Variant galactokinase kinetic data

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Resource or Project Abstract

It is proposed to assess the potential of two related recombinant human enzymes ? galactokinase and N-acetylgalactosamine kinase ? as catalysts for low environmental impact site- and stereospecific phosphorylation of sugars.

This will be achieved by:
1. Rational, structure-based mutagenesis of both enzymes to alter the substrate specificity thus providing new synthetic routes to sugar and N-acetyl sugar phosphates.
2. Determining the effects of temperature, organic solvents and covalent immobilisation to a solid substrate (such as agarose or sepharose) on the enzymes to assess their suitability for use in scaled-up industrial processes.

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Contact Information for This Resource

Dr. David Timson
Queen's University Belfast
Environmental Research Scientist
Medical Biology Centre - G87, 97 Lisburn Road, School of Biological Sciences, 97 Lisburn Road Belfast BT9 7BL, Northern Ireland
Telephone: +44 (0) 28 9097 5875
e-mail: d.timson@qub.ac.uk

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Data, Files, Information Objects Related To This Project Resource

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Attachment Name and Download Link
Att 1    GALK1.zip   (18.04 Mb)

Suggested Citation Information

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Author(s)Timson, D.
Title Of WebsiteSecure Archive For Environmental Research Data
Publication InformationVariant galactokinase kinetic data
Name of OrganisationEnvironmental Protection Agency Ireland
Electronic Address or URL http://erc.epa.ie/safer/resource?id=76dec008-1f7b-102f-a0a4-f81fb11d7d1c
Unique Identifier76dec008-1f7b-102f-a0a4-f81fb11d7d1c
Date of AccessLast Updated on SAFER: 2017-08-16

An example of this citation in proper usage:

Timson, D.   "Variant galactokinase kinetic data". Associated datasets and digitial information objects connected to this resource are available at: Secure Archive For Environmental Research Data (SAFER) managed by Environmental Protection Agency Ireland http://erc.epa.ie/safer/resource?id=76dec008-1f7b-102f-a0a4-f81fb11d7d1c (Last Accessed: 2017-08-16)

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Access Information For This Resource

SAFER-Data Display URL http://erc.epa.ie/safer/iso19115/display?isoID=213
Resource KeywordsGalactokinase, GALK1, enzyme, variant, specificity change, green chemistry
EPA/ERTDI/STRIVE Project Code2007-PhD-ET-9
EPA/ERTDI/STRIVE Project ThemeEnvironmental Technologies
Resource Availability: Any User Can Download Files From This Resource
Public-Open
Limitations on the use of this ResourceData may be used freely; however, if input is required from the data provided this should be acknowledged (usually by co-authorship) in any publications.

Users of the data must cite this resource AND:
Kristiansson H & Timson DJ (2011) Increased Promiscuity of Human Galactokinase Following Alteration of a Single Amino Acid Residue Distant from the Active Site. Chembiochem. doi: 10.1002/cbic.201100308
Number of Attached Files (Publicly and Openly Available for Download): 1
Project Start Date Monday 1st October 2007 (01-10-2007)
Earliest Recorded Date within any attached datasets or digital objects Monday 1st October 2007 (01-10-2007)
Most Recent Recorded Date within any attached datasets or digital objects Friday 31st December 2010 (31-12-2010)
Published on SAFERWednesday 24th August 2011 (24-08-2011)
Date of Last EditWednesday 24th August 2011 at 10:13:40 (24-08-2011)
Datasets or Files Updated On Wednesday 24th August 2011 at 09:39:24 (24-08-2011)

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Geographical and Spatial Information Related To This Resource

Description of Geographical Characteristics of This Project or Dataset
NONE

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Supplementary Information About This Resource

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Lineage information about this project or dataset
Sugar phosphates are difficult to make by traditional synthetic chemistry methods. Furthermore, these methods tend to be energy intensive, require organic solvents and produce environmentally harmful waste products. Enzymes which catalyse the site- and stereo-specific phosphorylation of sugars (eg galactokinase) are a potential way around this problem. However, enzymes are generally highly specific and need to be modified in order to increase the range of substrates they will act upon. Some work has already been carried out (by others) on bacterial galactokinases which shows single amino acid changes in the protein can result in radical changes in specificity.
Supplementary Information
Data is provided as Excel files and also GraphPad Prism files. Data is provided "as is" and no warranty is made.
Links To Other Related Resources
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