Studies on the Biosynthesis of Cyclitols, XXXV (1) . On the Mechanism of Action of myo-Inositol-1-phosphate Synthase from Rat Testicles

Studies on the Biosynthesis of Cyclitols, XXXV (1) . On the Mechanism of Action of... Hoppe-Seyler's Z. Physiol. Chem. Bd. 357, S. 1667 -1671, Dezember 1976 Studies on the Biosynthesis of Cyclitols, XXXVUI On the Mechanism of Action of m.yo-Inositol-1 -phosphate Synthase from Rat Testicles Fritz PITTNER and Otto HOFFMANN-OSTENHOF Institut für Allgemeine Biochemie der Universität Wien, and Ludwig-Boltzmann-Forschungsstelle für Biochemie, Wien (Received'l6 September/8 November 1976) Summary: The animal myo-inositol-I-phosphate synthase is competitively inhibited by pyridoxal phosphate and trinitrobenzenesulphonate, both compounds known to prevent Schiffs base formation. When incubated with labelled substrate and then treated with NaBH4, label can be recovered in the enzyme protein. In analogous experiments with tritiated NaBH4 the enzyme pro- tein also becomes labelled; after hydrolysis of such protein only one labelled compound, derived from lysine and D-glucose 6-phosphate, could be isolated. Its exact structure is not yet known. From these results it can be concluded that during its action myo-inositol-1 -phosphate synthase forms a Schiffs base with its substrate, in analogy to the class I aldolases. Untersuchungen über die Biosynthese der Cyelite, XXXV Über den Wirkungsmechanismus von myo-Inosit-1-phosphat-Synthase aus Rattenhoden Zusammenfassung: Die tierische myo-Inosit-1gebaut. Nach Hydrolyse dieses Proteins wird nur phosphat-Synthase wird durch Pyridoxalphosphat eine einzige markierte Verbindung isoliert, die ein und durch Trinitrobenzolsulfonat kompetitiv ge- Produkt aus http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png hoppe-seyler's zeitschrift für physiologische chemie de Gruyter

Studies on the Biosynthesis of Cyclitols, XXXV (1) . On the Mechanism of Action of myo-Inositol-1-phosphate Synthase from Rat Testicles

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Publisher
de Gruyter
Copyright
Copyright © 1976 by the
ISSN
0018-4888
eISSN
1437-4315
DOI
10.1515/bchm2.1976.357.2.1667
Publisher site
See Article on Publisher Site

Abstract

Hoppe-Seyler's Z. Physiol. Chem. Bd. 357, S. 1667 -1671, Dezember 1976 Studies on the Biosynthesis of Cyclitols, XXXVUI On the Mechanism of Action of m.yo-Inositol-1 -phosphate Synthase from Rat Testicles Fritz PITTNER and Otto HOFFMANN-OSTENHOF Institut für Allgemeine Biochemie der Universität Wien, and Ludwig-Boltzmann-Forschungsstelle für Biochemie, Wien (Received'l6 September/8 November 1976) Summary: The animal myo-inositol-I-phosphate synthase is competitively inhibited by pyridoxal phosphate and trinitrobenzenesulphonate, both compounds known to prevent Schiffs base formation. When incubated with labelled substrate and then treated with NaBH4, label can be recovered in the enzyme protein. In analogous experiments with tritiated NaBH4 the enzyme pro- tein also becomes labelled; after hydrolysis of such protein only one labelled compound, derived from lysine and D-glucose 6-phosphate, could be isolated. Its exact structure is not yet known. From these results it can be concluded that during its action myo-inositol-1 -phosphate synthase forms a Schiffs base with its substrate, in analogy to the class I aldolases. Untersuchungen über die Biosynthese der Cyelite, XXXV Über den Wirkungsmechanismus von myo-Inosit-1-phosphat-Synthase aus Rattenhoden Zusammenfassung: Die tierische myo-Inosit-1gebaut. Nach Hydrolyse dieses Proteins wird nur phosphat-Synthase wird durch Pyridoxalphosphat eine einzige markierte Verbindung isoliert, die ein und durch Trinitrobenzolsulfonat kompetitiv ge- Produkt aus

Journal

hoppe-seyler's zeitschrift für physiologische chemiede Gruyter

Published: Jan 1, 1976

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