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 Daugherty, M.
Right arrow Articles by Osterman, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Daugherty, M.
Right arrow Articles by Osterman, A.
Right arrowPubmed/NCBI databases
*Domain*Gene
*Protein
*Compound via MeSH
*Substance via MeSH

 Previous Article  |  Next Article 

Journal of Bacteriology, January 2001, p. 292-300, Vol. 183, No. 1
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.1.292-300.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Archaeal Shikimate Kinase, a New Member of the GHMP-Kinase Family

Matthew Daugherty, Veronika Vonstein, Ross Overbeek, and Andrei Osterman*

Integrated Genomics Inc., Chicago, Illinois 60612

Received 24 August 2000/Accepted 9 October 2000

Shikimate kinase (EC 2.7.1.71) is a committed enzyme in the seven-step biosynthesis of chorismate, a major precursor of aromatic amino acids and many other aromatic compounds. Genes for all enzymes of the chorismate pathway except shikimate kinase are found in archaeal genomes by sequence homology to their bacterial counterparts. In this study, a conserved archaeal gene (gi|1500322 in Methanococcus jannaschii) was identified as the best candidate for the missing shikimate kinase gene by the analysis of chromosomal clustering of chorismate biosynthetic genes. The encoded hypothetical protein, with no sequence similarity to bacterial and eukaryotic shikimate kinases, is distantly related to homoserine kinases (EC 2.7.1.39) of the GHMP-kinase superfamily. The latter functionality in M. jannaschii is assigned to another gene (gi|1591748), in agreement with sequence similarity and chromosomal clustering analysis. Both archaeal proteins, overexpressed in Escherichia coli and purified to homogeneity, displayed activity of the predicted type, with steady-state kinetic parameters similar to those of the corresponding bacterial kinases: Km,shikimate = 414 ± 33 µM, Km,ATP = 48 ± 4 µM, and kcat = 57 ± 2 s-1 for the predicted shikimate kinase and Km,homoserine = 188 ± 37 µM, Km,ATP = 101 ± 7 µM, and kcat = 28 ± 1 s-1 for the homoserine kinase. No overlapping activity could be detected between shikimate kinase and homoserine kinase, both revealing a >1,000-fold preference for their own specific substrates. The case of archaeal shikimate kinase illustrates the efficacy of techniques based on reconstruction of metabolism from genomic data and analysis of gene clustering on chromosomes in finding missing genes.

* Corresponding author. Mailing address: Integrated Genomics Inc., 2201 W. Campbell Park Dr., Chicago, IL 60612. Phone: (312) 491-0846. Fax: (312) 491-0856. E-mail: andrei{at}integratedgenomics.com.

