Characterization of 3-phosphoglycerate kinase from Corynebacterium glutamicum and its impact on amino acid production

Komati Reddy G, Wendisch VF (2014)
BMC Microbiology 14(1): 54: 54.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
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Abstract / Bemerkung
Background Corynebacterium glutamicum cg1790/pgk encodes an enzyme active as a 3-phosphoglycerate kinase (PGK) (EC 2.7.2.3) catalyzing phosphoryl transfer from 1,3-biphosphoglycerate (bPG) to ADP to yield 3-phosphoglycerate (3-PG) and ATP in substrate chain phosphorylation. Results C. glutamicum 3-phosphoglycerate kinase was purified to homogeneity from the soluble fraction of recombinant E. coli. PGKHis was found to be active as a homodimer with molecular weight of 104 kDa. The enzyme preferred conditions of pH 7.0 to 7.4 and required Mg2+ for its activity. PGKHis is thermo labile and it has shown maximal activity at 50–65°C. The maximal activity of PGKHis was estimated to be 220 and 150 U mg-1 with KM values of 0.26 and 0.11 mM for 3-phosphoglycerate and ATP, respectively. A 3-phosphoglycerate kinase negative C. glutamicum strain ∆pgk was constructed and shown to lack the ability to grow under glycolytic or gluconeogenic conditions unless PGK was expressed from a plasmid to restore growth. When pgk was overexpressed in L-arginine and L-ornithine production strains the production increased by 8% and by 17.5%, respectively. Conclusion Unlike many bacterial PGKs, C. glutamicum PGK is active as a homodimer. PGK is essential for growth of C. glutamicum with carbon sources requiring glycolysis and gluconeogenesis. Competitive inhibition by ADP reveals the critical role of PGK in gluconeogenesis by energy charge. Pgk overexpression improved the productivity in L-arginine and L-ornithine production strains.
Erscheinungsjahr
2014
Zeitschriftentitel
BMC Microbiology
Band
14
Ausgabe
1
Art.-Nr.
54
Seite(n)
54
ISSN
1471-2180
eISSN
1471-2180
Page URI
https://pub.uni-bielefeld.de/record/2659778

Zitieren

Komati Reddy G, Wendisch VF. Characterization of 3-phosphoglycerate kinase from Corynebacterium glutamicum and its impact on amino acid production. BMC Microbiology. 2014;14(1):54: 54.
Komati Reddy, G., & Wendisch, V. F. (2014). Characterization of 3-phosphoglycerate kinase from Corynebacterium glutamicum and its impact on amino acid production. BMC Microbiology, 14(1), 54., 54. doi:10.1186/1471-2180-14-54
Komati Reddy, G., and Wendisch, V. F. (2014). Characterization of 3-phosphoglycerate kinase from Corynebacterium glutamicum and its impact on amino acid production. BMC Microbiology 14, 54:54.
Komati Reddy, G., & Wendisch, V.F., 2014. Characterization of 3-phosphoglycerate kinase from Corynebacterium glutamicum and its impact on amino acid production. BMC Microbiology, 14(1), p 54: 54.
G. Komati Reddy and V.F. Wendisch, “Characterization of 3-phosphoglycerate kinase from Corynebacterium glutamicum and its impact on amino acid production”, BMC Microbiology, vol. 14, 2014, pp. 54, : 54.
Komati Reddy, G., Wendisch, V.F.: Characterization of 3-phosphoglycerate kinase from Corynebacterium glutamicum and its impact on amino acid production. BMC Microbiology. 14, 54 : 54 (2014).
Komati Reddy, Gajendar, and Wendisch, Volker F. “Characterization of 3-phosphoglycerate kinase from Corynebacterium glutamicum and its impact on amino acid production”. BMC Microbiology 14.1 (2014): 54: 54.
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