Structure of Bacterial Glutathione-S-Transferase Maleyl Pyruvate Isomerase and Implications for Mechanism of Isomerisation

Maleyl pyruvate isomerase (MPI) is a bacterial glutathione S-transferase (GST) from the pathway for degradation of naphthalene via gentisate that enables the bacterium Ralstonia to use polyaromatic hydrocarbons as a sole carbon source. Genome sequencing projects have revealed the presence of large n...

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Veröffentlicht in:	Journal of molecular biology 2008-12, Vol.384 (1), p.165-177
Hauptverfasser:	Marsh, May, Shoemark, Deborah K., Jacob, Alyssa, Robinson, Charles, Cahill, Brent, Zhou, Ning-Yi, Williams, Peter A., Hadfield, Andrea T.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Arabidopsis - enzymology Bacteria Binding Sites biodegradation cis-trans-Isomerases - chemistry cis-trans-Isomerases - metabolism Crystallography, X-Ray Dicarboxylic Acids - metabolism Dimerization enzyme–substrate complex X-ray structure Glutathione - metabolism Glutathione Transferase - chemistry Glutathione Transferase - metabolism glutathione transferase Zeta Humans isomerisation Isomerism maleylacetoacetate isomerase Models, Molecular Molecular Sequence Data Naphthalenes - metabolism Pimelic Acids - metabolism Protein Folding Protein Structure, Secondary Ralstonia Ralstonia - enzymology Sequence Alignment
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