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

Risultato della ricerca: Contributo su rivista › Articolo in rivista › 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.

Lingua originale	Inglese
pagine (da-a)	1255-1256
Numero di pagine	2
Rivista	Journal of the Chemical Society, Perkin Transactions 1
Numero di pubblicazione	9
DOI	https://doi.org/10.1039/a701747b
Stato di pubblicazione	Pubblicato - 7 mag 1997
Pubblicato esternamente	Sì

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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",

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AU - Panza, Luigi

AU - Chiappini, Pietro L.

AU - Russo, Giovanni

AU - Monti, Daniela

AU - Riva, Sergio

PY - 1997/5/7

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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.

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ER -

Stereoselective enzymatic galactosylation of C-glucosides

Abstract

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