The active site of the Escherichia coli glycogen synthase is similar to the active site of retaining GT-B glycosyltransferases

Alejandra Yep; Miguel A. Ballicora; Jack Preiss

doi:10.1016/j.bbrc.2004.02.136

The active site of the Escherichia coli glycogen synthase is similar to the active site of retaining GT-B glycosyltransferases

Alejandra Yep, Miguel A. Ballicora, Jack Preiss

Michigan State University

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

Original language	American English
Journal	Biochemical and Biophysical Research Communications
Volume	316
Issue number	3
DOIs	https://doi.org/10.1016/j.bbrc.2004.02.136
State	Published - Apr 1 2004
Externally published	Yes

Disciplines

Biochemistry
Biology
Molecular Biology

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title = "The active site of the Escherichia coli glycogen synthase is similar to the active site of retaining GT-B glycosyltransferases",

author = "Alejandra Yep and Ballicora, {Miguel A.} and Jack Preiss",

note = "Bacterial glycogen synthases transfer a glucosyl unit, retaining the anomeric configuration, from ADP-glucose to the non-reducing end of glycogen. We ...",

year = "2004",

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doi = "10.1016/j.bbrc.2004.02.136",

language = "American English",

volume = "316",

journal = "Biochemical and Biophysical Research Communications",

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T1 - The active site of the Escherichia coli glycogen synthase is similar to the active site of retaining GT-B glycosyltransferases

AU - Yep, Alejandra

AU - Ballicora, Miguel A.

AU - Preiss, Jack

N1 - Bacterial glycogen synthases transfer a glucosyl unit, retaining the anomeric configuration, from ADP-glucose to the non-reducing end of glycogen. We ...

PY - 2004/4/1

Y1 - 2004/4/1

UR - https://www.sciencedirect.com/science/article/pii/S0006291X04004140

U2 - 10.1016/j.bbrc.2004.02.136

DO - 10.1016/j.bbrc.2004.02.136

M3 - Article

VL - 316

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 3

ER -

The active site of the Escherichia coli glycogen synthase is similar to the active site of retaining GT-B glycosyltransferases

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