Plant Physiol. Journal of Pharmacology and Experimental Therapeutics
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Plant Physiology 51:998-1001 (1973)
© 1973 American Society of Plant Biologists

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Substrate Activation of {beta}-(1 -> 3) Glucan Synthetase and Its Effect on the Structure of {beta}-Glucan Obtained from UDP-D-glucose and Particulate Enzyme of Oat Coleoptiles 1

C. M. Tsai2 and W. Z. Hassid

a Department of Biochemistry, University of California, Berkeley, California 94720

UDP-D-glucose, at a micromolar level in the presence of MgCl2 and oat (Avena sativa) coleoptile particulate enzyme which contains both {beta}-(1 -> 3) and {beta}-(1 -> 4) glucan synthetases, produces glucan with mainly {beta}-(1 -> 4) glucosyl linkages. An activation of {beta}-(1 -> 3) glucan synthetase by UDP-D-glucose and a decrease in the formation of {beta}-(1 -> 3) glucan in the presence of MgCl2 have been observed. However, at high substrate concentration (≥ 10–4M), the activation of {beta}-(1 -> 3) glucan synthetase is so pronounced that the formation of {beta}-(1 -> 3) glucosyl linkage predominates in synthesized glucan regardless of the presence of MgCl2. These observations may explain the striking shift in the composition of glucan of particulate enzyme from a {beta}-(1 -> 4) to {beta}-(1 -> 3) glucosyl linkage when UDP-D-glucose concentration is raised from a low concentration (≤ 10–5M) to a higher concentration (≥ 10–4M).

Besides UDP-D-glucose, CDP-D-glucose can also serve as substrate for the formation of {beta}-(1 -> 3) glucan in the presence of {beta}-(1 -> 3) synthetase.

2 Present address: Yale University School of Medicine, Department of Pharmacology, 333 Cedar Street, New Haven, Conn. 06510.

1 This investigation was supported in part by Research Grant A-1418 from the National Institutes of Health, United States Public Health Service, and by Research Grant GB 11819 from the National Science Foundation. Support of this work by the Agricultural Experiment Station of the University of California is also acknowledged.






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