Synthesis of <i>N</i>2-Protected <scp>l</scp>-2,3-Diaminopropanoic Acids

Noguchi, Noriyoshi; Kuroda, T.; Hatanaka, Minoru; Ishimaru, Toshiyasu

doi:10.1246/bcsj.55.633

Cited by 9 publications

(1 citation statement)

References 10 publications

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“…D-α-Aminopimelic acid was prepared by the method of Wade et al [19] as modified by Bommarius et al [20]. The amino group was then protected by reaction with benzyl chloroformate [21] and then the α-carboxyl group by cyclization with formaldehyde [22]. Condensation of the resulting R-3-benzyloxycarbonyl-5oxo-4-oxazolidine valeric acid with D-alanyl-D-alanine methyl ester was achieved by dicyclohexyl carbodi-imide coupling [23].…”

Section: D-α-aminopimelyl-ε-d-alanyl-d-alanine (3)mentioning

confidence: 99%

On the substrate specificity of bacterial DD-peptidases: evidence from two series of peptidoglycan-mimetic peptides

Anderson

Adediran

Charlier

et al. 2003

Biochemical Journal

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The reactions between bacterial DD-peptidases and beta-lactam antibiotics have been studied for many years. Less well understood are the interactions between these enzymes and their natural substrates, presumably the peptide moieties of peptidoglycan. In general, remarkably little activity has previously been demonstrated in vitro against potential peptide substrates, although in many cases the peptides employed were non-specific and not homologous with the relevant peptidoglycan. In this paper, the specificity of a panel of DD-peptidases against elements of species-specific D-alanyl-D-alanine peptides has been assessed. In two cases, those of soluble, low-molecular-mass DD-peptidases, high activity against the relevant peptides has been demonstrated. In these cases, the high specificity is towards the free N-terminus of the peptidoglycan fragment. With a number of other enzymes, particularly high-molecular-mass DD-peptidases, little or no activity against these peptides was observed. In separate experiments, the reactivity of the enzymes against the central, largely invariant, peptide stem was examined. None of the enzymes surveyed showed high activity against this structural element although weak specificity in the expected direction towards the one structural variable (D-gammaGln versus D-gammaGlu) was observed. The current state of understanding of the activity of these enzymes in vitro is discussed.

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Section: D-α-aminopimelyl-ε-d-alanyl-d-alanine (3)mentioning

confidence: 99%

On the substrate specificity of bacterial DD-peptidases: evidence from two series of peptidoglycan-mimetic peptides

Anderson

Adediran

Charlier

et al. 2003

Biochemical Journal

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ChemInform Abstract: SYNTHESIS OF N2‐PROTECTED L‐2,3‐DIAMINOPROPANOIC ACIDS

Noguchi¹,

Kuroda²,

Hatanaka³

et al. 1982

Chemischer Informationsdienst

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Asymmetric synthesis of (R)‐6‐amino‐1‐methyl‐4‐(3‐methyl‐benzyl)hexahydro‐1H‐1,4‐diazepine from L‐asparagine

Kato

Harada

Mode

1997

Journal of Heterocyclic Chem

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An efficient asymmetric synthesis of (R)‐6‐amino‐1‐methyl‐4‐(3‐rnethylbenzyl)hexahydro‐1H‐1,4‐diazepine [(R)‐2] which serves as the amine part of (R)‐1, a potent and selective 5‐HT3 receptor antagonist, is described. Formation of the hexahydro‐1H‐1,4‐diazepine ring was achieved by the intramolecular ami‐dation of the optically active aminocarboxylic acid 18 or reductive cyclization of the optically active aminoaldehyde 25. Compounds 18 and 25 were prepared from L‐asparagine via the key aziridine derivatives 15 and 22, respectively, with retention of the configuration. The intramolecular aziridine ring opening reaction of 29 gave the C2N bond cleavage product of the aziridine ring, the piperazin‐5‐one 30, as the main product along with the desired 7‐membered ring, the hexahydro‐1H‐1,4‐diazepine product 19.

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Synthesis of N2-Protected l-2,3-Diaminopropanoic Acids

Abstract: The title compounds have been synthesized from N-protected l-aspartic acid via Curtius rearrangement.

Cited by 9 publications

References 10 publications

On the substrate specificity of bacterial DD-peptidases: evidence from two series of peptidoglycan-mimetic peptides

On the substrate specificity of bacterial DD-peptidases: evidence from two series of peptidoglycan-mimetic peptides

ChemInform Abstract: SYNTHESIS OF N2‐PROTECTED L‐2,3‐DIAMINOPROPANOIC ACIDS

Asymmetric synthesis of (R)‐6‐amino‐1‐methyl‐4‐(3‐methyl‐benzyl)hexahydro‐1H‐1,4‐diazepine from L‐asparagine

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