Expression and initial characterization of WbbI, a putative d-Galf:α-d-Glc β-1,6-galactofuranosyltransferase from Escherichia coli K-12

Corin Wing; James C. Errey; Balaram Mukhopadhyay; John S. Blanchard; Robert A. Field

doi:10.1039/b609455d

Expression and initial characterization of WbbI, a putative d-Galf:α-d-Glc β-1,6-galactofuranosyltransferase from Escherichia coli K-12

Corin Wing, James C. Errey, Balaram Mukhopadhyay, John S. Blanchard, Robert A. Field

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

38 Citations (Scopus)

Abstract

Cloning of E. coli K-12 orf8 (wbbI) and over-expression of the corresponding enzyme as a maltose-binding fusion protein provided recombinant WbbI β-1,6-galactofuranosyltransferase activity. Challenged with synthetic acceptor analogues in the presence of UDP-galactofuranose as a donor, WbbI showed a modest preference for pyranoside acceptor substrates of the α-d-gluco-configuration but it also possessed the ability to turn-over acceptor analogues.

Original language	English
Pages (from-to)	3945-3950
Number of pages	6
Journal	Organic and Biomolecular Chemistry
Volume	4
Issue number	21
Early online date	21 Sept 2006
DOIs	https://doi.org/10.1039/b609455d
Publication status	Published - 2006

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abstract = "Cloning of E. coli K-12 orf8 (wbbI) and over-expression of the corresponding enzyme as a maltose-binding fusion protein provided recombinant WbbI β-1,6-galactofuranosyltransferase activity. Challenged with synthetic acceptor analogues in the presence of UDP-galactofuranose as a donor, WbbI showed a modest preference for pyranoside acceptor substrates of the α-d-gluco-configuration but it also possessed the ability to turn-over acceptor analogues.",

author = "Corin Wing and Errey, {James C.} and Balaram Mukhopadhyay and Blanchard, {John S.} and Field, {Robert A.}",

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AU - Mukhopadhyay, Balaram

AU - Blanchard, John S.

AU - Field, Robert A.

PY - 2006

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AB - Cloning of E. coli K-12 orf8 (wbbI) and over-expression of the corresponding enzyme as a maltose-binding fusion protein provided recombinant WbbI β-1,6-galactofuranosyltransferase activity. Challenged with synthetic acceptor analogues in the presence of UDP-galactofuranose as a donor, WbbI showed a modest preference for pyranoside acceptor substrates of the α-d-gluco-configuration but it also possessed the ability to turn-over acceptor analogues.

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ER -

Expression and initial characterization of WbbI, a putative d-Galf:α-d-Glc β-1,6-galactofuranosyltransferase from Escherichia coli K-12

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