This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Rijnen, L.
Right arrow Articles by Yvon, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Rijnen, L.
Right arrow Articles by Yvon, M.
Agricola
Right arrow Articles by Rijnen, L.
Right arrow Articles by Yvon, M.

 Previous Article  |  Next Article 

Applied and Environmental Microbiology, November 1999, p. 4873-4880, Vol. 65, No. 11
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Genetic Characterization of the Major Lactococcal Aromatic Aminotransferase and Its Involvement in Conversion of Amino Acids to Aroma Compounds

Liesbeth Rijnen,1 Sophie Bonneau,2 and Mireille Yvon1,*

Unité de Recherches de Biochimie et Structure des Protéines1 and Laboratoire de Génétique Microbienne,2 INRA, 78352 Jouy-en-Josas Cedex, France

Received 25 January 1999/Accepted 17 August 1999

In lactococci, transamination is the first step of the enzymatic conversion of aromatic and branched-chain amino acids to aroma compounds. In previous work we purified and biochemically characterized the major aromatic aminotransferase (AraT) of a Lactococcus lactis subsp. cremoris strain. Here we characterized the corresponding gene and evaluated the role of AraT in the biosynthesis of amino acids and in the conversion of amino acids to aroma compounds. Amino acid sequence homologies with other aminotransferases showed that the enzyme belongs to a new subclass of the aminotransferase I subfamily gamma ; AraT is the best-characterized representative of this new aromatic-amino-acid-specific subclass. We demonstrated that AraT plays a major role in the conversion of aromatic amino acids to aroma compounds, since gene inactivation almost completely prevented the degradation of these amino acids. It is also highly involved in methionine and leucine conversion. AraT also has a major physiological role in the biosynthesis of phenylalanine and tyrosine, since gene inactivation weakly slowed down growth on medium without phenylalanine and highly affected growth on every medium without tyrosine. However, another biosynthesis aromatic aminotransferase is induced in the absence of phenylalanine in the culture medium.

* Corresponding author. Mailing address: Unité de Recherches de Biochimie et Structure des Protéines, INRA, Centre de Recherches de Jouy-en-Josas, Domaine de Vilvert, 78352 Jouy-en-Josas, Cedex, France. Phone: 33 1 34 65 21 59. Fax: 33 1 34 65 21 63. E-mail: Mireille.Yvon{at}diamant.jouy.inra.fr.

Applied and Environmental Microbiology, November 1999, p. 4873-4880, Vol. 65, No. 11
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Liu, M., Nauta, A., Francke, C., Siezen, R. J. (2008). Comparative Genomics of Enzymes in Flavor-Forming Pathways from Amino Acids in Lactic Acid Bacteria. Appl. Environ. Microbiol. 74: 4590-4600 [Full Text]  
  • Irmler, S., Raboud, S., Beisert, B., Rauhut, D., Berthoud, H. (2008). Cloning and Characterization of Two Lactobacillus casei Genes Encoding a Cystathionine Lyase. Appl. Environ. Microbiol. 74: 99-106 [Abstract] [Full Text]  
  • Martinez-Cuesta, M. C., Pelaez, C., Eagles, J., Gasson, M. J., Requena, T., Hanniffy, S. B. (2006). YtjE from Lactococcus lactis IL1403 Is a C-S Lyase with {alpha},{gamma}-Elimination Activity toward Methionine.. Appl. Environ. Microbiol. 72: 4878-4884 [Abstract] [Full Text]  
  • Ganesan, B., Dobrowolski, P., Weimer, B. C. (2006). Identification of the Leucine-to-2-Methylbutyric Acid Catabolic Pathway of Lactococcus lactis.. Appl. Environ. Microbiol. 72: 4264-4273 [Abstract] [Full Text]  
  • den Hengst, C. D., Curley, P., Larsen, R., Buist, G., Nauta, A., van Sinderen, D., Kuipers, O. P., Kok, J. (2005). Probing Direct Interactions between CodY and the oppD Promoter of Lactococcus lactis. J. Bacteriol. 187: 512-521 [Abstract] [Full Text]  
  • Helinck, S., Le Bars, D., Moreau, D., Yvon, M. (2004). Ability of Thermophilic Lactic Acid Bacteria To Produce Aroma Compounds from Amino Acids. Appl. Environ. Microbiol. 70: 3855-3861 [Abstract] [Full Text]  
  • van der Kaaij, H., Desiere, F., Mollet, B., Germond, J.-E. (2004). L-Alanine Auxotrophy of Lactobacillus johnsonii as Demonstrated by Physiological, Genomic, and Gene Complementation Approaches. Appl. Environ. Microbiol. 70: 1869-1873 [Abstract] [Full Text]  
  • Ganesan, B., Weimer, B. C. (2004). Role of Aminotransferase IlvE in Production of Branched-Chain Fatty Acids by Lactococcus lactis subsp. lactis. Appl. Environ. Microbiol. 70: 638-641 [Abstract] [Full Text]  
  • Chambellon, E., Yvon, M. (2003). CodY-Regulated Aminotransferases AraT and BcaT Play a Major Role in the Growth of Lactococcus lactis in Milk by Regulating the Intracellular Pool of Amino Acids. Appl. Environ. Microbiol. 69: 3061-3068 [Abstract] [Full Text]  
  • Madsen, S. M., Beck, H. C., Ravn, P., Vrang, A., Hansen, A. M., Israelsen, H. (2002). Cloning and Inactivation of a Branched-Chain-Amino-Acid Aminotransferase Gene from Staphylococcus carnosus and Characterization of the Enzyme. Appl. Environ. Microbiol. 68: 4007-4014 [Abstract] [Full Text]  
  • Aubel, D., Germond, J. E., Gilbert, C., Atlan, D. (2002). Isolation of the patC gene encoding the cystathionine {beta}-lyase of Lactobacillus delbrueckii subsp. bulgaricus and molecular analysis of inter-strain variability in enzyme biosynthesis. Microbiology 148: 2029-2036 [Abstract] [Full Text]  
  • Rijnen, L., Courtin, P., Gripon, J.-C., Yvon, M. (2000). Expression of a Heterologous Glutamate Dehydrogenase Gene in Lactococcus lactis Highly Improves the Conversion of Amino Acids to Aroma Compounds. Appl. Environ. Microbiol. 66: 1354-1359 [Abstract] [Full Text]  
  • Yvon, M., Chambellon, E., Bolotin, A., Roudot-Algaron, F. (2000). Characterization and Role of the Branched-Chain Aminotransferase (BcaT) Isolated from Lactococcus lactis subsp. cremoris NCDO 763. Appl. Environ. Microbiol. 66: 571-577 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»