Expression of the Escherichia coli pntAB genes encoding a membrane-bound transhydrogenase in Corynebacterium glutamicum improves L-lysine formation

Kabus A, Georgi T, Wendisch VF, Bott M (2007)
Applied Microbiology and Biotechnology 75(1): 47-53.

Journal Article | Published | English

No fulltext has been uploaded

Author
; ; ;
Abstract
A critical factor in the biotechnological production of (L)-lysine with Corynebacterium glutamicum is the sufficient supply of NADPH. The membrane-integral nicotinamide nucleotide transhydrogenase PntAB of Escherichia coli can use the electrochemical proton gradient across the cytoplasmic membrane to drive the reduction of NADP(+) stop via the oxidation of NADH. As C. glutamicum does not possess such an enzyme, we expressed the E. coli pntAB genes in the genetically defined C. glutamicum lysine-producing strain DM1730, resulting in membrane-associated transhydrogenase activity of 0.7 U/mg protein. When cultivated in minimal medium with 10% (w/v) carbon source, the presence of transhydrogenase slightly reduced glucose consumption, whereas the consumption of fructose, glucose plus fructose, and, in particular, sucrose was stimulated. Biomass was increased by pntAB expression between 10 and 30% on all carbon sources tested. Most importantly, the lysine concentration was increased in the presence of transhydrogenase by similar to 10% on glucose, similar to 70% on fructose, similar to 50% on glucose plus fructose, and even by similar to 300% on sucrose. Thus, the presence of a proton-coupled transhydrogenase was shown to be an efficient way to improve lysine production by C. glutamicum. In contrast, pntAB expression had a negative effect on growth and glutamate production of C. glutamicum wild type.
Publishing Year
ISSN
eISSN
PUB-ID

Cite this

Kabus A, Georgi T, Wendisch VF, Bott M. Expression of the Escherichia coli pntAB genes encoding a membrane-bound transhydrogenase in Corynebacterium glutamicum improves L-lysine formation. Applied Microbiology and Biotechnology. 2007;75(1):47-53.
Kabus, A., Georgi, T., Wendisch, V. F., & Bott, M. (2007). Expression of the Escherichia coli pntAB genes encoding a membrane-bound transhydrogenase in Corynebacterium glutamicum improves L-lysine formation. Applied Microbiology and Biotechnology, 75(1), 47-53.
Kabus, A., Georgi, T., Wendisch, V. F., and Bott, M. (2007). Expression of the Escherichia coli pntAB genes encoding a membrane-bound transhydrogenase in Corynebacterium glutamicum improves L-lysine formation. Applied Microbiology and Biotechnology 75, 47-53.
Kabus, A., et al., 2007. Expression of the Escherichia coli pntAB genes encoding a membrane-bound transhydrogenase in Corynebacterium glutamicum improves L-lysine formation. Applied Microbiology and Biotechnology, 75(1), p 47-53.
A. Kabus, et al., “Expression of the Escherichia coli pntAB genes encoding a membrane-bound transhydrogenase in Corynebacterium glutamicum improves L-lysine formation”, Applied Microbiology and Biotechnology, vol. 75, 2007, pp. 47-53.
Kabus, A., Georgi, T., Wendisch, V.F., Bott, M.: Expression of the Escherichia coli pntAB genes encoding a membrane-bound transhydrogenase in Corynebacterium glutamicum improves L-lysine formation. Applied Microbiology and Biotechnology. 75, 47-53 (2007).
Kabus, A., Georgi, T., Wendisch, Volker F., and Bott, M. “Expression of the Escherichia coli pntAB genes encoding a membrane-bound transhydrogenase in Corynebacterium glutamicum improves L-lysine formation”. Applied Microbiology and Biotechnology 75.1 (2007): 47-53.
This data publication is cited in the following publications:
This publication cites the following data publications:

42 Citations in Europe PMC

Data provided by Europe PubMed Central.

