Broad-specificity quinate (shikimate) dehydrogenase from Pinus taeda needles
In: Plant physiology and biochemistry (Paris), Jg. 38 (2000), Heft 12, S. 923-928
academicJournal
- print, 18 ref
Zugriff:
Two proteins having quinate dehydrogenase (QDH, quinate:NAD(P)+-oxidoreductase, EC 1.1.1.24) and shikimate dehydrogenase (SDH, shikimate:NADP+-oxidoreductase, EC 1.1.1.25) activities were purified about 3 000-fold from young loblolly pine (Pinus taeda L.) needles. A combination of ammonium sulfate solubilization, and chromatographies on DEAE-cellulose, 2', 5' ADP-Sepharose and Mono-Q was used. Throughout all purification steps, the QDH activity consistently co-purified with the activity of the first of three forms of SDH, and the ratio of QDH/SDH was constant (variation from 1.63 to 1.89). These data indicate that both QDH and SDH activities are catalyzed by a single broad-specificity quinate (shikimate) dehydrogenase. Gel chromatography on Superdex 75 was used to estimate the native molecular mass of two forms of the enzyme as 35 and 53 kDa.
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Broad-specificity quinate (shikimate) dehydrogenase from Pinus taeda needles
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Autor/in / Beteiligte Person: | OSSIPOV, Vladimir ; BONNER, Carol ; OSSIPOVA, Svetlana ; JENSEN, Roy |
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Zeitschrift: | Plant physiology and biochemistry (Paris), Jg. 38 (2000), Heft 12, S. 923-928 |
Veröffentlichung: | Paris: Elsevier, 2000 |
Medientyp: | academicJournal |
Umfang: | print, 18 ref |
ISSN: | 0981-9428 (print) |
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