1h5r
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(New page: 200px<br /> <applet load="1h5r" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h5r, resolution 1.9Å" /> '''THYMIDYLYLTRANSFERAS...)
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Revision as of 16:03, 29 October 2007
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THYMIDYLYLTRANSFERASE COMPLEXED WITH THIMIDINE AND GLUCOSE-1-PHOSPATE
Overview
Glucose-1-phosphate thymidylyltransferase is the first enzyme in the, biosynthesis of dTDP-l-rhamnose, the precursor of l-rhamnose, an essential, component of surface antigens, such as the O-lipopolysaccharide, mediating, virulence and adhesion to host tissues in many microorganisms. The enzyme, catalyses the formation of dTDP-glucose, from dTTP and glucose, 1-phosphate, as well as its pyrophosphorolysis. To shed more light on the, catalytic properties of glucose-1-phosphate thymidylyltransferase from, Escherichia coli, specifically distinguishing between ping pong and, sequential ordered bi bi reaction mechanisms, the enzyme kinetic, properties have been analysed in the presence of different substrates and, inhibitors. Moreover, three different complexes of glucose-1-phosphate, ... [(full description)]
About this Structure
1H5R is a [Protein complex] structure of sequences from [[1]] with G1P, SO4 and THM as [ligands]. Active as [[2]], with EC number [2.7.7.24]. Full crystallographic information is available from [OCA].
Reference
Kinetic and crystallographic analyses support a sequential-ordered bi bi catalytic mechanism for Escherichia coli glucose-1-phosphate thymidylyltransferase., Zuccotti S, Zanardi D, Rosano C, Sturla L, Tonetti M, Bolognesi M, J Mol Biol. 2001 Nov 2;313(4):831-43. PMID:11697907
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