Ac-Lys(Ac)-D-Ala-D-Ala-OH
Ac-Lys(Ac)-D-Ala-D-Ala-OH structure
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Common Name | Ac-Lys(Ac)-D-Ala-D-Ala-OH | ||
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| CAS Number | 24570-39-6 | Molecular Weight | 372.417 | |
| Density | 1.2±0.1 g/cm3 | Boiling Point | 840.0±65.0 °C at 760 mmHg | |
| Molecular Formula | C16H28N4O6 | Melting Point | N/A | |
| MSDS | Chinese USA | Flash Point | 461.8±34.3 °C | |
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Conformational studies of resin-bound vancomycin and the complex of vancomycin and Ac2-L-Lys-D-Ala-D-Ala.
J. Comb. Chem. 7(1) , 123-9, (2005) The molecular target of vancomycin, a commonly used glycopeptide antibiotic, is the D-Ala-D-Ala dipeptide subunit on the bacterial cell wall. The molecular basis of interaction between vancomycin and D-Ala-D-Ala in solution is well-known. However, there is no... |
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Isolation of the membrane-bound 26 000-Mr penicillin-binding protein of Streptomyces strain K15 in the form of a penicillin-sensitive D-alanyl-D-alanine-cleaving transpeptidase.
Biochem. J. 207 , 109, (1982) The membrane-bound, 26 000-Mr penicillin-binding protein of Streptomyces K15 has been isolated in the form of an effective, penicillin-sensitive D-alanyl-D-alanine-cleaving peptidase exhibiting high transpeptidase activity (greater than 95%) and very low carb... |
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Conformational analysis of peptide substrates and inhibitors of the Zn2+ G and serine R61 D-alanyl-D-alanine peptidases.
Eur. J. Biochem. 121(1) , 221-32, (1981)
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Partitioning the loss in vancomycin binding affinity for D-Ala-D-Lac into lost H-bond and repulsive lone pair contributions.
J. Am. Chem. Soc. 125(31) , 9314-5, (2003) The binding affinity of 4, which incorporates a methylene (CH2) in place of the key linking amide of Ac2-l-Lys-d-Ala-d-Ala, for vancomycin was compared with that of Ac2-l-Lys-d-Ala-d-Ala (3) and Ac2-l-Lys-d-Ala-d-Lac (5). The vancomycin affinity for 4 was app... |
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Preparation of biologically active ristocetin derivatives: replacements of the 1'-amino group.
J. Med. Chem. 28(9) , 1371-5, (1985) A series of ristocetin analogues with modifications (OH, C=O, C=NOH, NCOCH3) at the C-1' amino group was synthesized and found to possess antibacterial activity against gram-positive bacteria and to bind to Ac2-Lys-D-Ala-D-Ala, a model for the antibiotic's si... |
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Dual nano-electrospray for probing solution interactions and fast reactions of complex biomolecules.
Eur. J. Mass Spectrom. (Chichester, Eng.) 18(5) , 439-46, (2012) A novel nano-electrospray emitter has been developed containing two separated channels running throughout the length of the emitter. The emitters have been fabricated from "theta-shaped" borosilicate capillaries. Loading of different solutions into the two di... |
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Synthesis and antibacterial activity of a series of basic amides of teicoplanin and deglucoteicoplanin with polyamines.
J. Med. Chem. 35(22) , 4054-60, (1992) Basic carboxamides of teicoplanin A2 (CTA) and its aglycon (TD) are prepared by condensation of the 63-carboxyl function of these antibiotics with linear or branched polyamines. The antimicrobial activities of some of the resulting compounds were better than ... |
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Streptomyces K15 DD-peptidase-catalysed reactions with ester and amide carbonyl donors.
Biochem. J. 235(1) , 167-76, (1986) In water, the purified 26 000-Mr membrane-bound DD-peptidase of Streptomyces K15 hydrolyses the ester carbonyl donor Ac2-L-Lys-D-Ala-D-lactate (release of D-lactate) and the amide carbonyl donor Ac2-L-Lys-D-Ala-D-Ala (release of D-alanine) with accumulation o... |
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Crystal structures of the complexes between vancomycin and cell-wall precursor analogs.
J. Mol. Biol. 385 , 1422-1432, (2009) The crystal structures of three vancomycin complexes with two vancomycin-sensitive cell-wall precursor analogs (diacetyl-Lys-D-Ala-D-Ala and acetyl-D-Ala-D-Ala) and a vancomycin-resistant cell-wall precursor analog (diacetyl-Lys-D-Ala-D-lactate) were determin... |
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Streptomyces K15 DD-peptidase-catalysed reactions with suicide beta-lactam carbonyl donors.
Biochem. J. 235(1) , 177-82, (1986) The values of the kinetic parameters that govern the interactions between the Streptomyces K15 DD-peptidase and beta-lactam compounds were determined by measuring the inactivating effect that these compounds exert on the transpeptidase activity of the enzyme ... |