Use of 6-(l-2-aminoadipyl)-l-cysteinyl-l-valine for the biosynthesis of penicillin byPenicillium chrysogenum
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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 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...
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abstract nowadays, the science of decision making has been paid to more attention due to the complexity of the problems of suppliers selection. as known, one of the efficient tools in economic and human resources development is the extension of communication networks in developing countries. so, the proper selection of suppliers of tc equipments is of concern very much. in this study, a ...
15 صفحه اولCyclization 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 کاملA non-planar peptide bond in L-seryl-L-valine.
The molecular structure of (I) is shown in Fig. 1. Bond lengths and angles are normal, but the unusual non-planarity of the peptide bond is quite evident. The associated torsion angle C1ÐC3ÐN2ÐC4 (!) is 157.37 (15) , a deviation from 180 that is superceded among small chiral peptides only by the 156.6 ! angle in N-(tert-butoxycarbonyl)-l-Pro-l-Leu benzyl ester (Sugino et al., 1978). Fig. 2(a) s...
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ژورنال
عنوان ژورنال: FEMS Microbiology Letters
سال: 1978
ISSN: 0378-1097,1574-6968
DOI: 10.1111/j.1574-6968.1978.tb02836.x