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Galactosylononitol and Stachyose Synthesis in Seeds of Adzuki Bean1
Purification and Characterization of Stachyose Synthase

Thomas Peterbauer and Andreas Richter*

Institute of Plant Physiology, University of Vienna, A-1091 Vienna, Austria

Stachyose synthase (STS) (EC 2.4.1.67) was purified to homogeneity from mature seeds of adzuki bean (Vigna angularis). Electrophoresis under denaturing conditions revealed a single polypeptide of 90 kD. Size-exclusion chromatography of the purified enzyme yielded two activity peaks with apparent molecular masses of 110 and 283 kD. By isoelectric focusing and chromatofocusing the protein was separated into several active forms with isoelectric point values between pH 4.7 and 5.0. Purified STS catalyzed the transfer of the galactosyl group from galactinol to raffinose and myo-inositol. Additionally, the enzyme catalyzed the galactinol-dependent synthesis of galactosylononitol from d-ononitol. The synthesis of a galactosylcyclitol by STS is a new oberservation. Mutual competitive inhibition was observed when the enzyme was incubated with both substrates (raffinose and ononitol) simultaneously. Galactosylononitol could also substitute for galactinol in the synthesis of stachyose from raffinose. Although galactosylononitol was the less-efficient donor, the Michaelis constant value for raffinose was lower in the presence of galactosylononitol (13.2 mm) compared with that obtained in the presence of galactinol (38.6 mm). Our results indicate that STS catalyzes the biosynthesis of galactosylononitol, but may also mediate a redistribution of galactosyl residues from galactosylononitol to stachyose.

1   This work was supported by the Austrian Science Foundation (project no. P10917-BIO).
*   Corresponding author; e-mail arichter{at}pflaphy.pph.univie.ac.at; fax 43-1-31336-776.

Plant Physiol. (1998) 117: 165-172
Copyright Clearance Center:   0032-0889/98/117/0165/08
© 1998 American Society of Plant Physiologists




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