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

Biochemistry

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

36 Scopus citations

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 (US)
Pages (from-to)	3945-3950
Number of pages	6
Journal	Organic and Biomolecular Chemistry
Volume	4
Issue number	21
DOIs	https://doi.org/10.1039/b609455d
State	Published - 2006

ASJC Scopus subject areas

Biochemistry
Physical and Theoretical Chemistry
Organic Chemistry

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

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.",

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AU - Wing, Corin

AU - Errey, James C.

AU - Mukhopadhyay, Balaram

AU - Blanchard, John S.

AU - Field, Robert A.

PY - 2006

Y1 - 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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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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