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methyl 4-acetylquinoline-2-carboxylate is a chemical with a specific purpose. Lookchem provides you with multiple data and supplier information of this chemical.

150147-06-1

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150147-06-1 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 150147-06-1 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,5,0,1,4 and 7 respectively; the second part has 2 digits, 0 and 6 respectively.
Calculate Digit Verification of CAS Registry Number 150147-06:
(8*1)+(7*5)+(6*0)+(5*1)+(4*4)+(3*7)+(2*0)+(1*6)=91
91 % 10 = 1
So 150147-06-1 is a valid CAS Registry Number.

150147-06-1Relevant academic research and scientific papers

Discovery and efficient synthesis of a biologically active alkaloid inspired by thiostrepton biosynthesis

Zheng, Qingfei,Wang, Shoufeng,Liu, Wen

, p. 7686 - 7690 (2014/12/10)

Thiostrepton, a natural peptide macrocycle, is of great interest due to its structural complexity and numerous biological activities, including anti-bacterial, anti-tumor, and anti-plasmodial activities. The quinaldic acid (QA) moiety-containing side ring (loop 2) was proven to play an important role in carrying out these functions. Previously, we proposed biosynthetic logic for thiostrepton loop 2 and demonstrated the formation mechanism of QA. Herein, we report the discovery and efficient synthesis of a biologically active alkaloid, that is, a key intermediate involved in the thiostrepton biosynthetic pathway. A chemo-enzymatic method was performed to synthesize the molecule, and a series of analogs were prepared for bioassays, which included the examination of anti-bacterial and anti-tumor activities.

Synthetic studies on thiostrepton family of peptide antibiotics: Synthesis of the dihydroquinoline portion of thiostrepton, the siomycins, and the thiopeptins

Mori, Tomonori,Satouchi, Yukiko,Tohmiya, Hiraku,Higashibayashi, Shuhei,Hashimoto, Kimiko,Nakata, Masaya

, p. 6417 - 6422 (2007/10/03)

Synthesis of the dihydroquinoline portion of thiostrepton, the siomycins, and the thiopeptins, members of the thiostrepton family of peptide antibiotics, has been achieved featuring the one-pot olefination via the Matsumura- Boekelheide rearrangement "using trifluoromethanesulfonic anhydride and triethylamine" and the stereoselective addition reaction controlled by the stereocenter of the peri-position.

Studies on the biosynthesis of thiostrepton: 4-(1- hydroxyethyl)quinoline-2-carboxylate as a free intermediate on the pathway to the quinaldic acid moiety

Priestley, Nigel D.,Smith, Todd M.,Shipley, Paul R.,Floss, Heinz G.

, p. 1135 - 1147 (2007/10/03)

Specifically 13C-labeled quinoline-2-carboxylate derivatives were synthesized from quinoline and used to study the biosynthesis of thiostrepton in a strain of Streptomyces laurentii. 13C NMR analysis of thiostrepton recovered after feeding methyl (RS)-[11-13C]-4-(1-hydroxyethyl)quinoline- 2-carboxylate or methyl [11-13C]-4-acetylquinoline-2-carboxylate showed conclusively that these compounds are specifically and efficiently incorporated into thiostrepton. Both compounds were also detected in cultures of the producing organism by isotope dilution analysis. The significance of the relative endogenous concentrations of the two compounds and of the relative extent of the incorporation of exogenously added labeled material into thiostrepton are discussed in terms of the biosynthetic pathway linking tryptophan and 4-(1-hydroxyethyl)quinoline-2-carboxylate in S. laurentii. A highly specific enzyme activity was detected in cell-free extracts of S. laurentii that was capable of adenylating (12S)-4-(1-hydroxyethyl)quinoline- 2-carboxylic acid. Partial purification of the enzyme was achieved. The enzyme was found to be specific for the enantiomer of the substrate which has the same absolute configuration as found in the natural antibiotic structure. The presence of one specific enzyme catalysing the adenylation process in S. laurentii was shown by photoaffinity labeling with [α-32P]-8-azido-ATP and subsequent SDS PAGE analysis of the labeled products. The native molecular weight of the active enzyme, determined by gel permeation chromatography, was found to be approximately 47 kDa, compared with a denatured weight of 50 kDa estimated for the photoaffinity-labeled protein. The enzyme is thus probably monomeric.

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