Cell-free cyclization of delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine to isopenicillin N.
نویسندگان
چکیده
منابع مشابه
CYCLIZATION OF o-(L-(C-AMINOADIPYL)-L-CYSTEINYL-D-VALINE TO PENICILLINS BY CELL-FREE EXTRACTS OF STREPTOMYCES CLAVULIGERUS
Cell-free extracts prepared by sonication of Streptomyces clavuligerus cyclized 6-(L-aaminoadipyl)-L-cysteinyl-D-valine (ACV) into a penicillin-type antibiotic. The antibacterial spectrum of this antibiotic suggested it was a mixture of isopenicillin N and penicillin N indicating that both cyclization and racemase activities were present. Cyclization activity was optimal in extracts prepared fr...
متن کاملCyclization of phenylacetyl-L-cysteinyl-D-valine to benzylpenicillin using cell-free extracts of Streptomyces clavuligerus.
Benzylpenicillin, a typical antibiotic produced by some species of fungi, was obtained by direct cyclization of the heteropeptide phenylacetyl-L-cysteinyl-D-valine using cell-free extracts of Streptomyces clavuligerus. This is the first description of evidence of the synthesis of benzylpenicillin from a non natural molecule using a bacterial enzyme.
متن کاملStoichiometry of oxygen consumption in the biosynthesis of isopenicillin from a tripeptide.
The biosynthesis of isopenicillin N from delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine in a cell-free system has been correlated wih O2 consumption by two methods, involving the use of an oxygen-electrode and an n.m.r. spectrometer respectively. The results are consistent with a 1 : 1 stoichiometric ratio for the dioxygen consumed to the isopenicillin N formed.
متن کاملProduction of the penicillin precursor 5-(L-a-aminoadipyl)-L-cysteinyl-D-valine (ACV) by cell-free extracts from Streptomyces clavuligerus
Glycerol-stabilised cell extracts of Streptomyces clavuligerus contain an enzyme activity which synthesises ACV from the individual amino acids L-a-aminoadipic acid, t-cysteine and L-valine. Enzyme activity was optimum in reaction mixtures containing 1 mM ATP together with an ATP regenerating system. The ACV synthetase enzyme formed ACV analogs when provided with Lcarboxymethylcysteine in place...
متن کاملSite-directed mutagenesis of proline-285 to leucine in Cephalosporium acremonium isopenicillin-N-synthase affects catalysis and increases soluble expression at higher temperatures.
The conversion of delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV) to isopenicillin N is dependant on the catalytic action of isopenicillin N-synthase (IPNS), an important enzyme in the penicillin and cephalosporin biosynthetic pathway. One of the amino acid residues suggested by the Aspergillus nidulans IPNS crystal structure for interaction with the valine isopropyl group of ACV is prol...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Antimicrobial Agents and Chemotherapy
سال: 1980
ISSN: 0066-4804,1098-6596
DOI: 10.1128/aac.18.3.465