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

C. Wing; J.C. Errey; B. Mukhopadhyay; J.S. Blanchard; R.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

C. Wing, J.C. Errey, B. Mukhopadhyay, J.S. Blanchard, R.A. Field

Manchester Institute of Biotechnology

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

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	Undefined
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
Publication status	Published - 2006

Keywords

Cloning
Conformations
Enzymes
Escherichia coli
Maltose

Research Beacons, Institutes and Platforms

Manchester Institute of Biotechnology

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10.1039/b609455d

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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.",

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year = "2006",

doi = "10.1039/b609455d",

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T1 - Expression and initial characterization of WbbI, a putative d-Galf:α-d-Glc β-1,6-galactofuranosyltransferase from Escherichia coli K-12

AU - Wing, C.

AU - Errey, J.C.

AU - Mukhopadhyay, B.

AU - Blanchard, J.S.

AU - Field, R.A.

PY - 2006

Y1 - 2006

N2 - 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.

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.

KW - Cloning

KW - Conformations

KW - Enzymes

KW - Escherichia coli

KW - Maltose

UR - http://www.scopus.com/inward/record.url?eid=2-s2.0-33750180649&partnerID=MN8TOARS

U2 - 10.1039/b609455d

DO - 10.1039/b609455d

M3 - Article

SN - 1477-0520

VL - 4

SP - 3945

EP - 3950

JO - Organic and Biomolecular Chemistry

JF - Organic and Biomolecular Chemistry

IS - 21

ER -

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

Abstract

Keywords

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