A novel RPMXR motif among class II 5-enolpyruvylshikimate-3-phosphate synthases is required for enzymatic activity and glyphosate resistance

Journal of Biotechnology

Volumn 144, Issue 4, 2009, Pages 330-336

  Li, Liang ^a   Lu, Wei ^a   Han, Yunlei ^b   Ping, Shuzhen ^a   Zhang, Wei ^a   Chen, Ming ^a   Zhao, Zhonglin ^a   Yan, Yongliang ^a   Jiang, Yan ^b   Lin, Min ^a  

^a INSTITUTE OF PLANT PROTECTION   (China)

^b SICHUAN UNIVERSITY   (China)

Author keywords

Class II 5 enolpyruvylshikimate 3 phosphate synthase; Enzymatic activity; Glyphosate resistance; Pseudomonas stutzeri A1501; RPMXR motif

Indexed keywords

CLASS II; CLASS II 5-ENOLPYRUVYLSHIKIMATE-3-PHOSPHATE SYNTHASE; ENZYMATIC ACTIVITIES; GLYPHOSATES; PSEUDOMONAS STUTZERI; SYNTHASES;

ACID RESISTANCE; AMINES; AMINO ACIDS; HERBICIDES; ORGANIC ACIDS; THREE DIMENSIONAL;

ENZYMES;

3 PHOSPHOSHIKIMATE 1 CARBOXYVINYLTRANSFERASE; AMINO ACID; ARGININE; ASPARAGINE; GLYPHOSATE; HERBICIDE; METHIONINE; PHOSPHOENOLPYRUVATE; PROLINE; SHIKIMIC ACID; SHIKIMIC ACID DERIVATIVE;

AMINO ACID SUBSTITUTION; ARTICLE; CONSENSUS SEQUENCE; CONTROLLED STUDY; DRUG TARGETING; ENZYME ACTIVITY; GENETIC CONSERVATION; HERBICIDE RESISTANCE; MOLECULAR INTERACTION; MUTATIONAL ANALYSIS; NONHUMAN; PRIORITY JOURNAL; PSEUDOMONAS STUTZERI;

3-PHOSPHOSHIKIMATE 1-CARBOXYVINYLTRANSFERASE; AMINO ACID MOTIFS; AMINO ACID SEQUENCE; CONSERVED SEQUENCE; DRUG RESISTANCE, BACTERIAL; ENZYME INHIBITORS; ESCHERICHIA COLI; GLYCINE; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PHOSPHOENOLPYRUVATE; SHIKIMIC ACID; STRUCTURE-ACTIVITY RELATIONSHIP;

PSEUDOMONAS STUTZERI;

EID: 70449726477     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2009.09.014     Document Type: Article

References (18)

