Aminoacetone (hydrochloride)
(Synonyms: 氨基丙酮盐酸盐) 目录号 : GC42786
A catabolite of threonine and glycine
Cas No.:7737-17-9
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >95.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
Aminoacetone is a threonine and glycine catabolite that can be converted to methylglyoxal by amine oxidases. It has been identified as one of several endogenous sources of methylglyoxal found in the plasma of diabetes patients. As a pro-oxidant, 0.10-5 mM aminoacetone can induce cell death in RINm5f pancreatic β-cells. Aminoacetone is used as a growth substrate for Pseudomonas.
| Cas No. | 7737-17-9 | SDF | |
| 别名 | 氨基丙酮盐酸盐 | ||
| Canonical SMILES | CC(CN)=O.Cl | ||
| 分子式 | C3H7NO•HCl | 分子量 | 109.6 |
| 溶解度 | DMF: 25 mg/ml,DMSO: 15 mg/ml,Ethanol: 10 mg/ml,PBS (pH 7.2): 10 mg/ml | 储存条件 | Store at -20°C |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 储备液的保存方式和期限：-80°C 储存时，请在 6 个月内使用，-20°C 储存时，请在 1 个月内使用。 为了提高溶解度，请将管子加热至37℃，然后在超声波浴中震荡一段时间。 |
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| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 制备储备液 | |||
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1 mg | 5 mg | 10 mg |
| 1 mM | 9.1241 mL | 45.6204 mL | 91.2409 mL |
| 5 mM | 1.8248 mL | 9.1241 mL | 18.2482 mL |
| 10 mM | 0.9124 mL | 4.562 mL | 9.1241 mL |
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
| 第二步：请输入动物体内配方组成（配方适用于不溶于水的药物；不同批次药物配方比例不同，请联系GLPBIO为您提供正确的澄清溶液配方） | ||||||||||
| % DMSO % % Tween 80 % saline | ||||||||||
| 计算重置 | ||||||||||
计算结果:
工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
一定要按照顺序依次将溶剂加入，进行下一步操作之前必须保证上一步操作得到的是澄清的溶液，可采用涡旋、超声或水浴加热等物理方法助溶。
3. 以上所有助溶剂都可在 GlpBio 网站选购。
Ferricytochrome (c) directly oxidizes Aminoacetone to methylglyoxal, a catabolite accumulated in carbonyl stress
PLoS One 2013;8(3):e57790.PMID:23483930DOI:10.1371/journal.pone.0057790.
Age-related diseases are associated with increased production of reactive oxygen and carbonyl species such as methylglyoxal. Aminoacetone, a putative threonine catabolite, is reportedly known to undergo metal-catalyzed oxidation to methylglyoxal, NH4(+) ion, and H2O2 coupled with (i) permeabilization of rat liver mitochondria, and (ii) apoptosis of insulin-producing cells. Oxidation of Aminoacetone to methylglyoxal is now shown to be accelerated by ferricytochrome c, a reaction initiated by one-electron reduction of ferricytochrome c by Aminoacetone without amino acid modifications. The participation of O2(•-) and HO (•) radical intermediates is demonstrated by the inhibitory effect of added superoxide dismutase and Electron Paramagnetic Resonance spin-trapping experiments with 5,5'-dimethyl-1-pyrroline-N-oxide. We hypothesize that two consecutive one-electron transfers from Aminoacetone (E0 values = -0.51 and -1.0 V) to ferricytochrome c (E0 = 0.26 V) may lead to Aminoacetone enoyl radical and, subsequently, imine Aminoacetone, whose hydrolysis yields methylglyoxal and NH4(+) ion. In the presence of oxygen, Aminoacetone enoyl and O2(•-) radicals propagate Aminoacetone oxidation to methylglyoxal and H2O2. These data endorse the hypothesis that Aminoacetone, putatively accumulated in diabetes, may directly reduce ferricyt c yielding methylglyoxal and free radicals, thereby triggering redox imbalance and adverse mitochondrial responses.
Oxidative DNA damage induced by Aminoacetone, an amino acid metabolite
Arch Biochem Biophys 1999 May 1;365(1):62-70.PMID:10222039DOI:10.1006/abbi.1999.1161.
We investigated DNA damage induced by Aminoacetone, a metabolite of threonine and glycine. Pulsed-field gel electrophoresis revealed that Aminoacetone caused cellular DNA cleavage. Aminoacetone increased the amount of 8-oxo-7,8-dihydro-2'-deoxyguanosine (8-oxodG) in human cultured cells in a dose-dependent manner. The formation of 8-oxodG in calf thymus DNA increased due to Aminoacetone only in the presence of Cu(II). DNA ladder formation was observed at higher concentrations of Aminoacetone than those causing DNA cleavage. Flow cytometry showed that Aminoacetone enhanced the generation of hydrogen peroxide (H2O2) in cultured cells. Aminoacetone caused damage to 32P-5'-end-labeled DNA fragments, obtained from the human c-Ha-ras-1 and p53 genes, at cytosine and thymine residues in the presence of Cu(II). Catalase and bathocuproine inhibited DNA damage, suggesting that H2O2 and Cu(I) were involved. Analysis of the products generated from Aminoacetone revealed that Aminoacetone underwent Cu(II)-mediated autoxidation in two different pathways: the major pathway in which methylglyoxal and NH+4 are generated and the minor pathway in which 2,5-dimethylpyrazine is formed through condensation of two molecules of Aminoacetone. These findings suggest that H2O2 generated by the autoxidation of Aminoacetone reacts with Cu(I) to form reactive species capable of causing oxidative DNA damage.
