Conversion of17O/18O-labelled δ-(L-α-aminoadipyl)–L-cycteinyl–D-valine into17O/18O-labelled isopenicillin N in a cell-free extract of C. acremonium

1982 ◽  
pp. 137-139 ◽  
Author(s):  
Robert M. Adlington ◽  
Robin T. Aplin ◽  
Jack E. Baldwin ◽  
Leslie D. Field ◽  
Eeva-M. M. John ◽  
...  
Keyword(s):  
Cell Free Extract ◽  
A Cell ◽  
Isopenicillin N

Conversion of 17O/18O labelled δ-(L-α-aminoadlpyl)-L-cysteinyl-D-valine to 17O/18O labelled isopenicillin n in a cell-free extract of . A study by 17O-NMR spectroscopy and mass spectrometry

Tetrahedron ◽  
1983 ◽  
Vol 39 (7) ◽  
pp. 1061-1068 ◽  
Author(s):  
Robert M. Adlington ◽  
Robin T. Aplin ◽  
Jack E. Baldwin ◽  
Bulbul Chakravarti ◽  
Leslie D. Field ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Nmr Spectroscopy ◽  
Cell Free Extract ◽  
17O Nmr ◽  
A Cell ◽  
17O Nmr Spectroscopy ◽  
Isopenicillin N

scholarly journals Incorporation of 3H from δ-(l-α-amino (4,5-3H)adipyl)-l-cysteinyl-d-(4,4-3H)valine into isopenicillin N

1979 ◽  
Vol 184 (2) ◽  
pp. 421-426 ◽  
Author(s):  
J O'Sullivan ◽  
R C Bleaney ◽  
J A Huddleston ◽  
E P Abraham
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Adipic Acid ◽  
Experimental Error ◽  
Acid Oxidase ◽  
Cephalosporium Acremonium ◽  
Amino Acid Oxidase ◽  
Free System ◽  
A Cell ◽  
Isopenicillin N

1. delta-(L-alpha-Amino[4,5-3H]adipyl)-L-cysteinyl-D-[4,4-3H]valine has been synthesized from its constituent amino acids, the L-alpha-amino[4,5-3H]adipic acid being obtained by reduction with 3H2 of methyl 5-acetamido-5,5-diethoxycarbonylpent-2-enoate and subsequent decarboxylation and hydrolysis. 2. In a cell-free system prepared by lysis of protoplasts of Cephalosporium acremonium 3H was incorporated from the doubly labelled tripeptide into a compound that behaved like penicillin N or isopenicillin N. The relative specific radioactivities of the alpha-aminoadipyl and penicillamine moieties of the penicillin were the same (within experimental error) as those of the alpha-aminoadipic acid and valine residues respectively of the tripeptide. 3. The behaviour of the labelled alpha-aminoadipic acid from the penicillin to the L-amino acid oxidase of Crotalus adamanteus venom showed that it was mainly L-alpha-aminoadipic acid. 4. The results are consistent with the hypothesis that the carbon skeleton of the LLD-tripeptide is incorporated intact into the penicillin molecule and that the first product is isopenicillin N.

The translation of rabbit hemoglobin messenger RNA in a cell-free extract from chick embryo brain

1974 ◽  
Vol 36 (2) ◽  
pp. 299-310 ◽  
Author(s):  
Don Hendrick ◽  
Walter Knöchel ◽  
Walter Schwarz ◽  
Sabine Pitzel ◽  
Heinz Tiedemann
Keyword(s):  
Chick Embryo ◽  
Messenger Rna ◽  
Cell Free Extract ◽  
A Cell ◽  
Embryo Brain

Antioxidant activity of selenium nanoparticles biosynthesized using a cell-free extract of Geobacillus

2020 ◽  
Vol 102 (10) ◽  
pp. 556-567
Author(s):  
Awanish Kumar ◽  
Bablu Prasad ◽  
Jayanand Manjhi ◽  
Kumar Suranjit Prasad
Keyword(s):  
Antioxidant Activity ◽  
Selenium Nanoparticles ◽  
Cell Free Extract ◽  
A Cell

scholarly journals The enzymic conversion of squalene, 2(3),22(23)-diepoxide to α-onocerin by a cell-free extract of Ononis spinosa

FEBS Letters ◽  
1971 ◽  
Vol 12 (4) ◽  
pp. 229-232 ◽  
Author(s):  
M.G. Rowan ◽  
P.D.G. Dean ◽  
T.W. Goodwin
Keyword(s):  
Cell Free Extract ◽  
A Cell

Evidence for cellular control in the synthesis of acetoin or α-ketoisovaleric acid by microorganisms

1974 ◽  
Vol 20 (6) ◽  
pp. 805-811 ◽  
Author(s):  
E. B. Collins ◽  
R. A. Speckman
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Steady State ◽  
Serratia Marcescens ◽  
Lactobacillus Casei ◽  
Optically Active ◽  
Cell Free Extract ◽  
Data Support ◽  
A Cell ◽  
Cellular Control ◽  
Spent Media

Commercial α-acetolactate at pH 4.5 decarboxylated nonenzymatically (5 to 8%/h) to acetoin (69%) and diacetyl (31%), and an extract of Streptococcus diacetilactis 18-16 produced α-acetolactate (in addition to acetoin and diacetyl) from pyruvate in the presence of TPP and MgSO4. Nevertheless, α-acetolactate was not dispersed into media by any of four microorganisms (S. diacetilactis, strains 18-16 and DRC1, Saccharomyces cerevisiae 299, and Lactobacillus casei 393) that produced diacetyl and acetoin or by one (Serratia marcescens) that produced only acetoin. Lactobacillus casei and S. diacetilactis 18-16 produced unknown compounds that falsely indicated the presence of α-acetolactate when tests were made without separating acetoin and diacetyl from other components of the spent media. The production of acetoin by S. diacetilactis 18-16 was not inhibited by valine, the acetoin produced by this organism was optically active (+101.0°), and a cell-free extract of S. marcescens did not produce diacetyl while producing a large amount of acetoin. Data support the conclusion that the conversion of pyruvate to acetoin by some microorganisms and to α-ketoisovaleric acid by others is enzymatic and under cellular control, resulting in the synthesis of only steady-state amounts of enzymatically bound α-acetolactate in each of the pathways.

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