InChI
1S/C14H18N5O11P/c20-7(21)1-5(14(24)25)18-11-8-12(16-3-15-11)19(4-17-8)13-10(23)9(22)6(30-13)2-29-31(26,27)28/h3-6,9-10,13,22-23H,1-2H2,(H,20,21)(H,24,25)(H,15,16,18)(H2,26,27,28)/t5-,6+,9+,10+,13+/m0/s1
InChI key
OFBHPPMPBOJXRT-VWJPMABRSA-N
SMILES string
O[C@H]1[C@@H](O)[C@@H](O[C@@H]1COP(O)(O)=O)n2cnc3c(N[C@@H](CC(O)=O)C(O)=O)ncnc23
assay
~96% (HPLC)
form
powder
storage temp.
−20°C
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存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
法规信息
新产品
此项目有
Maria Novikova et al.
The Journal of biological chemistry, 285(17), 12662-12669 (2010-02-18)
The heptapeptide-nucleotide microcin C (McC) is a potent inhibitor of enteric bacteria growth. McC is excreted from producing cells by the MccC transporter. The residual McC that remains in the producing cell can be processed by cellular aminopeptidases with the
H Mejdoub et al.
Biochemistry, 26(7), 2054-2059 (1987-04-07)
Aspartyl-tRNA synthetase from bakers' yeast gives an unstable complex with the cognate adenylate, which reacts after dissociation with amino acid side chains of the protein. This leads to a covalent incorporation of aspartic acid into aspartyl-tRNA synthetase via amide or
B Rees et al.
Journal of molecular biology, 299(5), 1157-1164 (2000-06-30)
The crystal structure of aspartyl-tRNA synthetase from Escherichia coli has been determined to a resolution of 2.7 A. The structure is compared to the same enzyme co-crystallized with tRNA(Asp) and containing aspartyl adenylate or ATP. The asymmetric unit contains three
Dominic Bernard et al.
Journal of enzyme inhibition and medicinal chemistry, 22(1), 77-82 (2007-03-22)
Asparaginyl-tRNA formation in Pseudomonas aeruginosa PAO1 involves a nondiscriminating aspartyl-tRNA synthetase (ND-AspRS) which forms Asp-tRNA(Asp) and Asp-tRNA(Asn), and a tRNA-dependent amidotransferase which transamidates the latter into Asn-tRNA(Asn). We report here that the inhibition of this ND-AspRS by L-aspartol adenylate (Asp-ol-AMP)
Teymur Kazakov et al.
Journal of bacteriology, 190(7), 2607-2610 (2008-01-29)
The heptapeptide-nucleotide microcin C (McC) targets aspartyl-tRNA synthetase. Upon its entry into a susceptible cell, McC is processed to release a nonhydrolyzable aspartyl-adenylate that inhibits aspartyl-tRNA synthetase, leading to the cessation of translation and cell growth. Here, we surveyed Escherichia
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