Add time:08/04/2019         Source:sciencedirect.com

Activity of 6-Hydroxymellein (cas 19314-92-2) synthase, an inducible polyketide biosynthetic enzyme in carrot cell extracts, was appreciably inhibited in the presence of molar levels of NaCl or (NH4)2SO4. However, the salt-induced inhibition of the synthase activity was reversible, and was almost fully restored after the salts were removed. Highly purified 6-hydroxymellein synthase showed essentially one band of Mr 128 000 as analysed by SDS-PAGE. However, in gelfiltration analysis, the synthase activity was recovered in fractions corresponding to Mr 285 000 when the enzyme was eluted with buffered saline. By contrast, the enzyme protein was eluted at the position of Mr 136 000 with loss of the activity under high-salt condition. Activity of the Mr 136 000 peptide was restored after desalting. The Mr of the reactivated enzyme was found to shift to 285 000. The results suggest that two polypeptides associate and form an active 6-hydroxymellein synthase.

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