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39614-17-0

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39614-17-0 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 39614-17-0 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 3,9,6,1 and 4 respectively; the second part has 2 digits, 1 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 39614-17:
(7*3)+(6*9)+(5*6)+(4*1)+(3*4)+(2*1)+(1*7)=130
130 % 10 = 0
So 39614-17-0 is a valid CAS Registry Number.

39614-17-0Relevant articles and documents

Synthesis and biological evaluation of a novel series of curcumin-peptide derivatives as PepT1-mediated transport drugs

Zhang, Jiyun,Wen, Hongmei,Shen, Fei,Wang, Xinzhi,Shan, Chenxiao,Chai, Chuan,Liu, Jian,Li, Wei

, (2019)

Curcumin (CUR) is a natural yellow pigment from turmeric with extensive bioactivities. However its relatively poor solubility limited its absorption and bioavailability. In this study, a novel series of CUR-peptide conjugates were designed and synthesized

Bispidine as a helix inducing scaffold: Examples of helically folded linear peptides

Haridas,Sadanandan, Sandhya,Gopalakrishna,Bijesh,Verma, Ram. P.,Chinthalapalli, Srinivas,Shandilya, Ashutosh

, p. 10980 - 10982 (2013/11/19)

We designed and synthesized bispidine-anchored peptides and showed that these peptides as small as B3 (containing four chiral α-amino acid residues) adopt a right handed helical conformation. Bispidine anchored linear peptide B3 adopts a helical conformat

A novel L-amino acid ligase from bacillus subtilis NBRC3134 catalyzed oligopeptide synthesis

Kino, Kuniki,Arai, Toshinobu,Tateiwa, Daisuke

experimental part, p. 129 - 134 (2010/04/24)

L-Amino acid ligase catalyzes dipeptide synthesis from unprotected L-amino acids in an ATP-dependent manner. We have purified a new L-amino acid ligase, RizA, which synthesizes dipeptides whose N-terminus is Arg, from Bacillus subtilis NBRC3134, a microorganism that produces a rhizocticin peptide antibiotic. It was suggested that RizA is probably involved in rhizocticin biosynthesis. In this study, we performed sequence analysis of unknown regions around rizA, and newly identified a gene that encodes a protein that possesses an ATP-grasp motif upstream of rizA. This gene was designated rizB, and its recombinant protein was prepared. Recombinant RizB synthesized homo-oligo-mers of branched-chain L-amino acids and L-methionine consisting of two to five amino acids in an ATP-dependent manner. RizB also synthesized various heteropeptides. Further examination showed that RizB might elongate a peptide chain at the N-terminus. This is the first report on an L-amino acid ligase catalyzing oligopeptide synthesis.

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