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Trehalase and the enzymes of trehalose biosynthesis in lilium longiflorum m pollen






Phytochemistry (Oxford) 9(9): 1915-1920

Trehalase and the enzymes of trehalose biosynthesis in lilium longiflorum m pollen

Lilium longiflorum cv. “Ace”, contained a trehalase which was not bound to cell structure. The enzyme was active over a broad range of pH, with an optimum at 5·4. It had an energy of activation of 8·2 kcal/mole, a transition temp. of 56°, and was exceptionally heat stable, retaining full activity when incubated at 50° for 30 min in the absence of substrate. The enzyme had a Km of 1 × 103 M for trehalose and was competitively inhibited by phloridzin. The enzymes of trehalose biosynthesis—hexokinase, phosphoglucomutase, UDPG pyrophosphorylase, trehalose-6-P synthetase, and trehalose-6-P phosphatase—were present in pollen; all except hexokinase were fully soluble.


Accession: 006839058

DOI: 10.1016/S0031-9422(00)85339-X



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