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22477-86-7

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22477-86-7 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 22477-86-7 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 2,2,4,7 and 7 respectively; the second part has 2 digits, 8 and 6 respectively.
Calculate Digit Verification of CAS Registry Number 22477-86:
(7*2)+(6*2)+(5*4)+(4*7)+(3*7)+(2*8)+(1*6)=117
117 % 10 = 7
So 22477-86-7 is a valid CAS Registry Number.

22477-86-7Relevant articles and documents

Mechanism of action and inhibition of dehydrosqualene synthase

Lin, Fu-Yang,Liu, Chia-I.,Liu, Yi-Liang,Zhang, Yonghui,Wang, Ke,Jeng, Wen-Yih,Ko, Tzu-Ping,Cao, Rong,Wang, Andrew H.-J.,Oldfield, Eric

, p. 21337 - 21342 (2010)

"Head-to-head" terpene synthases catalyze the first committed steps in sterol and carotenoid biosynthesis: the condensation of two isoprenoid diphosphates to form cyclopropylcarbinyl diphosphates, followed by ring opening. Here, we report the structures of Staphylococcus aureus dehydrosqualene synthase (CrtM) complexed with its reaction intermediate, presqualene diphosphate (PSPP), the dehydrosqualene (DHS) product, as well as a series of inhibitors. The results indicate that, on initial diphosphate loss, the primary carbocation so formed bends down into the interior of the protein to react with C2,3 double bond in the prenyl acceptor to form PSPP, with the lower two-thirds of both PSPP chains occupying essentially the same positions as found in the two farnesyl chains in the substrates. The second-half reaction is then initiated by the PSPP diphosphate returning back to the Mg2+ cluster for ionization, with the resultant DHS so formed being trapped in a surface pocket. This mechanism is supported by the observation that cationic inhibitors (of interest as antiinfectives) bind with their positive charge located in the same region as the cyclopropyl carbinyl group; that S-thiolo-diphosphates only inhibit when in the allylic site; activity results on 11 mutants show that both DXXXD conserved domains are essential for PSPP ionization; and the observation that head-to-tail isoprenoid synthases as well as terpene cyclases have ionization and alkene-donor sites which spatially overlap those found in CrtM.

HIV-1 integrase inhibitor-inspired antibacterials targeting isoprenoid biosynthesis

Zhang, Yonghui,Lin, Fu-Yang,Li, Kai,Zhu, Wei,Liu, Yi-Liang,Cao, Rong,Pang, Ran,Lee, Eunhae,Axelson, Jordan,Hensler, Mary,Wang, Ke,Molohon, Katie J.,Wang, Yang,Mitchell, Douglas A.,Nizet, Victor,Oldfield, Eric

scheme or table, p. 402 - 406 (2012/06/29)

We report the discovery of antibacterial leads, keto- and diketo-acids, targeting two prenyl transferases: undecaprenyl diphosphate synthase (UPPS) and dehydrosqualene synthase (CrtM). The leads were suggested by the observation that keto- and diketo-acids bind to the active site Mg2+/Asp domain in HIV-1 integrase, and similar domains are present in prenyl transferases. We report the X-ray crystallographic structures of one diketo-acid and one keto-acid bound to CrtM, which supports the Mg2+ binding hypothesis, together with the X-ray structure of one diketo-acid bound to UPPS. In all cases, the inhibitors bind to a farnesyl diphosphate substrate-binding site. Compound 45 had cell growth inhibition MIC90 values of ~250-500 ng/mL against Staphylococcus aureus, 500 ng/mL against Bacillus anthracis, 4 μg/mL against Listeria monocytogenes and Enterococcus faecium, and 1 μg/mL against Streptococcus pyogenes M1 but very little activity against Escherichia coli (DH5α, K12) or human cell lines.

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