Substrate-induced activation of maltose phosphorylase: Interaction with the anomeric hydroxyl group of α-maltose and α-d-glucose controls the enzyme's glucosyltransferase activity

Yoichi Tsumuraya, Curtis F. Brewer, Edward J. Hehre

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Abstract

Maltose phosphorylase, long considered strictly specific for β-d-glucopyranosyl phosphate (β-d-glucose 1-P), was found to catalyze the reaction β-d-glucosyl fluoride + α-d-glucose → α-maltose + HF, at a rapid rate, V = 11.2 ± 1.2 μmol/(min·mg), and K = 13.1 ± 4.4 mM with α-d-glucose saturating, at 0 °C. This reaction is analogous to the synthesis of maltose from β-d-glucose 1-P + d-glucose (the reverse of maltose phosphorolysis). In acting upon β-d-glucosyl fluoride, maltose phosphorylase was found to use α-d-glucose as a cosubstrate but not β-d-glucose or other close analogs (e.g., α-d-glucosyl fluoride) lacking an axial 1-OH group. Similarly, the enzyme was shown to use α-maltose as a substrate but not β-maltose or close analogs (e.g., α-maltosyl fluoride) lacking an axial 1-OH group. These results indicate that interaction of the axial 1-OH group of the disaccharide donor or sugar acceptor with a particular protein group near the reaction center is required for effective catalysis. This interaction appears to be the means that leads maltose phosphorylase to promote a narrowly defined set of glucosyl transfer reactions with little hydrolysis, in contrast to other glycosylases that catalyze both hydrolytic and nonhydrolytic reactions.

Original languageEnglish (US)
Pages (from-to)58-65
Number of pages8
JournalArchives of Biochemistry and Biophysics
Volume281
Issue number1
DOIs
StatePublished - Aug 15 1990

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maltose phosphorylase
Glucosyltransferases
Maltose
Enzyme activity
Hydroxyl Radical
Chemical activation
Glucose
Substrates
Enzymes
Disaccharides
Catalysis
Fluorides
Sugars
Hydrolysis

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

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title = "Substrate-induced activation of maltose phosphorylase: Interaction with the anomeric hydroxyl group of α-maltose and α-d-glucose controls the enzyme's glucosyltransferase activity",
abstract = "Maltose phosphorylase, long considered strictly specific for β-d-glucopyranosyl phosphate (β-d-glucose 1-P), was found to catalyze the reaction β-d-glucosyl fluoride + α-d-glucose → α-maltose + HF, at a rapid rate, V = 11.2 ± 1.2 μmol/(min·mg), and K = 13.1 ± 4.4 mM with α-d-glucose saturating, at 0 °C. This reaction is analogous to the synthesis of maltose from β-d-glucose 1-P + d-glucose (the reverse of maltose phosphorolysis). In acting upon β-d-glucosyl fluoride, maltose phosphorylase was found to use α-d-glucose as a cosubstrate but not β-d-glucose or other close analogs (e.g., α-d-glucosyl fluoride) lacking an axial 1-OH group. Similarly, the enzyme was shown to use α-maltose as a substrate but not β-maltose or close analogs (e.g., α-maltosyl fluoride) lacking an axial 1-OH group. These results indicate that interaction of the axial 1-OH group of the disaccharide donor or sugar acceptor with a particular protein group near the reaction center is required for effective catalysis. This interaction appears to be the means that leads maltose phosphorylase to promote a narrowly defined set of glucosyl transfer reactions with little hydrolysis, in contrast to other glycosylases that catalyze both hydrolytic and nonhydrolytic reactions.",
author = "Yoichi Tsumuraya and Brewer, {Curtis F.} and Hehre, {Edward J.}",
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T1 - Substrate-induced activation of maltose phosphorylase

T2 - Interaction with the anomeric hydroxyl group of α-maltose and α-d-glucose controls the enzyme's glucosyltransferase activity

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AU - Brewer, Curtis F.

AU - Hehre, Edward J.

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N2 - Maltose phosphorylase, long considered strictly specific for β-d-glucopyranosyl phosphate (β-d-glucose 1-P), was found to catalyze the reaction β-d-glucosyl fluoride + α-d-glucose → α-maltose + HF, at a rapid rate, V = 11.2 ± 1.2 μmol/(min·mg), and K = 13.1 ± 4.4 mM with α-d-glucose saturating, at 0 °C. This reaction is analogous to the synthesis of maltose from β-d-glucose 1-P + d-glucose (the reverse of maltose phosphorolysis). In acting upon β-d-glucosyl fluoride, maltose phosphorylase was found to use α-d-glucose as a cosubstrate but not β-d-glucose or other close analogs (e.g., α-d-glucosyl fluoride) lacking an axial 1-OH group. Similarly, the enzyme was shown to use α-maltose as a substrate but not β-maltose or close analogs (e.g., α-maltosyl fluoride) lacking an axial 1-OH group. These results indicate that interaction of the axial 1-OH group of the disaccharide donor or sugar acceptor with a particular protein group near the reaction center is required for effective catalysis. This interaction appears to be the means that leads maltose phosphorylase to promote a narrowly defined set of glucosyl transfer reactions with little hydrolysis, in contrast to other glycosylases that catalyze both hydrolytic and nonhydrolytic reactions.

AB - Maltose phosphorylase, long considered strictly specific for β-d-glucopyranosyl phosphate (β-d-glucose 1-P), was found to catalyze the reaction β-d-glucosyl fluoride + α-d-glucose → α-maltose + HF, at a rapid rate, V = 11.2 ± 1.2 μmol/(min·mg), and K = 13.1 ± 4.4 mM with α-d-glucose saturating, at 0 °C. This reaction is analogous to the synthesis of maltose from β-d-glucose 1-P + d-glucose (the reverse of maltose phosphorolysis). In acting upon β-d-glucosyl fluoride, maltose phosphorylase was found to use α-d-glucose as a cosubstrate but not β-d-glucose or other close analogs (e.g., α-d-glucosyl fluoride) lacking an axial 1-OH group. Similarly, the enzyme was shown to use α-maltose as a substrate but not β-maltose or close analogs (e.g., α-maltosyl fluoride) lacking an axial 1-OH group. These results indicate that interaction of the axial 1-OH group of the disaccharide donor or sugar acceptor with a particular protein group near the reaction center is required for effective catalysis. This interaction appears to be the means that leads maltose phosphorylase to promote a narrowly defined set of glucosyl transfer reactions with little hydrolysis, in contrast to other glycosylases that catalyze both hydrolytic and nonhydrolytic reactions.

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