NADPH-generating systems in bacteria and archaea.
Spaans SK, Weusthuis RA, van der Oost J, Kengen SW., Front Microbiol 6(), 2015
PMID: 26284036
A giant market and a powerful metabolism: L-lysine provided by Corynebacterium glutamicum.
Eggeling L, Bott M., Appl. Microbiol. Biotechnol. 99(8), 2015
PMID: 25761623
Increasing available NADH supply during succinic acid production by Corynebacterium glutamicum.
Zhou Z, Wang C, Chen Y, Zhang K, Xu H, Cai H, Chen Z., Biotechnol. Prog. 31(1), 2015
PMID: 25311136
Construction of a novel expression system for use in Corynebacterium glutamicum.
Hu J, Li Y, Zhang H, Tan Y, Wang X., Plasmid 75(), 2014
PMID: 25108235
Application of metabolic engineering for the biotechnological production of L-valine.
Oldiges M, Eikmanns BJ, Blombach B., Appl. Microbiol. Biotechnol. 98(13), 2014
PMID: 24816722
Metabolic engineering and transhydrogenase effects on NADPH availability in Escherichia coli.
Jan J, Martinez I, Wang Y, Bennett GN, San KY., Biotechnol. Prog. 29(5), 2013
PMID: 23794523
Effects of NADH kinase on NADPH-dependent biotransformation processes in Escherichia coli.
Lee WH, Kim JW, Park EH, Han NS, Kim MD, Seo JH., Appl. Microbiol. Biotechnol. 97(4), 2013
PMID: 23053084
Optimization of enzyme parameters for fermentative production of biorenewable fuels and chemicals.
Jarboe LR, Liu P, Kautharapu KB, Ingram LO., Comput Struct Biotechnol J 3(), 2012
PMID: 24688665

42 References

Data provided by Europe PubMed Central.

Response of the central metabolism of Corynebacterium glutamicum to different flux burdens.
Marx A, Striegel K, de Graaf AA, Sahm H, Eggeling L., Biotechnol. Bioeng. 56(2), 1997
PMID: 18636622
Response of the central metabolism in Corynebacterium glutamicum to the use of an NADH-dependent glutamate dehydrogenase.
Marx A, Eikmanns BJ, Sahm H, de Graaf AA, Eggeling L., Metab. Eng. 1(1), 1999
PMID: 10935753
Metabolic phenotype of phosphoglucose isomerase mutants of Corynebacterium glutamicum.
Marx A, Hans S, Mockel B, Bathe B, de Graaf AA, McCormack AC, Stapleton C, Burke K, O'Donohue M, Dunican LK., J. Biotechnol. 104(1-3), 2003
PMID: 12948638
Analyses of enzyme II gene mutants for sugar transport and heterologous expression of fructokinase gene in Corynebacterium glutamicum ATCC 13032.
Moon MW, Kim HJ, Oh TK, Shin CS, Lee JS, Kim SJ, Lee JK., FEMS Microbiol. Lett. 244(2), 2005
PMID: 15766777
A novel methodology employing Corynebacterium glutamicum genome information to generate a new L-lysine-producing mutant.
Ohnishi J, Mitsuhashi S, Hayashi M, Ando S, Yokoi H, Ochiai K, Ikeda M., Appl. Microbiol. Biotechnol. 58(2), 2002
PMID: 11876415
Corynebacterium glutamicum: a dissection of the PTS.
Parche S, Burkovski A, Sprenger GA, Weil B, Kramer R, Titgemeyer F., J. Mol. Microbiol. Biotechnol. 3(3), 2001
PMID: 11361073
Biotechnological manufacture of lysine.
Pfefferle W, Mockel B, Bathe B, Marx A., Adv. Biochem. Eng. Biotechnol. 79(), 2003
PMID: 12523389

A, Biotechnol Bioeng 51(), 1996
Ethambutol, a cell wall inhibitor of Mycobacterium tuberculosis, elicits L-glutamate efflux of Corynebacterium glutamicum.
Radmacher E, Stansen KC, Besra GS, Alderwick LJ, Maughan WN, Hollweg G, Sahm H, Wendisch VF, Eggeling L., Microbiology (Reading, Engl.) 151(Pt 5), 2005
PMID: 15870446
Pathway analysis and metabolic engineering in Corynebacterium glutamicum.
Sahm H, Eggeling L, de Graaf AA., Biol. Chem. 381(9-10), 2000
PMID: 11076021
Measurement of protein using bicinchoninic acid.
Smith PK, Krohn RI, Hermanson GT, Mallia AK, Gartner FH, Provenzano MD, Fujimoto EK, Goeke NM, Olson BJ, Klenk DC., Anal. Biochem. 150(1), 1985
PMID: 3843705

Export

0 Marked Publications

Open Data PUB

Web of Science

View record in Web of Science®

Sources

PMID: 17216441
PubMed | Europe PMC

Search this title in

Google Scholar