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 Yvon, M.
Right arrow Articles by Roudot-Algaron, F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Yvon, M.
Right arrow Articles by Roudot-Algaron, F.
Agricola
Right arrow Articles by Yvon, M.
Right arrow Articles by Roudot-Algaron, F.

 Previous Article  |  Next Article 

Applied and Environmental Microbiology, February 2000, p. 571-577, Vol. 66, No. 2
0099-2240/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Characterization and Role of the Branched-Chain Aminotransferase (BcaT) Isolated from Lactococcus lactis subsp. cremoris NCDO 763

Mireille Yvon,1,* Emilie Chambellon,1 Alexander Bolotin,2 and Florence Roudot-Algaron1

Unité de Recherche de Biochimie et Structure des Protéines1 and Laboratoire de Génétique Microbienne,2 I.N.R.A., 78352 Jouy-en-Josas, France

Received 18 August 1999/Accepted 9 November 1999

In Lactococcus lactis, which is widely used as a starter in the cheese industry, the first step of aromatic and branched-chain amino acid degradation is a transamination which is catalyzed by two major aminotransferases. We have previously purified and characterized biochemically and genetically the aromatic aminotransferase, AraT. In the present study, we purified and studied the second enzyme, the branched-chain aminotransferase, BcaT. We cloned and sequenced the corresponding gene and used a mutant, along with the luciferase gene as the reporter, to study the role of the enzyme in amino acid metabolism and to reveal the regulation of gene transcription. BcaT catalyzes transamination of the three branched-chain amino acids and methionine and belongs to class IV of the pyridoxal 5'-phosphate-dependent aminotransferases. In contrast to most of the previously described bacterial BcaTs, which are hexameric, this enzyme is homodimeric. It is responsible for 90% of the total isoleucine and valine aminotransferase activity of the cell and for 50 and 40% of the activity towards leucine and methionine, respectively. The original role of BcaT was probably biosynthetic since expression of its gene was repressed by free amino acids and especially by isoleucine. However, in dairy strains, which are auxotrophic for branched-chain amino acids, BcaT functions only as a catabolic enzyme that initiates the conversion of major aroma precursors. Since this enzyme is still active under cheese-ripening conditions, it certainly plays a major role in cheese flavor development.

* Corresponding author. Mailing address: Unité de Recherche de Biochimie et Structure des Protéines, I.N.R.A., 78352 Jouy-en-Josas, 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, February 2000, p. 571-577, Vol. 66, No. 2
0099-2240/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Bachmann, H., Kruijswijk, Z., Molenaar, D., Kleerebezem, M., van Hylckama Vlieg, J. E. T. (2009). A high-throughput cheese manufacturing model for effective cheese starter culture screening. J DAIRY SCI 92: 5868-5882 [Abstract] [Full Text]  
  • Bachmann, H., Starrenburg, M. J. C., Dijkstra, A., Molenaar, D., Kleerebezem, M., Rademaker, J. L. W., van Hylckama Vlieg, J. E. T. (2009). Regulatory Phenotyping Reveals Important Diversity within the Species Lactococcus lactis. Appl. Environ. Microbiol. 75: 5687-5694 [Abstract] [Full Text]  
  • 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]  
  • Hullo, M.-F., Auger, S., Soutourina, O., Barzu, O., Yvon, M., Danchin, A., Martin-Verstraete, I. (2007). Conversion of Methionine to Cysteine in Bacillus subtilis and Its Regulation. J. Bacteriol. 189: 187-197 [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]  
  • Tanous, C., Chambellon, E., Le Bars, D., Delespaul, G., Yvon, M. (2006). Glutamate Dehydrogenase Activity Can Be Transmitted Naturally to Lactococcus lactis Strains To Stimulate Amino Acid Conversion to Aroma Compounds. Appl. Environ. Microbiol. 72: 1402-1409 [Abstract] [Full Text]  
  • Gitton, C., Meyrand, M., Wang, J., Caron, C., Trubuil, A., Guillot, A., Mistou, M.-Y. (2005). Proteomic Signature of Lactococcus lactis NCDO763 Cultivated in Milk. Appl. Environ. Microbiol. 71: 7152-7163 [Abstract] [Full Text]  
  • den Hengst, C. D., van Hijum, S. A. F. T., Geurts, J. M. W., Nauta, A., Kok, J., Kuipers, O. P. (2005). The Lactococcus lactis CodY Regulon: IDENTIFICATION OF A CONSERVED cis-REGULATORY ELEMENT. J. Biol. Chem. 280: 34332-34342 [Abstract] [Full Text]  
  • Cernat Bondar, D., Beckerich, J.-M., Bonnarme, P. (2005). Involvement of a Branched-Chain Aminotransferase in Production of Volatile Sulfur Compounds in Yarrowia lipolytica. Appl. Environ. Microbiol. 71: 4585-4591 [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]  
  • Ganesan, B., Seefeldt, K., Weimer, B. C. (2004). Fatty Acid Production from Amino Acids and {alpha}-Keto Acids by Brevibacterium linens BL2. Appl. Environ. Microbiol. 70: 6385-6393 [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]  
  • Miyazaki, T., Miyazaki, J., Yamane, H., Nishiyama, M. (2004). {alpha}-Aminoadipate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus. Microbiology 150: 2327-2334 [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]  
  • Matalon, R., Surendran, S., Matalon, K. M., Tyring, S., Quast, M., Jinga, W., Ezell, E., Szucs, S. (2003). Future Role of Large Neutral Amino Acids in Transport of Phenylalanine Into the Brain. Pediatrics 112: 1570-1574 [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]  
  • Berger, B. J., English, S., Chan, G., Knodel, M. H. (2003). Methionine Regeneration and Aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis. J. Bacteriol. 185: 2418-2431 [Abstract] [Full Text]  
  • Kieronczyk, A., Skeie, S., Langsrud, T., Yvon, M. (2003). Cooperation between Lactococcus lactis and Nonstarter Lactobacilli in the Formation of Cheese Aroma from Amino Acids. Appl. Environ. Microbiol. 69: 734-739 [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]  
  • Thierry, A., Maillard, M.-B., Yvon, M. (2002). Conversion of L-Leucine to Isovaleric Acid by Propionibacterium freudenreichii TL 34 and ITGP23. Appl. Environ. Microbiol. 68: 608-615 [Abstract] [Full Text]  
  • Dudley, E. G., Steele, J. L. (2001). Lactococcus lactis LM0230 contains a single aminotransferase involved in aspartate biosynthesis, which is essential for growth in milk. Microbiology 147: 215-224 [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]  
  • Bolotin, A., Wincker, P., Mauger, S., Jaillon, O., Malarme, K., Weissenbach, J., Ehrlich, S. D., Sorokin, A. (2001). The Complete Genome Sequence of the Lactic Acid Bacterium Lactococcus lactis ssp. lactis IL1403. Genome Res 11: 731-753 [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»