| Literature DB >> 16665132 |
J E Pinto1, J A Suzich, K M Herrmann.
Abstract
3-Deoxy-d-arabino-heptulosonate 7-phosphate synthase, the first enzyme of the shikimate pathway, was purified to electrophoretic homogeneity from tubers of Solanum tuberosum L. cv Superior. The enzyme is a dimer with a native molecular weight of 110,000. The enzyme appears to be hysteretic. The enzyme activity is stimulated by Mn(2+) and l-tryptophan. Chromatofocusing resolved two forms of the enzyme with isoelectric points of 7.8 and 8.4, respectively. The enzyme closely resembles an analogous activity previously isolated from roots of Daucus carota (JA Suzich, JFD Dean, KM Herrmann 1985 Plant Physiol 79: 765-770).Entities:
Year: 1986 PMID: 16665132 PMCID: PMC1056255 DOI: 10.1104/pp.82.4.1040
Source DB: PubMed Journal: Plant Physiol ISSN: 0032-0889 Impact factor: 8.340