-sensitive aminooxidases and cellular on the cytotoxic effect of allylamine, acrolein, and in human cultured endothelial cells]. Vopr Med Khim. 1997 Nov-Dec;43(6):537-47. |
0(0,0,0,0) | Details |