Catalytic versatility of trehalase: Synthesis of α-d-glucopyranosyl α-d-xylopyranoside from β-d-glucosyl fluoride and α-d-xylose

Takafumi Kasumi, Curtis F. Brewer, Elwyn T. Reese, Edward J. Hehre

Research output: Contribution to journalArticle

31 Citations (Scopus)

Abstract

Trehalase was previously shown (see ref. 5) to hydrolyze α-d-glucosyl fluoride, forming β-d-glucose, and to synthesize α,α-trehalose from β-d-glucosyl fluoride plus α-d-glucose. Present observations further define the enzyme's separate cosubstrate requirements in utilizing these nonglycosidic substrates. α-d-Glucopyranose and α-d-xylopyranose were found to be uniquely effective in enabling Trichoderma reesei trehalase to catalyze reactions with β-d-glucosyl fluoride. As little as 0.2mm added α-d-glucose (0.4mm α-d-xylose) substantially increased the rate of enzymically catalyzed release of fluoride from 25mm β-d-glucosyl fluoride at 0°. Digest of β-d-glucosyl fluoride plus α-d-xylose yielded the α,α-trehalose analog, α-d-glucopyranosyl α-d-xylopyranoside, as a transient (i.e., subsequently hydrolyzed) transfer-product. The need for an aldopyranose acceptor having an axial 1-OH group when β-d-glucosyl fluoride is the donor, and for water when α-d-glucosyl fluoride is the substrate, indicates that the catalytic groups of trehalose have the flexibility to catalyze different stereochemical reactions.

Original languageEnglish (US)
Pages (from-to)39-42
Number of pages4
JournalCarbohydrate Research
Volume146
Issue number1
DOIs
StatePublished - Jan 15 1986

Fingerprint

Trehalase
Xylose
Trehalose
Glucose
Trichoderma
Substrates
glucosyl fluoride
Fluorides
Water
Enzymes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Organic Chemistry

Cite this

Catalytic versatility of trehalase : Synthesis of α-d-glucopyranosyl α-d-xylopyranoside from β-d-glucosyl fluoride and α-d-xylose. / Kasumi, Takafumi; Brewer, Curtis F.; Reese, Elwyn T.; Hehre, Edward J.

In: Carbohydrate Research, Vol. 146, No. 1, 15.01.1986, p. 39-42.

Research output: Contribution to journalArticle

@article{de8f80b3af9441e691e1ce51a93d3920,
title = "Catalytic versatility of trehalase: Synthesis of α-d-glucopyranosyl α-d-xylopyranoside from β-d-glucosyl fluoride and α-d-xylose",
abstract = "Trehalase was previously shown (see ref. 5) to hydrolyze α-d-glucosyl fluoride, forming β-d-glucose, and to synthesize α,α-trehalose from β-d-glucosyl fluoride plus α-d-glucose. Present observations further define the enzyme's separate cosubstrate requirements in utilizing these nonglycosidic substrates. α-d-Glucopyranose and α-d-xylopyranose were found to be uniquely effective in enabling Trichoderma reesei trehalase to catalyze reactions with β-d-glucosyl fluoride. As little as 0.2mm added α-d-glucose (0.4mm α-d-xylose) substantially increased the rate of enzymically catalyzed release of fluoride from 25mm β-d-glucosyl fluoride at 0°. Digest of β-d-glucosyl fluoride plus α-d-xylose yielded the α,α-trehalose analog, α-d-glucopyranosyl α-d-xylopyranoside, as a transient (i.e., subsequently hydrolyzed) transfer-product. The need for an aldopyranose acceptor having an axial 1-OH group when β-d-glucosyl fluoride is the donor, and for water when α-d-glucosyl fluoride is the substrate, indicates that the catalytic groups of trehalose have the flexibility to catalyze different stereochemical reactions.",
author = "Takafumi Kasumi and Brewer, {Curtis F.} and Reese, {Elwyn T.} and Hehre, {Edward J.}",
year = "1986",
month = "1",
day = "15",
doi = "10.1016/0008-6215(86)85022-4",
language = "English (US)",
volume = "146",
pages = "39--42",
journal = "Carbohydrate Research",
issn = "0008-6215",
publisher = "Elsevier BV",
number = "1",

}

TY - JOUR

T1 - Catalytic versatility of trehalase

T2 - Synthesis of α-d-glucopyranosyl α-d-xylopyranoside from β-d-glucosyl fluoride and α-d-xylose

AU - Kasumi, Takafumi

AU - Brewer, Curtis F.

AU - Reese, Elwyn T.

AU - Hehre, Edward J.

PY - 1986/1/15

Y1 - 1986/1/15

N2 - Trehalase was previously shown (see ref. 5) to hydrolyze α-d-glucosyl fluoride, forming β-d-glucose, and to synthesize α,α-trehalose from β-d-glucosyl fluoride plus α-d-glucose. Present observations further define the enzyme's separate cosubstrate requirements in utilizing these nonglycosidic substrates. α-d-Glucopyranose and α-d-xylopyranose were found to be uniquely effective in enabling Trichoderma reesei trehalase to catalyze reactions with β-d-glucosyl fluoride. As little as 0.2mm added α-d-glucose (0.4mm α-d-xylose) substantially increased the rate of enzymically catalyzed release of fluoride from 25mm β-d-glucosyl fluoride at 0°. Digest of β-d-glucosyl fluoride plus α-d-xylose yielded the α,α-trehalose analog, α-d-glucopyranosyl α-d-xylopyranoside, as a transient (i.e., subsequently hydrolyzed) transfer-product. The need for an aldopyranose acceptor having an axial 1-OH group when β-d-glucosyl fluoride is the donor, and for water when α-d-glucosyl fluoride is the substrate, indicates that the catalytic groups of trehalose have the flexibility to catalyze different stereochemical reactions.

AB - Trehalase was previously shown (see ref. 5) to hydrolyze α-d-glucosyl fluoride, forming β-d-glucose, and to synthesize α,α-trehalose from β-d-glucosyl fluoride plus α-d-glucose. Present observations further define the enzyme's separate cosubstrate requirements in utilizing these nonglycosidic substrates. α-d-Glucopyranose and α-d-xylopyranose were found to be uniquely effective in enabling Trichoderma reesei trehalase to catalyze reactions with β-d-glucosyl fluoride. As little as 0.2mm added α-d-glucose (0.4mm α-d-xylose) substantially increased the rate of enzymically catalyzed release of fluoride from 25mm β-d-glucosyl fluoride at 0°. Digest of β-d-glucosyl fluoride plus α-d-xylose yielded the α,α-trehalose analog, α-d-glucopyranosyl α-d-xylopyranoside, as a transient (i.e., subsequently hydrolyzed) transfer-product. The need for an aldopyranose acceptor having an axial 1-OH group when β-d-glucosyl fluoride is the donor, and for water when α-d-glucosyl fluoride is the substrate, indicates that the catalytic groups of trehalose have the flexibility to catalyze different stereochemical reactions.

UR - http://www.scopus.com/inward/record.url?scp=0023048847&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023048847&partnerID=8YFLogxK

U2 - 10.1016/0008-6215(86)85022-4

DO - 10.1016/0008-6215(86)85022-4

M3 - Article

C2 - 3955571

AN - SCOPUS:0023048847

VL - 146

SP - 39

EP - 42

JO - Carbohydrate Research

JF - Carbohydrate Research

SN - 0008-6215

IS - 1

ER -