Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 327018
Title Cloning, purification, crystallization and preliminary crystallographic analysis of galactokinase from Pyrococcus furiosus
Author(s) Geus, D. de; Hartley, A.P.; Sedelnikova, S.E.; Glynn, S.E.; Baker, P.J.; Verhees, C.H.; Oost, J. van der; Rice, D.W.
Source Acta Crystallographica Section D-Biological Crystallography 59 (2003)10. - ISSN 0907-4449 - p. 1819 - 1821.
DOI https://doi.org/10.1107/S090744490301607X
Department(s) Microbiology
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2003
Keyword(s) ghmp kinase superfamily - mevalonate kinase - sugar kinases - mechanism - galactose - complex - enzymes
Abstract Galactokinase catalyses the conversion of galactose to galactose-1-phosphate as the first step in the Leloir pathway, a metabolic route that eventually enables the degradation of galactose via the glycolytic pathway. Galactokinases have been isolated from a wide range of prokaryotic and eukaryotic organisms and the enzyme has been identified as a member of the GHMP kinase (galactokinase, homoserine kinase, mevalonate kinase and phosphomevalonate kinase) superfamily. Pyrococcus furiosus galactokinase was cloned, expressed in Escherichia coli, purified and crystallized using the hanging-drop method of vapour diffusion with ammonium sulfate as the precipitant. The crystals belong to the space group C222(1), with more than eight subunits in the asymmetric unit and with approximate unit-cell parameters a = 211.7, b = 355.4, c = 165.5 Angstrom, alpha = beta = gamma = 90degrees. The crystals diffract X-rays to 2.9 Angstrom resolution on a synchrotron-radiation source. Determination of the structure will provide insights into the molecular basis of substrate recognition and catalysis of this enzyme, for which no structures are currently available.
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