Penicillium janthinellum

Very recently Li et al. (2006) reported comparative studies of the similarities and differences between the microbial and mammalian metabolisms of l-THP, the microbial transformation by Penicillium janthinellum, and metabolism in rats [46]. The biotransformation of l-THP by P. janthinellum AS 3.510 resulted in the formation of three metabolites. Their structures (shown in Fig. 5) were identified as L-corydalmine, L-corypalmine, and 9-0-desmethyl-L-THP, by comprehensive NMR and MS analysis [46]. 

Li L et al. (2006) Liquid chromatography-tandem mass spectrometry for the identification of L-tetrahydropalmatine metabolites in Penicillium janthinellum and rats. Biomed Chromatogr 20(1) 95-100... 

Marinho AMdR et al. Biologically active polyketides produced by Penicillium janthinellum isolated as an endophytic fungus from fruits of Melia azedarach, J Brazil Chem Soc 16 280-283, 2005. 

Neoxaline, C23H25N5O4, a new metabolite of Aspergillus japonicus, exhibits similarities to oxaline in its i.r. and n.m.r. spectra, and may be an indole derivative, but nothing further is known of its constitution as yet.38a Similarly, three new tremorgenic mycotoxins from Penicillium janthinellum, janthitrems A, B, and C, may also be indole derivatives.386... 

Gao, P. J., Chen, G. J., Wang, T. H., Zhang, Y. S., and Liu, J. 2001. Non-hydrolytic disruption of crystalline structure of cellulose by cellulose binding domain and linker sequence of cellobiohydrolase I from Penicillium janthinellum. Shengwu Huaxue Yu Shengwu Wuli Xuebao, 33,13-18. 

Steyn PS Mycotoxins, general view, chemistry and structure. Toxicol Lett 1995 82 843-851. Yamaguchi T, Nozawa K, Hosoc T, Nakajima S, Kawai KL Indoloditerpenes related to tremorgenic mycotoxin penitrems, from Penicillium crustosum. Phytochemistry 1993 32 1177-1181. Penn J, Swift R, Wigley LJ, Mantle PG, Bilton JN, Sheppard RN Janthitrems B and C, two principal indole-diterpenoids produced by Penicillium janthinellum. Phytochemistry 1993 32 1431-1434. 

Wilkins AL, Miles CO, Ede RM, Gallagher RT, Munday SC Structure elucidation of janthitrem B, a tremorgenic metabolite of Penicillium janthinellum, and relative configuration of the A and B rings of janthitrems B, E, and F. J Agric Food Chem 1992 40 1307-1309. 

Primitive fungi do occur in acidic media. Penicillopepsin is formed by Penicillium janthinellum if the pH of the medium remains below 4.5 (31). On a synthetic medium the enzyme appears only at a development stage where mycelial growth has ceased and sporulation has started (32), The exact role in the sporulation process is, however, still obscure. No information is available about a possible role in a physiological environment. 

The design procedure described above was applied to the protein penicillopepsin, an aspartyl protease from Penicillium janthinellum. The coordinates for the protein were obtained from the Protein Data Bank (Jil) entry 2APP. The crystal structure was determined by James and Sielecki (11) at 1.8A resolution. 

Smetanina OF, Kahnovski Al, Khudyakova YV, Pivkin MV, Dmitrenok PS, Fedorov SN, et al. Indole alkaloids produced by a marine fungus isolate of Penicillium janthinellum biourge. J Nat Prod 2007 70 906. ... 

Figure 4. Action of three different a-galactosidases AGL L AGL II and AGL III from Penicillium janthinellum on two galactomannas having different degrees of substitution. 5000 nkat of a-galactosidase /gram of mannan was incubated...

I. Hsu, T. J. Delbaere, M. M. G. James, and T. Hofmann (1977), Penicillopepsin from Penicillium janthinellum. Crystal structure at 2.8 A and sequence. Homology with porcine pepsin. Nature 266 140-145. 

Penicillopepsin is an acid protease produced by the mold Penicillium janthinellum at pH s less than 4.1 (1). Enzyme production occurs after the mycelial growth has ceased and sporulation has begun (2). The specificity and catalytic mechanism of penicillopepsin are very similar to those of porcine pepsin (3). The two active site aspartic acid residues, Asp-32 and Asp-215, occur in peptide sequences of at least eight amino acid residues which are almost identical in penicillopepsin, pepsin and chymosin (1,4-10). 

If all species from which at least 16 residues had been removed are base denaturable, then this interpretation is consistent with our kinetic experiments. In this instance the removal of the peptide comprising residues 17-44 may well be by one or more bimolecular processes. If one assumes a strict structural homology between porcine pepsin and the fungal proteases from Penicillium janthinellum, Rhizopus chinensis, and Endothia parasitica, (see Chapters 2,3,4, and 5) then this suggestion of subsequent bimolecular degradation is attractive since the NH2 termini of these enzymes are not located near their active centers. 

Seki Y, Takeguchi M, Okura I. Purification and properties of bilirubin oxidase from Penicillium janthinellum. J Biotechnol 1996 46 145-151. 

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