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Plant Physiology 70:765-770 (1982) © 1982 American Society of Plant Biologists myo-Inositol-1-Phosphatase from the Pollen of Lilium longiflorum Thunb. 1Institute of Biological Chemistry, Washington State University, Pullman, Washington 99164
A Mg2+-dependent, alkaline phosphatase has been isolated from mature pollen of Lilium longiflorum Thunb., cv. Ace and partially purified. It hydrolyzes 1L- and 1D-myo-inositol 1-phosphate, myo-inositol 2-phosphate, and In higher plants this myo-inositol-1-phosphatase links myo-inositol biosynthesis to the myo-inositol oxidation pathway to produce an alternative path from D-glucose 6-phosphate to UDP-D-glucuronate that bypasses UDP-D-glucose dehydrogenase. myo-Inositol-1-phosphatase also furnishes free myo-inositol for reactions that lead to other cyclitols and cyclitol-containing compounds of biosynthetic and/or regulatory significance in plant growth and development.
2 To whom inquiries and requests for reprints should be addressed. 1 Supported by Grant GM-22427 from the National Institute of General Medical Sciences, National Institutes of Health, United States Public Health Service. Scientific Paper No. 6173, Project 0266, College of Agriculture Research Center, Washington State University, Pullman, WA 99164. This article has been cited by other articles:
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