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A5028

Sigma-Aldrich

Adenylosuccinic acid

~96% (HPLC)

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About This Item

Empirical Formula (Hill Notation):
C14H18N5O11P
CAS Number:
Molecular Weight:
463.29
UNSPSC Code:
12352204
PubChem Substance ID:

assay

~96% (HPLC)

form

powder

storage temp.

−20°C

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

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

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Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


Certificates of Analysis (COA)

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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
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
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
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
Iu N Zhukov et al.
Bioorganicheskaia khimiia, 14(7), 969-972 (1988-07-01)
A number of earlier unknown phosphonate analogues of aspartyl adenylate with anhydride oxygen substituted by --CH2--, and the carbonyl group substituted by --CH(OH)- or --CH(NH2)-groups were synthesized. These compounds were used to study the reaction mechanism of asparagine synthetases from

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