Penicillium terlikowskii

Gliotoxiii.—In contrast to the recent report that the cyclic dipeptide (121) is not incorporated into gliotoxin (123) in Penicillium terlikowskii, it has recently been found that this cyclic dipeptide, with both constituent amino-acids labelled, is efficiently incorporated into gliotoxin (123) in Trichoderma viride and without alteration in isotope ratio. Thus, (123), like brevianamide A and echinulin, originates from a cyclic dipeptide. The difference in the two results could be due to the different organisms used in the two experiments, but is was suggested that the probable reason was associated with the large excess of (121) used in the first experiment. 

Further investigation of the biosynthesis of gliotoxin has shown that although cyc/o-L-phenylalanyl-L-seryl (157) was apparently able to permeate the mycelium of Penicillium terlikowskii, it was not incorporated into gliotoxin (156) under conditions when phenylalanine was. Similar negative results were obtained for mycelianamide (158) in P. patulum with cycto-L-alanyl-L-tyrosyl (159) and cyc/o-L-alanyl-D-tyrosyl which were also able to permeate the mycelium. In contrast [l- CJtyrosine was specifically incorporated with high efficiency (there was no significant difference in the efficiency with which the d- and L-isomers of tyrosine were utilized). 

Gliotoxin.—Gliotoxin (46) is a metabolite of Trichoderma viride and Penicillium terlikowskii. Recently, phenylalanine but not w-tyrosine (in contrast to earlier work ) or o-tyrosine or 2,3-dihydroxyphenylalanine has been shown to be incorporated. The incorporation was sufficiently high to allow the use of... 

Finally, independent studies by Brannon et al (1971) gave results fully in accord with the foregoing findings. They found that DL-[3- C]phenyla-lanine was incorporated into gliotoxin with consistently greater efficiency than DL-[2- " C]-w-tyrosine in both T, viride and Penicillium terlikowskii. 

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