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108761-28-0

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108761-28-0 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 108761-28-0 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,0,8,7,6 and 1 respectively; the second part has 2 digits, 2 and 8 respectively.
Calculate Digit Verification of CAS Registry Number 108761-28:
(8*1)+(7*0)+(6*8)+(5*7)+(4*6)+(3*1)+(2*2)+(1*8)=130
130 % 10 = 0
So 108761-28-0 is a valid CAS Registry Number.

108761-28-0Relevant articles and documents

Synthesis of styryl substituted semicarbazides under microwave irradiation

Chai, Lan-Qin,Zhang, Hong-Song,Liu, Gang,Huang, Jiao-Jiao,Cheng, Qiao-Qiao

, p. 356 - 358 (2013)

A series of styryl substituted semicarbazides were synthesised by reaction of trans-styryl isocyanate, prepared by Curtius rearrangement of cinnamoyl azide, with acid hydrazides under microwave irradiation using a one-pot procedure. The effects of microwa

Benzoic hydroxamate-based iron complexes as model compounds for humic substances: Synthesis, characterization and algal growth experiments

Orlowska, Ewelina,Roller, Alexander,Wiesinger, Hubert,Pignitter, Marc,Jirsa, Franz,Krachler, Regina,Kandioller, Wolfgang,Keppler, Bernhard K.

, p. 40238 - 40249 (2016/05/24)

A series of monomeric and dimeric FeIII complexes bearing benzoic hydroxamates as O,O-chelates has been prepared and characterized by elemental analysis, IR spectroscopy, UV-Vis spectroscopy, electrospray ionization mass spectrometry (ESI-MS), cyclic voltammetry, EPR spectroscopy and for some examples by X-ray diffraction analysis. The stability of the synthesized complexes in pure water and seawater was monitored over 24 h by means of UV-Vis spectrometry. The ability to release iron from the synthesized model complexes has been investigated with algae growth experiments.

Screening and Engineering the Synthetic Potential of Carboxylating Reductases from Central Metabolism and Polyketide Biosynthesis

Peter, Dominik M.,Schada Von Borzyskowski, Lennart,Kiefer, Patrick,Christen, Philipp,Vorholt, Julia A.,Erb, Tobias J.

supporting information, p. 13457 - 13461 (2015/11/09)

Carboxylating enoyl-thioester reductases (ECRs) are a recently discovered class of enzymes. They catalyze the highly efficient addition of CO2 to the double bond of α,β-unsaturated CoA-thioesters and serve two biological functions. In primary metabolism of many bacteria they produce ethylmalonyl-CoA during assimilation of the central metabolite acetyl-CoA. In secondary metabolism they provide distinct α-carboxyl-acyl-thioesters to vary the backbone of numerous polyketide natural products. Different ECRs were systematically assessed with a diverse library of potential substrates. We identified three active site residues that distinguish ECRs restricted to C4 and C5-enoyl-CoAs from highly promiscuous ECRs and successfully engineered a selected ECR as proof-of-principle. This study defines the molecular basis of ECR reactivity, allowing for predicting and manipulating a key reaction in natural product diversification.

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