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ACPK Sale

目录号 : GC35241

ACPK 是一种吡咯赖氨酸类似物,具有叠氮残基。

ACPK Chemical Structure

Cas No.:1304056-21-0

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Sample solution is provided at 25 µL, 10mM.

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产品描述

ACPK is a pyrrolysine analogue bearing an azide residue.

[1]. Yang M, et al. Biocompatible click chemistry enabled compartment-specific pH measurement inside E. coli. Nat Commun. 2014 Sep 19;5:4981.

Chemical Properties

Cas No. 1304056-21-0 SDF
Canonical SMILES N[C@@H](CCCCNC(O[C@H]1[C@H](N=[N+]=[N-])CCC1)=O)C(O)=O
分子式 C12H21N5O4 分子量 299.33
溶解度 Soluble in DMSO 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。
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。

溶解性数据

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1 mg 5 mg 10 mg
1 mM 3.3408 mL 16.704 mL 33.4079 mL
5 mM 0.6682 mL 3.3408 mL 6.6816 mL
10 mM 0.3341 mL 1.6704 mL 3.3408 mL
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动物体内配方计算器 (澄清溶液)

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Research Update

Natural Gas Storage Filled with Peat-Derived Carbon Adsorbent: Influence of Nonisothermal Effects and Ethane Impurities on the Storage Cycle

Nanomaterials (Basel) 2022 Nov 18;12(22):4066.PMID:36432352DOI:10.3390/nano12224066.

Adsorbed natural gas (ANG) is a promising solution for improving the safety and storage capacity of low-pressure gas storage systems. The structural-energetic and adsorption properties of active carbon ACPK, synthesized from cheap peat raw materials, are presented. Calculations of the methane-ethane mixture adsorption on ACPK were performed using the experimental adsorption isotherms of pure components. It is shown that the accumulation of ethane can significantly increase the energy capacity of the ANG storage. Numerical molecular modeling of the methane-ethane mixture adsorption in slit-like model micropores has been carried out. The molecular effects associated with the displacement of ethane by methane molecules and the formation of a molecule layered structure are shown. The integral molecular adsorption isotherm of the mixture according to the molecular modeling adequately corresponds to the ideal adsorbed solution theory (IAST). The cyclic processes of gas charging and discharging from the ANG storage based on the ACPK are simulated in three modes: adiabatic, isothermal, and thermocontrolled. The adiabatic mode leads to a loss of 27-33% of energy capacity at 3.5 MPa compared to the isothermal mode, which has a 9.4-19.5% lower energy capacity compared to the thermocontrolled mode, with more efficient desorption of both methane and ethane.

Evidence of a "new" allele of red cell and phosphatase ACPK

Forensic Sci Int 1984 Nov;26(3):163-7.PMID:6595186DOI:10.1016/0379-0738(84)90214-7.

Phenotypes of members of one Polish family have revealed a "new" allele in the AcP system: called ACPK. Quantitative data of the phenotypes are given.

4'-phosphopantetheine transfer in primary and secondary metabolism of Bacillus subtilis

J Biol Chem 2001 Oct 5;276(40):37289-98.PMID:11489886DOI:10.1074/jbc.M103556200.

4'-Phosphopantetheine transferases (PPTases) transfer the 4'-phosphopantetheine moiety of coenzyme A onto a conserved serine residue of acyl carrier proteins (ACPs) of fatty acid and polyketide synthases as well as peptidyl carrier proteins (PCPs) of nonribosomal peptide synthetases. This posttranslational modification converts ACPs and PCPs from their inactive apo into the active holo form. We have investigated the 4'-phosphopantetheinylation reaction in Bacillus subtilis, an organism containing in total 43 ACPs and PCPs but only two PPTases, the acyl carrier protein synthase AcpS of primary metabolism and Sfp, a PPTase of secondary metabolism associated with the nonribosomal peptide synthetase for the peptide antibiotic surfactin. We identified and cloned ydcB encoding AcpS from B. subtilis, which complemented an Escherichia coli acps disruption mutant. B. subtilis AcpS and its substrate ACP were biochemically characterized. AcpS also modified the d-alanyl carrier protein but failed to recognize PCP and an acyl carrier protein of secondary metabolism discovered in this study, designated ACPK, that was not identified by the Bacillus genome project. On the other hand, Sfp was able to modify in vitro all acyl carrier proteins tested. We thereby extend the reported broad specificity of this enzyme to the homologous ACP. This in vitro cross-interaction between primary and secondary metabolism was confirmed under physiological in vivo conditions by the construction of a ydcB deletion in a B. subtilis sfp(+) strain. The genes coding for Sfp and its homolog Gsp from Bacillus brevis could also complement the E. coli acps disruption. These results call into question the essential role of AcpS in strains that contain a Sfp-like PPTase and consequently the suitability of AcpS as a microbial target in such strains.

Accumulated creatine phosphokinase release as a prognostic index in the course of acute myocardial infarction

Cor Vasa 1979;21(1):1-7.PMID:477327doi

Accumulated creatine phosphokinase (ACPK) in 25 patients with acute transmural myocardial infarction (MI) was evaluated as a prognostic criterion of clinical severity of the disease. It has been shown that ACPK values above 2.5U/ml are observed in 91.7% in MI complicated by pump failure. This does not apply to repeated MI. The possibility of mathematical estimation of the course of CPK release was also verified. The contribution of this method for the clinician is discussed.

Convergence of isoprene and polyketide biosynthetic machinery: isoprenyl-S-carrier proteins in the pksX pathway of Bacillus subtilis

Proc Natl Acad Sci U S A 2006 Jun 13;103(24):8977-82.PMID:16757561DOI:10.1073/pnas.0603148103.

The pksX gene cluster from Bacillus subtilis is predicted to encode the biosynthesis of an as yet uncharacterized hybrid nonribosomal peptide/polyketide secondary metabolite. We used a combination of biochemical and mass spectrometric techniques to assign functional roles to the proteins ACPK, PksC, PksL, PksF, PksG, PksH, and PksI, and we conclude that they act to incorporate an acetate-derived beta-methyl branch on an acetoacetyl-S-carrier protein and ultimately generate a Delta(2)-isoprenyl-S-carrier protein. This work highlights the power of mass spectrometry to elucidate the functions of orphan biosynthetic enzymes, and it details a mechanism by which single-carbon beta-branches can be inserted into polyketide-like structures. This pathway represents a noncanonical route to the construction of prenyl units and serves as a prototype for the intersection of isoprenoid and polyketide biosynthetic manifolds in other natural product biosynthetic pathways.