The ‘pH optimum anomaly’ of intracellular enzymes of Ferroplasma acidiphilum
Article first published online: 7 SEP 2005
Volume 8, Issue 3, pages 416–425, March 2006
How to Cite
Golyshina, O. V., Golyshin, P. N., Timmis, K. N. and Ferrer, M. (2006), The ‘pH optimum anomaly’ of intracellular enzymes of Ferroplasma acidiphilum. Environmental Microbiology, 8: 416–425. doi: 10.1111/j.1462-2920.2005.00907.x
- Issue published online: 14 FEB 2006
- Article first published online: 7 SEP 2005
- Received 20 April, 2005; accepted 18 July, 2005.
A wide range of microorganisms, the so-called acidophiles, inhabit acidic environments and grow optimally at pH values between 0 and 3. The intracellular pH of these organisms is, however, close to neutrality or slightly acidic. It is to be expected that enzymatic activities dedicated to extracellular functions would be adapted to the prevailing low pH of the environment (0–3), whereas intracellular enzymes would be optimally active at the near-neutral pH of the cytoplasm (4.6–7.0). The genes of several intracellular or cell-bound enzymes, a carboxylesterase and three α-glucosidases, from Ferroplasma acidiphilum, a cell wall-lacking acidophilic archaeon with a growth optimum at pH 1.7, were cloned and expressed in Escherichia coli, and their products purified and characterized. The Ferroplasmaα-glucosidases exhibited no sequence similarity to known glycosyl hydrolases. All enzymes functioned and were stable in vitro in the pH range 1.7–4.0, and had pH optima much lower than the mean intracellular pH of 5.6. This ‘pH optimum anomaly’ suggests the existence of yet-undetected cellular compartmentalization providing cytoplasmic pH patchiness and low pH environments for the enzymes we have analysed.