Developmental changes of enzymes involved in conversion of sucrose to hexose-phosphate during early tuberisation of potato
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- Appeldoorn, N., de Bruijn, S., Koot-Gronsveld, E. et al. Planta (1997) 202: 220. doi:10.1007/s004250050122
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A highly synchronised in-vitro tuberisation system, based on single-node cuttings containing an axillary bud, was used to investigate the activity patterns of enzymes involved in the conversion of sucrose to hexose-phosphates during stolon-to-tuber transition of potato (Solanum tuberosum L.). Two different non-tuberising systems were included to distinguish between changes that are or are not tuber-specific. At tuberisation the activity of soluble acid invertase decreased (13-fold) and of sucrose synthase increased (12-fold). The activity of both enzymes remained unchanged in the non-tuberising treatments. Based on the opposite patterns and large difference in activity of these two sucrolytic enzymes, we conclude that sucrose synthase constitutes the predominant route of sucrose breakdown after tuber initiation. During the period before tuberisation, the activity of cell-wall-bound invertase and of hexokinase showed a highly positive correlation (r2 = 0.96 in all the three treatments, suggesting coordinated coarse control of both enzyme activities. After the onset of tuberisation cell-wall-bound invertase activity decreased to a very low level, a change not observed in the non-tuberising systems, indicating that cell-wall-bound invertase is presumably not involved in the unloading mechanism and/or short-distance transport of sucrose within the perimedulla of growing tubers. The overall activity of fructokinase and of hexokinase both showed a fourfold increase after tuber initiation, but remained unchanged in the non-tuberising systems. The increase of fructokinase suggests that the phosphorylation of fructose by fructokinase down-regulates the cytosolic fructose content in order to maintain a high sucrose-synthase-catalysed net flux of sucrose to phosphorylated hexoses during rapid tuber growth. The increase of total glucose-phosphorylating potential could be a response to the tuberisation-related starch accumulation process. The activity of UDP-glucose pyrophosphorylase showed no developmental change. The level of UDP-glucose pyrophosphorylase activity is very likely the result of metabolic regulation.