1. Bentley R. The shikimate pathway-a metabolic tree with many branches. Crit. Rev. Biochem. Mol. Biol. 25 (1990) 307-387
2. Eschenburg S., Healy M.L., Priestman M.A., Lushington G.H., and Schönbrunn E. How the mutation glycine96 to alanine confers glyphosate insensitivity to 5-enolpyruvyl shikimate-3-phosphate synthase from Escherichia coli. Planta 216 (2002) 129-135
3. Franz J.E., Mao M.K., and Sikorski J.A. Glyphosate: A Unique Global Herbicide (1997), American Chemical Society, Washington, DC
4. Funke T., Han H., Healy-Fried M.L., Fischer M., and Schönbrunn E. Molecular basis for the herbicide resistance of Roundup Ready crops. Proc. Natl. Acad. Sci. U.S.A. 103 (2006) 13010-13015
5. Funke T., Yang Y., Han H., Healy-Fried M.L., Olesen S., Becker A., and Schönbrunn E. Structural basis of glyphosate tolerance resulting from the double mutation Thr97Ala and Pro101Ser in 5-enolpyruvyl-shikimate-3-phosphate synthase from Escherichia coli. J. Biol. Chem. 15 (2009) 9854-9860
6. Hewett-Emmett D., and Tashian R.E. Functional diversity, conservation, and convergence in the evolution of the alpha-, beta-, and gamma-carbonic anhydrase gene families. Mol. Phylogenet. Evol. 5 (1996) 50-77
7. James C. Global status of commercialized biotech/GM crops: 2008. International Service for the Acquisition of Agri-Biotech Applications Brief No. 39 (2008), ISAAA, Ithaca, NY
8. Lanzetta P.A., Alvarez L.J., Reinach P.S., and Candia O.A. An improved assay for nanomole amounts of inorganic phosphate. Anal. Biochem. 100 (1979) 95-97
9. Liang A., Sha J., Lu W., Chen M., Li L., Jin D., Yan Y., Wang J., Ping S., Zhang W., Wang Y., and Lin M. A single residue mutation of 5-enoylpyruvylshikimate-3-phosphate synthase in Pseudomonas stutzeri A1501 enhances resistance to the herbicide glyphosate. Biotechnol. Lett. 30 (2008) 1397-1401
10. Marques M.R., Pereira J.H., Oliveira J.S., Basso L.A., de Azevedo Jr. W.F., Santos D.S., and Palma M.S. The inhibition of 5-enolpyruvylshikimate-3-phosphate synthase as a model for development of novel antimicrobials. Curr. Drug Targets 8 (2007) 445-457
11. Marques M.R., Vaso A., Neto J.R., Fossey M.A., Oliveira J.S., Basso L.A., dos Santos D.S., de Azevedo Junior W.F., and Palma M.S. Dynamics of glyphosate-induced conformational changes of Mycobacterium tuberculosis 5-enolpyruvylshikimate-3-phosphate synthase (EC 2.5.1.19) determined by hydrogen-deuterium exchange and electrospray mass spectrometry. Biochemistry 47 (2008) 7509-7522
12. Park H., Hilsenbeck J.L., Kim H.J., Shuttleworth W.A., Park Y.H., Evans J.N., and Kang C. Structural studies of Streptococcus pneumoniae EPSP synthase in unliganded state, tetrahedral intermediate-bound state and S3P-GLP-bound state. Mol. Microbiol. 51 (2004) 963-971
13. Pettersen E.F., Goddard T.D., Huang C.C., Couch G.S., Greenblatt D.M., Meng E.C., and Ferrin T.E. UCSF chimera-a visualization system for exploratory research and analysis. J. Comput. Chem. 25 (2004) 1605-1612
14. Roberts F., Roberts C.W., Johnson J.J., Kyle D.E., Krell T., Coggins J.R., Coombs G.H., Milhous W.K., Tzipori S., Ferguson D.J., Chakrabarti D., and McLeod R. Evidence for the shikimate pathway in apicomplexan parasites. Nature 393 (1998) 801-805
15. Schönbrunn E., Eschenburg S., Shuttleworth W.A., Schloss J.V., Amrhein N., Evans J.N., and Kabsch W. Interaction of the herbicide glyphosate with its target enzyme 5-enolpyruvylshikimate 3-phosphate synthase in atomic detail. Proc. Natl. Acad. Sci. U.S.A. 98 (2001) 1376-1380
16. Shuttleworth W.A., Pohl M.E., Helms G.L., Jakeman D.L., and Evans J.N. Site-directed mutagenesis of putative active site residues of 5-enolpyruvylshikimate-3-phosphate synthase. Biochemistry 38 (1999) 296-302
17. Stallings W.C., Abdel-Meguid S.S., Lim L.W., Shieh H.S., Dayringer H.E., Leimgruber N.K., Stegeman R.A., Anderson K.S., Sikorski J.A., Padgette S.R., and Kishore G.M. Structure and topological symmetry of the glyphosate target 5-enolpyruvylshikimate-3-phosphate synthase: a distinctive protein fold. Proc. Natl. Acad. Sci. U.S.A. 88 (1991) 5046-5050
18. Yan Y., Yang J., Dou Y., Chen M., Ping S., Peng J., Lu W., Zhang W., Yao Z., Li H., Liu W., He S., Geng L., Zhang X., Yang F., Yu H., Zhan Y., Li D., Lin Z., Wang Y., Elmerich C., Lin M., and Jin Q. Nitrogen fixation island and rhizosphere competence traits in the genome of root-associated Pseudomonas stutzeri A1501. Proc. Natl. Acad. Sci. U.S.A. 105 (2008) 7564-7569