Stereoselective enzymatic galactosylation of C-glucosides

Luigi Panza; Pietro L. Chiappini; Giovanni Russo; Daniela Monti; Sergio Riva

doi:10.1039/a701747b

Stereoselective enzymatic galactosylation of C-glucosides

Luigi Panza
, Pietro L. Chiappini
, Giovanni Russo
, Daniela Monti
, Sergio Riva

Research output: Contribution to journal › Article › peer-review

Abstract

The enzyme β-1,4-galactosyl transferase from bovine colostrum (GalT) is able stereoselectively to galactosylate C-glucosides (i.e. 1 and 4), precursors of stable glycoconjugate analogues, and a systematic investigation of the structural modifications at C-1 and/or C-5 of the glycosides that can be accepted by this enzyme has been undertaken, adding information to the currently accepted model of substrate binding into the GalT active site.

Original language	English
Pages (from-to)	1255-1256
Number of pages	2
Journal	Journal of the Chemical Society, Perkin Transactions 1
Issue number	9
DOIs	https://doi.org/10.1039/a701747b
Publication status	Published - 7 May 1997
Externally published	Yes

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title = "Stereoselective enzymatic galactosylation of C-glucosides",

abstract = "The enzyme β-1,4-galactosyl transferase from bovine colostrum (GalT) is able stereoselectively to galactosylate C-glucosides (i.e. 1 and 4), precursors of stable glycoconjugate analogues, and a systematic investigation of the structural modifications at C-1 and/or C-5 of the glycosides that can be accepted by this enzyme has been undertaken, adding information to the currently accepted model of substrate binding into the GalT active site.",

author = "Luigi Panza and Chiappini, \{Pietro L.\} and Giovanni Russo and Daniela Monti and Sergio Riva",

year = "1997",

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T1 - Stereoselective enzymatic galactosylation of C-glucosides

AU - Panza, Luigi

AU - Chiappini, Pietro L.

AU - Russo, Giovanni

AU - Monti, Daniela

AU - Riva, Sergio

PY - 1997/5/7

Y1 - 1997/5/7

N2 - The enzyme β-1,4-galactosyl transferase from bovine colostrum (GalT) is able stereoselectively to galactosylate C-glucosides (i.e. 1 and 4), precursors of stable glycoconjugate analogues, and a systematic investigation of the structural modifications at C-1 and/or C-5 of the glycosides that can be accepted by this enzyme has been undertaken, adding information to the currently accepted model of substrate binding into the GalT active site.

AB - The enzyme β-1,4-galactosyl transferase from bovine colostrum (GalT) is able stereoselectively to galactosylate C-glucosides (i.e. 1 and 4), precursors of stable glycoconjugate analogues, and a systematic investigation of the structural modifications at C-1 and/or C-5 of the glycosides that can be accepted by this enzyme has been undertaken, adding information to the currently accepted model of substrate binding into the GalT active site.

UR - https://www.scopus.com/pages/publications/33748637181

U2 - 10.1039/a701747b

DO - 10.1039/a701747b

M3 - Article

SN - 0300-922X

SP - 1255

EP - 1256

JO - Journal of the Chemical Society, Perkin Transactions 1

JF - Journal of the Chemical Society, Perkin Transactions 1

IS - 9

ER -

Stereoselective enzymatic galactosylation of C-glucosides

Abstract

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