Corynebacterium glutamicum contains 3-deoxy-D-arabino-heptulosonate 7-phosphate synthases that display novel biochemical features

Applied and Environmental Microbiology

Volumn 74, Issue 17, 2008, Pages 5497-5503

  Liu, Ya Jun ^a   Li, Pan Pan ^a   Zhao, Ke Xin ^a   Wang, Bao Jun ^a   Jiang, Cheng Ying ^a   Drake, Harold L ^b   Liu, Shuang Jiang ^a  

^a INSTITUTE OF MICROBIOLOGY   (China)

^b UNIVERSITY OF BAYREUTH   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

AMINATION; AMINES; AMINO ACIDS; AROMATIC COMPOUNDS; BIOCHEMICAL ENGINEERING; BIOCHEMISTRY; BIOSYNTHESIS; CLONING; ESCHERICHIA COLI; GENETIC ENGINEERING; METAL REFINING; ORGANIC ACIDS; SILICA; SILICATE MINERALS; WATER POLLUTION;

SYNTHASES;

ENZYMES;

3 DEOXY DEXTRO ARABINO HEPTULOSONATE 7 PHOSPHATE SYNTHASE; AMINO ACID; COBALT; MANGANESE; PHENYLALANINE; SYNTHETASE; TRYPTOPHAN; TYROSINE; UNCLASSIFIED DRUG;

AMINO ACID; BACTERIUM; BIOCHEMISTRY; CATALYSIS; CLONE; ENZYME ACTIVITY; GENE EXPRESSION; MUTATION; RECOMBINATION;

ARTICLE; BACTERIAL GENE; BACTERIAL GROWTH; BACTERIAL METABOLISM; CORYNEBACTERIUM GLUTAMICUM; CULTURE MEDIUM; ENZYME ACTIVITY; ESCHERICHIA COLI; GENE DELETION; GENE DISRUPTION; MOLECULAR CLONING; NONHUMAN; PROTEIN EXPRESSION;

3-DEOXY-7-PHOSPHOHEPTULONATE SYNTHASE; AMINO ACIDS, AROMATIC; BACTERIAL PROTEINS; CLONING, MOLECULAR; CORYNEBACTERIUM GLUTAMICUM; DNA, BACTERIAL; ELECTROPHORESIS, GEL, TWO-DIMENSIONAL; ESCHERICHIA COLI; FEEDBACK, BIOCHEMICAL; GENE DELETION; GENES, BACTERIAL; GENETIC COMPLEMENTATION TEST; METALS; PHENOTYPE; PLASMIDS; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION; RNA, BACTERIAL;

CORYNEBACTERIUM GLUTAMICUM; CORYNEBACTERIUM GLUTAMICUM ATCC 13032; ESCHERICHIA COLI;

EID: 50949128449     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.00262-08     Document Type: Article

References (30)

