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Ream JE, Steinrücken HC, Porter CA, et al. Purification and Properties of 5-Enolpyruvylshikimate-3-Phosphate Synthase from Dark-Grown Seedlings of Sorghum bicolor. Plant Physiol. 1988;87(1):232-8doi: 10.1104/pp.87.1.232.
Ream, J. E., Steinrücken, H. C., Porter, C. A., & Sikorski, J. A. (1988). Purification and Properties of 5-Enolpyruvylshikimate-3-Phosphate Synthase from Dark-Grown Seedlings of Sorghum bicolor. Plant physiology, 87(1), 232-8. https://doi.org/10.1104/pp.87.1.232
Ream, J E, et al. "Purification and Properties of 5-Enolpyruvylshikimate-3-Phosphate Synthase from Dark-Grown Seedlings of Sorghum bicolor." Plant physiology vol. 87,1 (1988): 232-8. doi: https://doi.org/10.1104/pp.87.1.232
Ream JE, Steinrücken HC, Porter CA, Sikorski JA. Purification and Properties of 5-Enolpyruvylshikimate-3-Phosphate Synthase from Dark-Grown Seedlings of Sorghum bicolor. Plant Physiol. 1988 May;87(1):232-8. doi: 10.1104/pp.87.1.232. PMID: 16666109; PMCID: PMC1054731.
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Plant Physiol. 1988 May;87(1):232-8. doi: 10.1104/pp.87.1.232.

Purification and Properties of 5-Enolpyruvylshikimate-3-Phosphate Synthase from Dark-Grown Seedlings of Sorghum bicolor.

Plant physiology

J E Ream, H C Steinrücken, C A Porter, J A Sikorski

Affiliations

  1. Monsanto Agricultural Company, Monsanto Company, Technology Division, St. Louis, Missouri 63167.

PMID: 16666109 PMCID: PMC1054731 DOI: 10.1104/pp.87.1.232

Abstract

5-Enolpyruvylshikimate-3-phosphate (EPSP) synthase (3-phospho-shikimate 1-carboxyvinyltransferase; EC 2.5.1.19) was purified 1300-fold from etiolated shoots of Sorghum bicolor (L.) Moench. Native polyacrylamide gel electrophoresis revealed three barely separated protein bands staining positive for EPSP synthase activity. The native molecular weight was determined to be 51,000. Enzyme activity was found to be sensitive to metal ions and salts. Apparent K(m) values of 7 and 8 micromolar were determined for the substrates shikimate-3-phosphate and phosphoenolpyruvate (PEP), respectively. The herbicide glyphosate was found to inhibit the enzyme competitively with respect to PEP (K(i) = 0.16 micromolar). Characterization studies support the conclusion of a high degree of similarity between EPSP synthase from S. bicolor, a monocot, and the enzyme from dicots. A similarity to bacterial EPSP synthase is also discussed. Three EPSP synthase isozymes (I, II, III) were elucidated in crude homogenates of S. bicolor shoots by high performance liquid chromatography. The major isozymes, II and III, were separated and partially characterized. No significant differences in pH activity profiles and glyphosate sensitivity were found. This report of isozymes of EPSP synthase from S. bicolor is consistent with other reports for shikimate pathway enzymes, including EPSP synthase.

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