Journal of Bacteriology, January 2001, p. 292-300, Vol. 183, No. 1
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.1.292-300.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Stockbridge, R. B., Wolfenden, R. (2009). The Intrinsic Reactivity of ATP and the Catalytic Proficiencies of Kinases Acting on Glucose, N-Acetylgalactosamine, and Homoserine: A THERMODYNAMIC ANALYSIS. J. Biol. Chem. 284: 22747-22757 [Abstract] [Full Text]  
  • Fan, C., Fromm, H. J., Bobik, T. A. (2009). Kinetic and Functional Analysis of L-Threonine Kinase, the PduX Enzyme of Salmonella enterica. J. Biol. Chem. 284: 20240-20248 [Abstract] [Full Text]  
  • Mashhadi, Z., Zhang, H., Xu, H., White, R. H. (2008). Identification and Characterization of an Archaeon-Specific Riboflavin Kinase. J. Bacteriol. 190: 2615-2618 [Abstract] [Full Text]  
  • Funke, T., Han, H., Healy-Fried, M. L., Fischer, M., Schonbrunn, E. (2006). Molecular basis for the herbicide resistance of Roundup Ready crops. Proc. Natl. Acad. Sci. USA 103: 13010-13015 [Abstract] [Full Text]  
  • Grochowski, L. L., Xu, H., White, R. H. (2006). Methanocaldococcus jannaschii Uses a Modified Mevalonate Pathway for Biosynthesis of Isopentenyl Diphosphate. J. Bacteriol. 188: 3192-3198 [Abstract] [Full Text]  
  • Gerdes, S. Y., Kurnasov, O. V., Shatalin, K., Polanuyer, B., Sloutsky, R., Vonstein, V., Overbeek, R., Osterman, A. L. (2006). Comparative Genomics of NAD Biosynthesis in Cyanobacteria.. J. Bacteriol. 188: 3012-3023 [Abstract] [Full Text]  
  • Hendrickson, E. L., Kaul, R., Zhou, Y., Bovee, D., Chapman, P., Chung, J., Conway de Macario, E., Dodsworth, J. A., Gillett, W., Graham, D. E., Hackett, M., Haydock, A. K., Kang, A., Land, M. L., Levy, R., Lie, T. J., Major, T. A., Moore, B. C., Porat, I., Palmeiri, A., Rouse, G., Saenphimmachak, C., Soll, D., Van Dien, S., Wang, T., Whitman, W. B., Xia, Q., Zhang, Y., Larimer, F. W., Olson, M. V., Leigh, J. A. (2004). Complete Genome Sequence of the Genetically Tractable Hydrogenotrophic Methanogen Methanococcus maripaludis. J. Bacteriol. 186: 6956-6969 [Abstract] [Full Text]  
  • Galperin, M. Y., Koonin, E. V. (2004). 'Conserved hypothetical' proteins: prioritization of targets for experimental study. Nucleic Acids Res 32: 5452-5463 [Abstract] [Full Text]  
  • Porat, I., Waters, B. W., Teng, Q., Whitman, W. B. (2004). Two Biosynthetic Pathways for Aromatic Amino Acids in the Archaeon Methanococcus maripaludis. J. Bacteriol. 186: 4940-4950 [Abstract] [Full Text]  
  • Singh, S. K., Yang, K., Karthikeyan, S., Huynh, T., Zhang, X., Phillips, M. A., Zhang, H. (2004). The thrH Gene Product of Pseudomonas aeruginosa Is a Dual Activity Enzyme with a Novel Phosphoserine:Homoserine Phosphotransferase Activity. J. Biol. Chem. 279: 13166-13173 [Abstract] [Full Text]  
  • Xie, G., Keyhani, N. O., Bonner, C. A., Jensen, R. A. (2003). Ancient Origin of the Tryptophan Operon and the Dynamics of Evolutionary Change. Microbiol. Mol. Biol. Rev. 67: 303-342 [Abstract] [Full Text]  
  • Miallau, L., Alphey, M. S., Kemp, L. E., Leonard, G. A., McSweeney, S. M., Hecht, S., Bacher, A., Eisenreich, W., Rohdich, F., Hunter, W. N. (2003). Biosynthesis of isoprenoids: Crystal structure of 4-diphosphocytidyl-2C-methyl-D-erythritol kinase. Proc. Natl. Acad. Sci. USA 100: 9173-9178 [Abstract] [Full Text]  
  • Choudhry, A. E., Mandichak, T. L., Broskey, J. P., Egolf, R. W., Kinsland, C., Begley, T. P., Seefeld, M. A., Ku, T. W., Brown, J. R., Zalacain, M., Ratnam, K. (2003). Inhibitors of Pantothenate Kinase: Novel Antibiotics for Staphylococcal Infections. Antimicrob. Agents Chemother. 47: 2051-2055 [Abstract] [Full Text]  
  • Overbeek, R., Larsen, N., Walunas, T., D'Souza, M., Pusch, G., Selkov, E. Jr, Liolios, K., Joukov, V., Kaznadzey, D., Anderson, I., Bhattacharyya, A., Burd, H., Gardner, W., Hanke, P., Kapatral, V., Mikhailova, N., Vasieva, O., Osterman, A., Vonstein, V., Fonstein, M., Ivanova, N., Kyrpides, N. (2003). The ERGOTM genome analysis and discovery system. Nucleic Acids Res 31: 164-171 [Abstract] [Full Text]  
  • Kurnasov, O. V., Polanuyer, B. M., Ananta, S., Sloutsky, R., Tam, A., Gerdes, S. Y., Osterman, A. L. (2002). Ribosylnicotinamide Kinase Domain of NadR Protein: Identification and Implications in NAD Biosynthesis. J. Bacteriol. 184: 6906-6917 [Abstract] [Full Text]  
  • Gerdes, S. Y., Scholle, M. D., D'Souza, M., Bernal, A., Baev, M. V., Farrell, M., Kurnasov, O. V., Daugherty, M. D., Mseeh, F., Polanuyer, B. M., Campbell, J. W., Anantha, S., Shatalin, K. Y., Chowdhury, S. A. K., Fonstein, M. Y., Osterman, A. L. (2002). From Genetic Footprinting to Antimicrobial Drug Targets: Examples in Cofactor Biosynthetic Pathways. J. Bacteriol. 184: 4555-4572 [Abstract] [Full Text]  
  • Daugherty, M., Polanuyer, B., Farrell, M., Scholle, M., Lykidis, A., de Crecy-Lagard, V., Osterman, A. (2002). Complete Reconstitution of the Human Coenzyme A Biosynthetic Pathway via Comparative Genomics. J. Biol. Chem. 277: 21431-21439 [Abstract] [Full Text]  
  • Bonanno, J. B., Edo, C., Eswar, N., Pieper, U., Romanowski, M. J., Ilyin, V., Gerchman, S. E., Kycia, H., Studier, F. W., Sali, A., Burley, S. K. (2001). Structural genomics of enzymes involved in sterol/isoprenoid biosynthesis. Proc. Natl. Acad. Sci. USA 98: 12896-12901 [Abstract] [Full Text]  
  • Yang, D., Shipman, L. W., Roessner, C. A., Scott, A. I., Sacchettini, J. C. (2002). Structure of the Methanococcus jannaschii Mevalonate Kinase, a Member of the GHMP Kinase Superfamily. J. Biol. Chem. 277: 9462-9467 [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»