1. Bentley, R. 1990. The shikimate pathway: a metabolic tree with many branches. Crit. Rev. Biochem. Mol. Biol. 25:307-384.
2. Bolotin, A., V. Khazak, N. Stoynova, K. Ratmanova, Y. Yomantas, and Y. Kozlov. 1995. Identical amino acid sequence of the aroA(G) gene products of Bacillus subtilis 168 and B. subtilis Marburg strain. Microbiology 141:2219-2222.
3. Bradford, M. M. 1976. A rapid and sensitive method for the quantization of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
4. Chen, C. C., C. C. Liao, and W. H. Hsu. 1993. The cloning and nucleotide sequence of a Corynebacterium glutamicum 3-deoxy-D- arabinoheptulosonate-7-phosphate synthase gene. FEMS Microbiol. Lett. 107:223-229.
5. Davies, W. D., and B. E. Davidson. 1982. The nucleotide sequence of aroG, the gene for 3-deoxy-D-arabino heptulosonate 7-phosphate synthetase (phe) in Escherichia coli K-12. Nucleic Acids Res. 10:4045-4058.
6. Dixon, M. 1953. The determination of enzyme inhibitor constants. Biochem. J. 55:170-171.
7. Gosset, G., C. A. Bonner, and R. A. Jensen. 2001. Microbial origin of plant-type 2-keto-3-deoxy-D-arabino-heptulosonate 7-phosphate synthases, exemplified by the chorismate- and tryptophan-regulated enzyme from Xanthomonas campestris. J. Bacteriol. 183:4061-4070.
8. Herrmann, K. M. 1983. The common aromatic biosynthetic pathway, p. 301-322. In K. M. Herrmann and R. L. Somervillle (ed.), Amino acids: biosynthsis and genetic regulation. Addison-Wesley, Reading, MA.
9. Ikeda, M. 2005. L-Tryptophan production, p. 489-510. In L. Eggeling and M. Bott (ed.), Handbook of Corynebacterium glutamicum. Taylor & Francis, Boca Raton, FL.
10. Ikeda, M. 2006. Towards bacterial strains overproducing L-tryptophan and other aromatics by metabolic engineering. Appl. Microbiol. Biotechnol. 69:615-626.
11. Ikeda, M., and S. Nakagawa. 2003. The Corynebacterium glutamicum genome: features and impacts on biotechnological processes. Appl. Microbiol. Biotechnol. 62:99-109.
12. Ito, H., K. Sato, K. Matsui, K. Sano, S. Nakamori, and T. Tanaka. 1990. Cloning and characterization of genes responsible for m-fluoro- D, L-phenylalanine resistance in Brevibacterium lactofermentum. Agric. Biol. Chem. 54:707-713.
13. Jakoby, M., C.-E. Ngougto-Nkili, and A. Burkovski. 1999. Construction and application of new Corynebacterium glutamicum vectors. Biotechnol. Tech. 13:437-441.
14. Jensen R. A., and E. W. Nester. 1966. Regulatory enzymes of aromatic amino acid biosynthesis in Bacillus subtilis. I. Purification and properties of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthetase. J. Biol. Chem. 241:3365-3372.
15. Kalinowski, J., B. Bathe, D. Bartels, N. Bischoff, M. Bott, A. Burkovski, N. Dusch, L. Eggeling, B. J. Eikmanns, L. Gaigalat, A. Goesmann, M. Hartmann, K. Huthmacher, R. Krämer, B. Linke, A. C. McHardy, F. Meyer, B. Meckel, W. Pfefferte, A. Pühler, D. A. Rey, C. Rückert, O. Rupp, H. Sahm, V. F. Wendisch, I. Wiegrabe, and A. Tauch. 2003. The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins. J. Biotechnol. 104:5-25.
16. Konopka, A. 1993. Isolation and characterization of subsurface bacterium that degrades aniline and methylanilines. FEMS Microbiol. Lett. 111:93-100.
17. Liao, H. F., L. L. Lin, H. R. Chen, and W. H. Hsu. 2001. Serine 187 is a crucial residue for allosteric regulation of Corynebacterium glutamicum 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase. FEMS Microbiol. Lett. 194:59-64.
18. Liebl, W. 2005. Corynebacterium taxonomy, p. 9-36. In L. Eggeling and M. Bott (ed.). Handbook of Corynebacterium glutamicum. Taylor & Francis, Boca Raton, FL.
19. Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
20. Schäfer, A., A. Tauch, W. Jager, J. Kalinowski, G. Thierbach, and A. Püler. 1994. Small mobilizable multi-purpose cloning vectors derived from the Escherichia coli plasmids pK18 and pK19: selection of defined deletions in the chromosome of Corynebacterium glutamicum. Gene 145:69-73.
21. Shiio, I., S. Sugimoto, and R. Miyajima. 1974. Regulation of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthetase in Brevibacterium flavum. J. Biochem. 75:987-997.
22. Siehl, D. L. 1997. Inhibitors of EPSP synthase, glutamine synthetase and histidine synthesis, p. 37-67. In R. M. Roe et al. (ed.), Toxicology, biochemistry and molecular biology of herbicide activity. IOS Press, Amsterdam, The Netherlands.
23. Sugimoto, S., and I. Shiio. 1980. Purification and properties of bifunctional 3-deoxy-D-arabino-heptulosonate 7-phosphate synthetase-chorismate mutase component A from Brevibacterium flavum. J. Biochem. 87:881-890.
24. Tauch, A., F. Kassing, J. Kalinowski, and A. Pühler. 1995. The Corynebacterium xerosis composite transposon Tn5432 consists of two identical insertion sequences, designated IS1249, flanking the erythromycin resistance gene ermCX. Plasmid 34:119-131.
25. Tauch, A., O. Kirchner, B. Loffler, S. Gotker, A. Puhler, and J. Kalinowski. 2002. Efficient electrotransformation of Corynebacterium diphtheriae with a mini-replicon derived from the Corynebacterium glutamicum plasmid pGA1. Curr. Microbiol. 45:362-367.
26. Umbarger, H. E. 1978. Amino acid biosynthesis and its regulation. Annu. Rev. Biochem. 47:532-606.
27. Walker, G. E., B. Dunbar, I. S. Hunter, H. G. Nimmo, and J. R. Coggins. 1996. Evidence for a novel class of microbial 3-deoxy-D- arabino-heptulosonate-7-phosphate synthase in Streptomyces coelicolor A3(2), Streptomyces rimosus and Neurospora crassa. Microbiology 142:1973-1982.
28. Wu, J., G. Y. Sheflyan, and R. W. Woodard. 2005. Bacillus subtilis 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase revisited: resolution of two long-standing enigmas. Biochem. J. 390:583-590.
29. Zurawski, G., K. Brown, D. Killingly, and C. Yanofsky. 1978. Nucleotide sequence of the leader region of the phenylalanine Operon of Escherichia coli. Proc. Natl. Acad. Sci. USA 75:4271-4275.
30. Zurawski, G., R. P. Gunsalus, K. D. Brown, and C. Yanofsky. 1981. Structure and regulation of aroH, the structural gene for the tryptophan-repressible 3-deoxy-D-arabino-heptulosonic acid 7-phosphate synthetase of Escherichia coli. J. Mol. Biol. 145:47-73.