This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Esmahan, C Articles by Martin, J F Search for Related Content PubMed PubMed Citation Articles by Esmahan, C Articles by Martin, J F Agricola Articles by Esmahan, C Articles by Martin, J F

Next Article 

Appl Environ Microbiol. 1994 June; 60(6): 1705-1710

Catabolism of lysine in Penicillium chrysogenum leads to formation of 2-aminoadipic acid, a precursor of penicillin biosynthesis.

Department of Ecology, Genetics and Microbiology, Faculty of Biology, University of León, Spain.

ABSTRACT

Penicillium chrysogenum L2, a lysine auxotroph blocked in the early steps of the lysine pathway before 2-aminoadipic acid, was able to synthesize penicillin when supplemented with lysine. The amount of penicillin produced increased as the level of lysine in the media was increased. The same results were observed in resting-cell systems. Catabolism of [U-14C]lysine by resting cells and batch cultures of P. chrysogenum L2 resulted in the formation of labeled saccharopine and 2-aminoadipic acid. Formation of [14C]saccharopine was also observed in vitro when cell extracts of P. chrysogenum L2 and Wis 54-1255 were used. Saccharopine dehydrogenase and saccharopine reductase activities were found in cell extracts of P. chrysogenum, which indicates that lysine catabolism may proceed by reversal of the two last steps of the lysine biosynthetic pathway. In addition, a high lysine:2-ketoglutarate-6-aminotransferase activity, which converts lysine into piperideine-6-carboxylic acid, was found in cell extracts of P. chrysogenum. These results suggest that lysine is catabolized to 2-aminoadipic acid in P. chrysogenum by two different pathways. The relative contribution of lysine catabolism in providing 2-aminoadipic acid for penicillin production is discussed.

This article has been cited by other articles:

• Revelles, O., Espinosa-Urgel, M., Fuhrer, T., Sauer, U., Ramos, J. L. (2005). Multiple and Interconnected Pathways for L-Lysine Catabolism in Pseudomonas putida KT2440. J. Bacteriol. 187: 7500-7510 [Abstract] [Full Text]  
• Naranjo, L., Martin de Valmaseda, E., Casqueiro, J., Ullan, R. V., Lamas-Maceiras, M., Banuelos, O., Martin, J. F. (2004). Inactivation of the lys7 Gene, Encoding Saccharopine Reductase in Penicillium chrysogenum, Leads to Accumulation of the Secondary Metabolite Precursors Piperideine-6-Carboxylic Acid and Pipecolic Acid from {alpha}-Aminoadipic Acid. Appl. Environ. Microbiol. 70: 1031-1039 [Abstract] [Full Text]  
• Naranjo, L., de Valmaseda, E. M., Banuelos, O., Lopez, P., Riano, J., Casqueiro, J., Martin, J. F. (2001). Conversion of Pipecolic Acid into Lysine in Penicillium chrysogenum Requires Pipecolate Oxidase and Saccharopine Reductase: Characterization of the lys7 Gene Encoding Saccharopine Reductase. J. Bacteriol. 183: 7165-7172 [Abstract] [Full Text]  
• Casqueiro, J., Gutiérrez, S., Bañuelos, O., Hijarrubia, M. J., Martín, J. F. (1999). Gene Targeting in Penicillium chrysogenum: Disruption of the lys2 Gene Leads to Penicillin Overproduction. J. Bacteriol. 181: 1181-1188 [Abstract] [Full Text]  
• Brakhage, A. A. (1998). Molecular Regulation of beta -Lactam Biosynthesis in Filamentous Fungi. Microbiol. Mol. Biol. Rev. 62: 547-585 [Abstract] [Full Text]