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13 items found (0 items not approved), displaying 11 to 13.[First/Prev] 1, 2 [Next/Last]

Instruments / Technical Area	Publication Details	Published
I04-Macromolecular Crystallography	Degradation of phytate by the 6-phytase from Hafnia alvei: a combined structural and solution study Antonio Ariza , Olga V. Moroz , Elena V. Blagova , Johan P. Turkenburg , Jitka Waterman , Shirley M. Roberts , Jesper Vind , Carsten Sjøholm , Søren F. Lassen , Leonardo De Maria , Vibe Glitsoe , Lars K. Skov , Keith S. Wilson Plos One 8 (5), 11766-11774 DOI: 10.1371/journal.pone.0065062 PMID: 23741456 Open Access Show Abstract ▼ Abstract: Phytases hydrolyse phytate (myo-inositol hexakisphosphate), the principal form of phosphate stored in plant seeds to produce phosphate and lower phosphorylated myo-inositols. They are used extensively in the feed industry, and have been characterised biochemically and structurally with a number of structures in the PDB. They are divided into four distinct families: histidine acid phosphatases (HAP), β-propeller phytases, cysteine phosphatases and purple acid phosphatases and also split into three enzyme classes, the 3-, 5- and 6-phytases, depending on the position of the first phosphate in the inositol ring to be removed. We report identification, cloning, purification and 3D structures of 6-phytases from two bacteria, Hafnia alvei and Yersinia kristensenii, together with their pH optima, thermal stability, and degradation profiles for phytate. An important result is the structure of the H. alvei enzyme in complex with the substrate analogue myo-inositol hexakissulphate. In contrast to the only previous structure of a ligand-bound 6-phytase, where the 3-phosphate was unexpectedly in the catalytic site, in the H. alvei complex the expected scissile 6-phosphate (sulphate in the inhibitor) is placed in the catalytic site.	May 2013
I04-1-Macromolecular Crystallography (fixed wavelength) I04-Macromolecular Crystallography	An enzyme-trap approach allows isolation of intermediates in cobalamin biosynthesis Evelyne Deery , Susanne Schroeder , Andrew D. Lawrence , Samantha L. Taylor , Jitka Waterman , Keith S. Wilson , David Brown , Michael A. Geeves , Mark J. Howard , Richard Pickersgill , Martin J. Warren , Arefeh Seyedarabi Nature Chemical Biology 8 (11), 933-940 DOI: 10.1038/nchembio.1086 PMID: 23042036 Open Access Show Abstract ▼ Abstract: The biosynthesis of many vitamins and coenzymes has often proven difficult to elucidate owing to a combination of low abundance and kinetic lability of the pathway intermediates. Through a serial reconstruction of the cobalamin (vitamin B12) pathway in Escherichia coli and by His tagging the terminal enzyme in the reaction sequence, we have observed that many unstable intermediates can be isolated as tightly bound enzyme-product complexes. Together, these approaches have been used to extract intermediates between precorrin-4 and hydrogenobyrinic acid in their free acid form and permitted the delineation of the overall reaction catalyzed by CobL, including the formal elucidation of precorrin-7 as a metabolite. Furthermore, a substrate-carrier protein, CobE, that can also be used to stabilize some of the transient metabolic intermediates and enhance their onward transformation, has been identified. The tight association of pathway intermediates with enzymes provides evidence for a form of metabolite channeling.	Oct 2012
	Diamond: open for business Elizabeth Shotton , Alexandre Dias , Anna Kroner , Claire Pizzey , Jitka Waterman Synchrotron Radiation News 24 (6), 30 - 33 Synchrotron Radiation News DOI: 10.1080/08940886.2011.634316 Show Abstract ▼ Abstract: The importance of industrial use of national and international infrastructure projects such as Diamond Light Source is well understood, with the facilities ever mindful of the impact agenda of their funding agencies and governments. Diamond opened its doors for academic users in January 2007, with industrial users following a year later. Since that time, more than 40 companies have used Diamond's beamlines and support laboratories through the proprietary access mode, i.e. paying for their usage. In addition, many more have collaborated with university partners and used facilities through the peer review route.	Nov 2011

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