Biotechnology and Bioprocess Engineering:BBE

The Korean Society for Biotechnology and Bioengineering (한국생물공학회)
권호 표지

Cloning and Characterization of Mannheimia succiniciproducens MBEL55E Phosphoenolpyruvate Carboxykinase (pckA) Gene

  • Lee, Sang-Yup (Metabolic and Biomolecular Engineering, National Research Laboratory, Department of Chemical & Biomolecular Engineering and BioProcess Engineering, Research Center, Korea Advanced Institute of Science and Technology) ;
  • Lee, Pyung-Cheon (Metabolic and Biomolecular Engineering, National Research Laboratory, Department of Chemical & Biomolecular Engineering and BioProcess Engineering, Research Center, Korea Advanced Institute of Science and Technology) ;
  • Hong, Soon-Ho (Metabolic and Biomolecular Engineering National Research Laboratory) ;
  • Chang, Ho-Nam (Department of Chemical & Biomoleculr Engineering and BioProcess Engineering Research Center, Korea Advanced Institute of Science and Technology)
  • Published : 2002.03.01
Download PDF
⟨ Previous Next ⟩

Abstract

A pckA gene encoding phosphoenolpyruvate carboxykinase (PEPCK) was cloned and sequenced from the succinic acid producing bacterium Mannheimia succiniciproducens MBEL55E. The gene encoded a 538 residue polypeptide with a calculated molecular mass of 58.8 kDa and a calculated pI of 5.03. The deduced amino acid sequence of the M. succiniciprodutens MBEL55E PEPCK was similar to those of all known ATP-dependent PEPCKS.

Keywords

References

  1. J. Biol. Chem. v.272 Structure and mechanism of phosphoenolpyruvate carboxykinase Matte, A.;L.W. Tari;H. Goldie;L.T.J. Delbaere https://doi.org/10.1074/jbc.272.13.8105
  2. J. Gen. Microbiol. v.139 Purification and characterization of phosphoenolpyruvate carboxykinase, a catabolic CO₂-fixing enzyme, from Anaerobiospirillum succiniciproducens Podkovyrove, S.M.;J.G. Zeikus https://doi.org/10.1099/00221287-139-2-223
  3. J. Biol. Chem. v.249 Phosphoenolpyruvate carboxykinase from bakers yeast. Kinetics of phosphoenolpyruvate formation Cannata, J.B.;M.A.C. de Flombaum
  4. Biochemistry v.20 Phosphoenolpyruvate carboxykinase (guanosine 5'-triphosphate) from rat liver cytosol. Dual-action requirement for the carboxylation reaction Colombo, G.;G.M. Carlson;H.A. Lardy https://doi.org/10.1021/bi00513a008
  5. Eur. J. Biochem. v.52 On the activity and regulation of anaplerotic and gluconeogenic enzymes during the growth process of baker's yeast Haarasilta, S.;E. Oura https://doi.org/10.1111/j.1432-1033.1975.tb03966.x
  6. Biochem. Biophys. Res. Commun. v.59 Two routes for synthesis of phosphoenolpyruvate from C4-dicarboxylic acids Hansen, E.J.;E. Juni https://doi.org/10.1016/0006-291X(74)90442-2
  7. J. Microbiol. Biotechnol. v.9 Enhancement of succinate production by organic solvents, detergents, and vegetable oils Kang, K.H.;H.W. Ryu
  8. J. Microbiol. Biotechnol. v.10 Metabolic flux distribution in a metabolically engineered Escherichia coli strain producing succinic acid Hong, S.H.;S.Y. Lee
  9. Enzyme Microb. Technol. v.24 Succinic acid production by Anaerobiospirillum succiniciproducens: Effects of the H₂/CO₂supply and glucose concentration Lee, P.C.;W.G. Lee;S. Kwon;S.Y. Lee;H.N. Chang https://doi.org/10.1016/S0141-0229(98)00156-2
  10. Biotechnol. Bioeng. v.72 Succinic acid production with reduced by-product formation the fermentation of Anaerobiospirillum succinicproducens using glycerol as a carbon source Lee, P.C.;W.G. Lee;S.Y. Lee;H.N. Chang
  11. Arch. Microbiol. v.167 Environmental and physiological factors affecting the succinate product ratio during carbohydrate fermentation by Actinobacillus sp. 120Z van der Werf, M.J.;M.V. Guettler;M.K. Jain;J.G. Zeikus https://doi.org/10.1007/s002030050452
  12. J. Bacteriol. v.134 Pathway of succinate and propionate formation in Bacteroides fragilis Macy, J.M.;L.G. Ljungdahl;G. Gottschalk
  13. J. Bacteriol. v.172 Sequence of the pckA gene of Escherichia coli K-12: relevance to genetic and allosteric regulation and homology of E. coli phosphoenolpyruvate carboxykinase with the enzymes from Trypanosoma brucei and Saccharomyces cerevisiae Medina, V.;R. Pontarollo;D. Glaeske;H. Tabel;H. Goldie https://doi.org/10.1128/jb.172.12.7151-7156.1990
  14. J. Bacteriol. v.177 Molecular and expression analysis of the Rhizobium meliloti phosphoenolpyruvate carboxykinase (pckA) gene Qsteras, M.;B.T. Driscoll;T.M. Finan https://doi.org/10.1128/jb.177.6.1452-1460.1995
  15. Mol Gen. Genet. v.230 Sitedirected mutagenesis and DNA sequence of pckA of Rhizobium NGR234, encoding phosphoenolpyruvate carboxykinase: gluconeogenesis and host-dependent symbiotic phenotype Qsteras, M.;T.M. Finan;J. Stanley https://doi.org/10.1007/BF00290676
  16. J. Bacteriol. v.178 Identification and characterization of the pckA gene from Staphylococcus aureus Scovill, W.H.;H.J. Schreier;K.W. Bayles https://doi.org/10.1128/jb.178.11.3362-3364.1996
  17. J. Bacteriol. v.181 Molecular and functional characterization of the Rhodopseudomonas palustris no. 7 phosphoenolpyruvate carboxykinase gene Inui, M.;K. Nakata;J.H. Roh;K. Zahn;H. Yukawa
  18. Appl. Environ. Microbiol. v.63 Cloning, sequencing, and overexpression of the Anaerobiospirillum succiniciproducens phosphoenolpyruvate carboxykinase (pckA) gene Laivenieks, M.;C. Vieille;J.G. Zeikus
  19. Biotechnol. Bioprocess Eng. v.5 Fermentative production of succinic acid from glucose and corn steep liquor by Anaerobiospirillium succiniciproducens Lee, P.C.;W.G. Lee;S.Y. Lee;H.N. Chang;Y.K. Chang https://doi.org/10.1007/BF02942216
  20. Molecular Cloning: A Laboratory Manual.(2nd ed.) Sambrook, J.;E.F. Fritsch;T. Maniatis
  21. Gene Function in Prokaryotes Beckwith, J.;J. Davies;J.A. Gallant
  22. J. Mol. Biol. v.256 Crystal structure of Escherichia coli phosphoenolpyruvate carboxykinase: a new structural family with the P-loop nucleotiside triphosphate hydrolase fold Matte, A.;H. Goldie;R.M. Sweet;L.T. Delbaere https://doi.org/10.1006/jmbi.1996.0072
  23. Nat. Struct. Biol. v.3 Snapshot of an enzyme reaction intermediate in the structure of the ATP-Mg²+-oxalate ternary complex of Escherichia coli PEP carboxykinase Tari, L.W.;A. Matte;U. Pugazhenthi;H. Goldie;L.T. Delbaere https://doi.org/10.1038/nsb0496-355