Biosynthesis of Lycomarasmin

1973 ◽  
Vol 51 (23) ◽  
pp. 3943-3949 ◽  
Author(s):  
C. R. POPPLESTONE ◽  
A. M. Unrau

Cultures of Fusarium oxysporum Schl. emend. Sny. et Hans. f lycopersici (Sacc.) Sny. et Hans. grown on a liquid medium with glucose as the principal carbon source produce, among other products, the phytotoxin lycomarasmin. Acid hydrolysis of lycomarasmin results in the formation of aspartic acid, glycine, and pyruvic acid. Tracer studies showed that glycine-U-I4C, L-serine-U-14C, DL-aspartic acid-4-14C, DL-alanine-1-14C, and glucose-U-14C served as relatively efficient precursors of the lycomarasmin molecule. DL-Aspartic acid-4-I4C was incorporated into the 4-carbon fragment without label scrambling. Glycine was found to be the most efficient precursor of the 2-carbon fragment while glucose afforded the most efficient and direct route for the 3-carbon fragment.

1954 ◽  
Vol 58 (2) ◽  
pp. 227-231 ◽  
Author(s):  
S. Blackburn ◽  
G. R. Lee

1967 ◽  
Vol 45 (12) ◽  
pp. 1953-1959 ◽  
Author(s):  
D. Desaty ◽  
L. C. Vining

When the fungus Fusarium oxysporum was cultured on a glucose–nitrate–salts medium, synthesis of nicotinic acid occurred only during the early growth phase and preceded the accumulation of fusaric acid. Radioactivity from DL-tryptophan-benzene ring-14C was efficiently incorporated into nicotinic acid obtained by acid hydrolysis of the mycelium, whereas DL-tryptophan-β-14C, L-aspartate-U-14C, and sodium acetate-2-14C were poor precursors. Under the conditions of these experiments, all four substrates were poor precursors of fusaric acid. It is concluded that different pathways are used in the biosynthesis of these two pyridine derivatives, the route to nicotinic acid probably involving metabolism of tryptophan via the reactions known to occur in Neurospora crassa.


1969 ◽  
Vol 111 (5) ◽  
pp. 689-694 ◽  
Author(s):  
J. J. Holbrook ◽  
Renate Jeckel

1. Inhibition of ox liver glutamate dehydrogenase with N-(N′-acetyl-4[35S]-sulphamoylphenyl)maleimide (ASPM) is more specific at pH7·3 than at pH6·9. At pH7·3 inhibition accompanies the incorporation at 1 mole of ASPM residues into about 53000g. of protein. 2. Digestion of the modified protein with chymotrypsin and trypsin yields a unique radioactive peptide. 3. Acid hydrolysis of 1 mole of this peptide yields 1 mole of N∈-succin-2-yl-lysine. The ∈-amino group of a lysyl residue is thus the site of modification of the protein. 4. The sequence containing the modified lysyl residue is: [Formula: see text] where Asx respresents either aspartic acid or asparagine.


1962 ◽  
Vol 41 (2) ◽  
pp. 234-246 ◽  
Author(s):  
H. J. van der Molen

ABSTRACT A procedure for the quantitative determination of 5β-pregnan-3α-ol-20-one in urine is described. After acid hydrolysis of the pregnanolone-conjugates in urine, the free steroids are extracted with toluene. Pregnanolone is isolated in a pure form as its acetate; after chromatographic separation of the free steroids on alumina, the fraction containing pregnanolone is acetylated and rechromatographed on alumina. Quantitative determination of the isolated pregnanolone-acetate is carried out with the aid of the infrared spectrum recorded by a micro KBr-wafermethod. The reliability of the method under various conditions is discussed under the headings, specificity, accuracy, precision and sensitivity. It is possible to determine 30–40 μg pregnanolone in a 24-hours urine portion with a precision of 25%.


Author(s):  
M. Alekseenko ◽  
V. Litvyak ◽  
A. Sysa ◽  
E. Hrabovska ◽  
O. Galenko

2012 ◽  
Vol 11 (12) ◽  
pp. 2313-2318
Author(s):  
Theodor Malutan ◽  
Adina Elena Panzariu

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