Studies on the substrate specificity of Escherichia coli galactokinase

Jie Yang; Xun Fu; Qiang Jia; Jie Shen; John B. Biggins; Jiqing Jiang; Jingjing Zhao; Joshua J. Schmidt; Peng G. Wang; Jon S. Thorson

doi:10.1021/ol034642d

Studies on the substrate specificity of Escherichia coli galactokinase

Jie Yang, Xun Fu, Qiang Jia, Jie Shen, John B. Biggins, Jiqing Jiang, Jingjing Zhao, Joshua J. Schmidt, Peng G. Wang, Jon S. Thorson

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

86 Scopus citations

Abstract

(Martix presented) In vitro glycorandomization (IVG) technology is dependent upon the ability to rapidly synthesize sugar phosphates. Compared with chemical synthesis, enzymatic (kinase) routes to sugar phosphates would be attractive for this application. This work focuses upon the development of a high-throughput colorimetric galactokinase (GalK) assay and its application toward probing the substrate specificity and kinetic parameters of Escherichia coli GalK. The demonstrated dinitrosalicylic assay should also be generally applicable to a variety of sugar-processing enzymes.

Original language	English
Pages (from-to)	2223-2226
Number of pages	4
Journal	Organic Letters
Volume	5
Issue number	13
DOIs	https://doi.org/10.1021/ol034642d
State	Published - Jun 26 2003

ASJC Scopus subject areas

Biochemistry
Physical and Theoretical Chemistry
Organic Chemistry

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10.1021/ol034642d

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title = "Studies on the substrate specificity of Escherichia coli galactokinase",

abstract = "(Martix presented) In vitro glycorandomization (IVG) technology is dependent upon the ability to rapidly synthesize sugar phosphates. Compared with chemical synthesis, enzymatic (kinase) routes to sugar phosphates would be attractive for this application. This work focuses upon the development of a high-throughput colorimetric galactokinase (GalK) assay and its application toward probing the substrate specificity and kinetic parameters of Escherichia coli GalK. The demonstrated dinitrosalicylic assay should also be generally applicable to a variety of sugar-processing enzymes.",

author = "Jie Yang and Xun Fu and Qiang Jia and Jie Shen and Biggins, {John B.} and Jiqing Jiang and Jingjing Zhao and Schmidt, {Joshua J.} and Wang, {Peng G.} and Thorson, {Jon S.}",

year = "2003",

month = jun,

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doi = "10.1021/ol034642d",

language = "English",

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TY - JOUR

T1 - Studies on the substrate specificity of Escherichia coli galactokinase

AU - Yang, Jie

AU - Fu, Xun

AU - Jia, Qiang

AU - Shen, Jie

AU - Biggins, John B.

AU - Jiang, Jiqing

AU - Zhao, Jingjing

AU - Schmidt, Joshua J.

AU - Wang, Peng G.

AU - Thorson, Jon S.

PY - 2003/6/26

Y1 - 2003/6/26

N2 - (Martix presented) In vitro glycorandomization (IVG) technology is dependent upon the ability to rapidly synthesize sugar phosphates. Compared with chemical synthesis, enzymatic (kinase) routes to sugar phosphates would be attractive for this application. This work focuses upon the development of a high-throughput colorimetric galactokinase (GalK) assay and its application toward probing the substrate specificity and kinetic parameters of Escherichia coli GalK. The demonstrated dinitrosalicylic assay should also be generally applicable to a variety of sugar-processing enzymes.

AB - (Martix presented) In vitro glycorandomization (IVG) technology is dependent upon the ability to rapidly synthesize sugar phosphates. Compared with chemical synthesis, enzymatic (kinase) routes to sugar phosphates would be attractive for this application. This work focuses upon the development of a high-throughput colorimetric galactokinase (GalK) assay and its application toward probing the substrate specificity and kinetic parameters of Escherichia coli GalK. The demonstrated dinitrosalicylic assay should also be generally applicable to a variety of sugar-processing enzymes.

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U2 - 10.1021/ol034642d

DO - 10.1021/ol034642d

M3 - Article

C2 - 12816414

AN - SCOPUS:0141518596

SN - 1523-7060

VL - 5

SP - 2223

EP - 2226

JO - Organic Letters

JF - Organic Letters

IS - 13

ER -

Studies on the substrate specificity of Escherichia coli galactokinase

Abstract

ASJC Scopus subject areas

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