Aminoacetone oxidase from Streptococcus oligofermentans belongs to a new three-domain family of bacterial flavoproteins
Biochem J 2014 Dec 15;464(3):387-99.PMID:25269103DOI:10.1042/BJ20140972.
The aaoSo gene from Streptococcus oligofermentans encodes a 43 kDa flavoprotein, Aminoacetone oxidase (SoAAO), which was reported to possess a low catalytic activity against several different L-amino acids; accordingly, it was classified as an L-amino acid oxidase. Subsequently, SoAAO was demonstrated to oxidize Aminoacetone (a pro-oxidant metabolite), with an activity ~25-fold higher than the activity displayed on L-lysine, thus lending support to the assumption of Aminoacetone as the preferred substrate. In the present study, we have characterized the SoAAO structure-function relationship. SoAAO is an FAD-containing enzyme that does not possess the classical properties of the oxidase/dehydrogenase class of flavoproteins (i.e. no flavin semiquinone formation is observed during anaerobic photoreduction as well as no reaction with sulfite) and does not show a true L-amino acid oxidase activity. From a structural point of view, SoAAO belongs to a novel protein family composed of three domains: an α/β domain corresponding to the FAD-binding domain, a β-domain partially modulating accessibility to the coenzyme, and an additional α-domain. Analysis of the reaction products of SoAAO on Aminoacetone showed 2,5-dimethylpyrazine as the main product; we propose that condensation of two Aminoacetone molecules yields 3,6-dimethyl-2,5-dihydropyrazine that is subsequently oxidized to 2,5-dimethylpyrazine. The ability of SoAAO to bind two molecules of the substrate analogue O-methylglycine ligand is thought to facilitate the condensation reaction. A specialized role for SoAAO in the microbial defence mechanism related to Aminoacetone catabolism through a pathway yielding dimethylpyrazine derivatives instead of methylglyoxal can be proposed.
Interaction between L-threonine dehydrogenase and Aminoacetone synthetase and mechanism of Aminoacetone production
J Biol Chem 1986 Dec 15;261(35):16428-37.PMID:3536927doi
A mixture of threonine dehydrogenase and Aminoacetone synthetase will catalyze the conversion of L-threonine to glycine. The overall reaction likely involves the conversion of L-threonine, NAD+, and CoA to glycine, NADH, and acetyl-CoA. Physical separation of L-threonine dehydrogenase from Aminoacetone synthetase results in the formation of Aminoacetone and CO2 from their substrates. A physical interaction between threonine dehydrogenase and Aminoacetone synthetase has been demonstrated by gel permeation chromatography and fluorescence polarization. Polarization of fluorescence measurements of threonine dehydrogenase and Aminoacetone synthetase labeled with fluorescein isothiocyanate indicated the formation of a soluble active complex, with an apparent dissociation constant (Kd) of 5-10 nM and an apparent stoichiometry of 2 Aminoacetone synthetase dimers/1 threonine dehydrogenase tetramer. Chemical experiments have identified Aminoacetone as the enzymatic product of L-threonine dehydrogenase acting on L-threonine. These experiments involved trapping pyrrole derivatives, [3H]NaBH4 reduction, and coupling with plasma amine oxidase. Kinetic experiments also showed NADH, CO2, and Aminoacetone to inhibit threonine dehydrogenase in a manner consistent with an ordered Bi-Ter kinetic mechanism. NAD+ is the lead substrate followed by threonine, and the products are released in the order: CO2, Aminoacetone, and NADH.
Aerobic co-oxidation of hemoglobin and Aminoacetone, a putative source of methylglyoxal
Free Radic Biol Med 2021 Apr;166:178-186.PMID:33636334DOI:10.1016/j.freeradbiomed.2021.02.023.
Aminoacetone (1-aminopropan-2-one), a putative minor biological source of methylglyoxal, reacts like other α-aminoketones such as 6-aminolevulinic acid (first heme precursor) and 1,4-diaminobutanone (a microbicide) yielding electrophilic α-oxoaldehydes, ammonium ion and reactive oxygen species by metal- and hemeprotein-catalyzed aerobic oxidation. A plethora of recent reports implicates triose phosphate-generated methylglyoxal in protein crosslinking and DNA addition, leading to age-related disorders, including diabetes. Importantly, methylglyoxal-treated hemoglobin adds four water-exposed arginine residues, which may compromise its physiological role and potentially serve as biomarkers for diabetes. This paper reports on the co-oxidation of Aminoacetone and oxyhemoglobin in normally aerated phosphate buffer, leading to structural changes in hemoglobin, which can be attributed to the addition of aminoacetone-produced methylglyoxal to the protein. Hydroxyl radical-promoted chemical damage to hemoglobin may also occur in parallel, which is suggested by EPR-spin trapping studies with 5,5-dimethyl-1-pyrroline-N-oxide and ethanol. Concomitantly, oxyhemoglobin is oxidized to methemoglobin, as indicated by characteristic CD spectral changes in the Soret and visible regions. Overall, these findings may contribute to elucidate the molecular mechanisms underlying human diseases associated with hemoglobin dysfunctions and with Aminoacetone in metabolic alterations related to excess glycine and threonine.