21566-74-5

Usage

Definition

ChEBI: A tripeptoid arising from cleavage of both rings of a penicillin derivative.

InChI:InChI=1/C14H25N3O6S/c1-7(2)11(14(22)23)17-12(19)9(6-24)16-10(18)5-3-4-8(15)13(20)21/h7-9,11,24H,3-6,15H2,1-2H3,(H,16,18)(H,17,19)(H,20,21)(H,22,23)/t8-,9-,11-/m0/s1

Upstream product

• 72-18-4 L-valine 
• 52-90-4 L-Cysteine 
• 1118-90-7 L-homoglutamic acid 
• 77257-03-5 α-²H-(S)-valine 
• 84701-31-5 di-(1-<(1R)-carboxy-2-methylpropyl>-(3R)-<-(5S)-5-amino-5-carboxypentanamido>-(4R)-mercapto azetidin-2-one)disulphide 
• 69644-78-6 (S)-2-Amino-5-[(R)-2-[(R)-2-(5-amino-5-carboxy-pentanoylamino)-2-((R)-1-carboxy-2-methyl-propylcarbamoyl)-ethyldisulfanyl]-1-((R)-1-carboxy-2-methyl-propylcarbamoyl)-ethylcarbamoyl]-pentanoic acid 
• 24325-17-5 N-benzyloxycarbonyl-α-benzylester-δ-L-α-aminoadipic acid 
• 79761-10-7 [(N-benzyloxycarbonyl)-(α-benzyl)-δ-(L-α-aminoadipoyl)]-S-benzyl-L-cysteine 
• 87141-23-9 p-nitrobenzyl N-benzyloxycarbonyl-L-α-aminoadipate 
• 87141-27-3 N-benzyloxycarbonyl-1-(p-nitrobenzyl)-δ-(L-α-aminoadipyl)-S-benzyl-L-cysteinyl-D-valine, benzhydryl ester 
• 87141-25-1 N-benzyloxycarbonyl-1-(p-nitrobenzyl)-δ-(L-α-aminoadipyl)-S-benzyl-L-cysteine, benzhydryl ester 
• 87141-26-2 N-benzyloxycarbonyl-1-(p-nitrobenzyl)-δ-(L-α-aminoadipyl)-S-benzyl-L-cysteine 
• 61852-70-8 D-valine, benzhydryl ester 
• 79761-03-8 N-benzyloxycarbonyl-S-benzyl-L-cysteinyl-D-valine benzyl ester 

Downstream Products

• 69644-78-6 bis[Aad(-Cys-D-Val)] 
• 525-94-0 isopenicillin N 

Relevant academic research and scientific papers

Exchange of the valine 2-H in the biosynthesis of L-δ-(α-aminoadipoyl)-L-cysteinyl-D-valine

Incubation of [2-2H]-valine with purified ACV synthetase from both Cephalosporium acremonium and Streptomyces davuligerus produced L-δ-(α-aminoadipoyl)-L-cysteinyl-D-valine (ACV), determined by the essentially complete (>95%) loss of deuterium from the α position of the incorporated valine. Incubations with deuterium oxide/water as solvent produced ACV with significant incorporation of deuterium into the valinyl residue. These observations confirm the prior proposal that a single multifunctional enzyme is responsible for both the formation of the peptide bonds of ACV and the epimerisation of the valinyl residue.

Synthesis of δ-(L-α-Aminoadipyl)-L-cysteinyl-D-valine and δ-(L-α-Aminoadipyl)-L-cysteinyl-D-valylglycine

An efficient synthesis of δ-(L-α-aminoadipyl)-L-cysteinyl-D-valine (ACV; 1) and δ-(L-α-aminoadipyl)-L-cysteinyl-D-valylglycine (ACVG; 2) via the protected tripeptide N-benzyloxycarbonyl-1-(p-nitrobenzyl)-δ-(L-α-aminoadipyl)-S-benzyl-L-cysteinyl-D-valine,

Conversion of 17O/18O-Labelled &δ-(L-&α-Aminoadipyl)-L-cysteinyl-D-valine into 17O/18O-Labelled Isopenicillin N in a Cell-free Extract of C. acremonium

δ-(L-α-Amino17O/18O>-adipyl)-L-cysteinyl-D-valine was converted into isopenicillin N in cell-free extracts of Cephalosporium acremonium with no loss of 17O/18O label as shown by 17O n.m.r. spectroscopy and mass spectrometry; incubation of unlabelled tripeptide in a cell-free system containing 17O/18O-enriched water produced isopenicillin N with no incorporation of 17O/18O.

Synthesis of δ-(L-α-Aminoadipoyl)-L-cysteinyl-D-valine and some Carbon-13 and Nitrogen-15 Labelled Isotopomers

δ-(L-α-Aminoadipoyl)-L-cysteinyl-D-valine (7a), δ-(L-α-aminoadipoyl)-L-cysteinyl-D-valine (7b), δ-(L-α-aminoadipoyl)-L-cysteinyl-D-valine (7c), and δ-(L-α-aminoadipoyl)-L-cysteinyl-D-valine (7d) were prepared by conv