Steric course of the hydration of D-gluco-octenitol catalyzed by α-glucosidases and by trehalase

Wolfgang Weiser, Jochen Lehmann, Seiya Chiba, Hirokazu Matsui, Curtis F. Brewer, Edward J. Hehre

Research output: Contribution to journalArticle

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Abstract

Crystalline Aspergillus niger α-glucosidase and highly purified preparations of rice α-glucosidase II and Trichoderma reesei trehalase were found to catalyze the hydration of [2-2H]-D-gluco-octenitol, i.e., (Z)-3,7-anhydro-1,2-dideoxy-[2-2H]-D-gluco-oct-2-enitol, to yield 1,2-dideoxy-[2-2H]-D-gluco-octulose. In each case, the stereochemistry of the reaction was elucidated by examining the newly formed centers of asymmetry at C-2 and C-3 of the hydration product. The C-1 to C-3 fragment of each isolated [2-2H]-D-gluco-octulose product was recovered as [2-2H]propionic acid and identified by its positive optical rotatory dispersion as the S isomer, showing that each enzyme had protonated the octenitol (at C-2) from above its re face. 1H NMR spectra of enzyme/D-gluco-octenitol digests in D2O showed that the α-anomer of [2-2H]-D-gluco-octulose was exclusively produced by each α-glucosidase, whereas the β-anomer was formed by action of the trehalase. The trans hydration catalyzed by the α-glucosidases was found to be very strongly inhibited by the substrate; the cis hydration reaction catalyzed by the trehalase showed no such inhibition. Special importance is attached to the finding that in hydrating octenitol each enzyme creates a product of the same anomeric form as in hydrolyzing an α-D-glucosidic substrate. This result adds substantially to the growing evidence that individual glycpsylases create the configuration of their reaction products by a means that is independent of donor substrate configuration, that is, by a means other than "retaining" or "inverting" substrate configuration.

Original languageEnglish (US)
Pages (from-to)2294-2300
Number of pages7
JournalBiochemistry®
Volume27
Issue number7
StatePublished - 1988

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Trehalase
Glucosidases
Hydration
Substrates
Enzymes
Optical Rotatory Dispersion
Trichoderma
Aspergillus niger
Stereochemistry
Aspergillus
Reaction products
Isomers
Nuclear magnetic resonance
Crystalline materials
3,7-anhydro-1,2-dideoxygluco-oct-2-enitol

ASJC Scopus subject areas

  • Biochemistry

Cite this

Weiser, W., Lehmann, J., Chiba, S., Matsui, H., Brewer, C. F., & Hehre, E. J. (1988). Steric course of the hydration of D-gluco-octenitol catalyzed by α-glucosidases and by trehalase. Biochemistry®, 27(7), 2294-2300.

Steric course of the hydration of D-gluco-octenitol catalyzed by α-glucosidases and by trehalase. / Weiser, Wolfgang; Lehmann, Jochen; Chiba, Seiya; Matsui, Hirokazu; Brewer, Curtis F.; Hehre, Edward J.

In: Biochemistry®, Vol. 27, No. 7, 1988, p. 2294-2300.

Research output: Contribution to journalArticle

Weiser, W, Lehmann, J, Chiba, S, Matsui, H, Brewer, CF & Hehre, EJ 1988, 'Steric course of the hydration of D-gluco-octenitol catalyzed by α-glucosidases and by trehalase', Biochemistry®, vol. 27, no. 7, pp. 2294-2300.
Weiser, Wolfgang ; Lehmann, Jochen ; Chiba, Seiya ; Matsui, Hirokazu ; Brewer, Curtis F. ; Hehre, Edward J. / Steric course of the hydration of D-gluco-octenitol catalyzed by α-glucosidases and by trehalase. In: Biochemistry®. 1988 ; Vol. 27, No. 7. pp. 2294-2300.
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