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127658-43-9

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127658-43-9 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 127658-43-9 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,2,7,6,5 and 8 respectively; the second part has 2 digits, 4 and 3 respectively.
Calculate Digit Verification of CAS Registry Number 127658-43:
(8*1)+(7*2)+(6*7)+(5*6)+(4*5)+(3*8)+(2*4)+(1*3)=149
149 % 10 = 9
So 127658-43-9 is a valid CAS Registry Number.

127658-43-9Downstream Products

127658-43-9Relevant articles and documents

Esterase-Catalyzed Siderophore Hydrolysis Activates an Enterobactin-Ciprofloxacin Conjugate and Confers Targeted Antibacterial Activity

Neumann, Wilma,Sassone-Corsi, Martina,Raffatellu, Manuela,Nolan, Elizabeth M.

, p. 5193 - 5201 (2018)

Enteric Gram-negative bacteria, including Escherichia coli, biosynthesize and deploy the triscatecholate siderophore enterobactin (Ent) in the vertebrate host to acquire iron, an essential nutrient. We report that Ent-Cipro, a synthetic siderophore-antibi

Synthesis and biological activity of analogues of vanchrobactin, a siderophore from Vibrio anguillarum serotype O2

Soengas, Raquel G.,Larrosa, Marta,Balado, Miguel,Rodriguez, Jaime,Lemos, Manuel L.,Jimenez, Carlos

experimental part, p. 1278 - 1287 (2008/10/09)

Several analogues of vanchrobactin, a catechol siderophore isolated from the bacterial fish pathogen Vibrio anguillarum serotype O2 strain RV22, have been synthesized. The biological evaluation of these novel compounds showed that most of them are active as siderophores, as determined by growth promotion assays using the producer strain, as well as V. anguillarum serotype O1, Salmonella enterica, and Erwinia chrysanthemi. These compounds also gave a positive chrome azurol-S (CAS) test. On the basis of these results, we were able to deduce some structure-activity relationships. Furthermore, we found an analogue with siderophore activity that has appropriate functionality (an amino group) for use as an antibiotic vector to be employed in a "Trojan horse strategy". This journal is The Royal Society of Chemistry.

Biosynthetic tailoring of microcin E492m: Post-translational modification affords an antibacterial siderophore-peptide conjugate

Nolan, Elizabeth M.,Fischbach, Michael A.,Koglin, Alexander,Walsh, Christopher T.

, p. 14336 - 14347 (2008/09/17)

The present work reveals that four proteins, MceCDIJ, encoded by the MccE492 gene cluster are responsible for the remarkable post-translational tailoring of microcin E492 (MccE492), an 84-residue protein toxin secreted by Klebsiella pneumonaie RYC492 that targets neighboring Gram-negative species. This modification results in attachment of a linearized and monoglycosylated derivative of enterobactin, a nonribosomal peptide and iron scavenger (siderophore), to the MccE492m C-terminus. MceC and MceD derivatize enterobactin by C-glycosylation at the C5 position of a N-(2,3-dihydroxybenzoyl)serine (DHB-Ser) moiety and regiospecific hydrolysis of an ester linkage in the trilactone scaffold, respectively. Mcel and MceJ form a protein complex that attaches C-glycosylated enterobactins to the C-terminal serine residue of both a C10 model peptide and full-length MccE492. In the enzymatic product, the C-terminal serine residue is covalently attached to the C4′ oxygen of the glucose moiety. Nonenzymatic and base-catalyzed migration of the peptide to the C6′ position affords the C6′ glycosyl ester linkage observed in the mature toxin, MccE492m, isolated from bacterial cultures.

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