Exopolyphosphatases PPX1 and PPX2 from Corynebacterium glutamicum

Lindner S, Knebel S, Wesseling H, Schoberth SM, Wendisch VF (2009)
Applied and Environmental Microbiology 75(10): 3161-3170.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
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Lindner, SteffenUniBi; Knebel, S.; Wesseling, H.; Schoberth, S. M.; Wendisch, Volker F.UniBi
Abstract / Bemerkung
Corynebacterium glutamicum accumulates up to 300 mM of inorganic polyphosphate (PolyP) in the cytosol or in granules. The gene products of cg0488 (ppx1) and cg1115 (ppx2) were shown to be active as exopolyphosphatases (PPX), as overexpression of either gene resulted in higher exopolyphosphatase activities in crude extracts and deletion of either gene with lower activities than those of the wild-type strain. PPX1 and PPX2 from C. glutamicum share only 25% identical amino acids and belong to different protein groups, which are distinct from enterobacterial, archaeal, and yeast exopolyphosphatases. In comparison to that in the wild type, more intracellular PolyP accumulated in the Delta ppx1 and Delta ppx2 deletion mutations but less when either ppx1 or ppx2 was overexpressed. When C. glutamicum was shifted from phosphate-rich to phosphate-limiting conditions, a growth advantage of the deletion mutants and a growth disadvantage of the overexpression strains compared to the wild type were observed. Growth experiments, exopolyphosphatase activities, and intracellular PolyP concentrations revealed PPX2 as being a major exopolyphosphatase from C. glutamicum. PPX2(His) was purified to homogeneity and shown to be active as a monomer. The enzyme required Mg2+ or Mn2+ cations but was inhibited by millimolar concentrations of Mg2+, Mn2+, and Ca2+center dot PPX2 from C. glutamicum was active with short-chain polyphosphates, even accepting pyrophosphate, and was inhibited by nucleoside triphosphates.
kinase; mycobacterium-tuberculosis; soluble exopolyphosphatase; chain exopolyphosphatase; biochemical-characterization; escherichia-coli; gene; pseudomonas-aeruginosa; inorganic polyphosphate; saccharomyces-cerevisiae
Applied and Environmental Microbiology
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Lindner S, Knebel S, Wesseling H, Schoberth SM, Wendisch VF. Exopolyphosphatases PPX1 and PPX2 from Corynebacterium glutamicum. Applied and Environmental Microbiology. 2009;75(10):3161-3170.
Lindner, S., Knebel, S., Wesseling, H., Schoberth, S. M., & Wendisch, V. F. (2009). Exopolyphosphatases PPX1 and PPX2 from Corynebacterium glutamicum. Applied and Environmental Microbiology, 75(10), 3161-3170. https://doi.org/10.1128/Aem.02705-08
Lindner, Steffen, Knebel, S., Wesseling, H., Schoberth, S. M., and Wendisch, Volker F. 2009. “Exopolyphosphatases PPX1 and PPX2 from Corynebacterium glutamicum”. Applied and Environmental Microbiology 75 (10): 3161-3170.
Lindner, S., Knebel, S., Wesseling, H., Schoberth, S. M., and Wendisch, V. F. (2009). Exopolyphosphatases PPX1 and PPX2 from Corynebacterium glutamicum. Applied and Environmental Microbiology 75, 3161-3170.
Lindner, S., et al., 2009. Exopolyphosphatases PPX1 and PPX2 from Corynebacterium glutamicum. Applied and Environmental Microbiology, 75(10), p 3161-3170.
S. Lindner, et al., “Exopolyphosphatases PPX1 and PPX2 from Corynebacterium glutamicum”, Applied and Environmental Microbiology, vol. 75, 2009, pp. 3161-3170.
Lindner, S., Knebel, S., Wesseling, H., Schoberth, S.M., Wendisch, V.F.: Exopolyphosphatases PPX1 and PPX2 from Corynebacterium glutamicum. Applied and Environmental Microbiology. 75, 3161-3170 (2009).
Lindner, Steffen, Knebel, S., Wesseling, H., Schoberth, S. M., and Wendisch, Volker F. “Exopolyphosphatases PPX1 and PPX2 from Corynebacterium glutamicum”. Applied and Environmental Microbiology 75.10 (2009): 3161-3170.

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