Structural basis for phosphomannose isomerase activity in phosphoglucose isomerase from Pyrobaculum aerophilum: a subtle difference between distantly related enzymes.

@article{Swan2004StructuralBF,
  title={Structural basis for phosphomannose isomerase activity in phosphoglucose isomerase from Pyrobaculum aerophilum: a subtle difference between distantly related enzymes.},
  author={Michael Kenneth Swan and Thomas Hansen and Peter Sch{\"o}nheit and Christopher Davies},
  journal={Biochemistry},
  year={2004},
  volume={43 44},
  pages={
          14088-95
        }
}
The crystal structure of a dual-specificity phosphoglucose/phosphomannose isomerase from the crenarchaeon Pyrobaculum aerophilum (PaPGI/PMI) has been determined in complex with glucose 6-phosphate at 1.16 A resolution and with fructose 6-phosphate at 1.5 A resolution. Subsequent modeling of mannose 6-phosphate (M6P) into the active site of the enzyme shows that the PMI activity of this enzyme may be due to the additional space imparted by a threonine. In PGIs from bacterial and eukaryotic… Expand
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TLDR
The almost total conservation of amino acids in the active site, including the glutamate base catalyst, shows that PaPGI/PMI uses the same catalytic mechanisms for both ring opening and isomerization for the interconversion of glucose 6-phosphate to fructose 6- phosphate. Expand
Crystal structure of rabbit phosphoglucose isomerase complexed with 5-phospho-D-arabinonate identifies the role of Glu357 in catalysis.
TLDR
The X-ray crystal structure of rabbit PGI complexed with a competitive inhibitor of isomerase activity, 5-phospho-D-arabinonate (5PAA), is determined at 1.9 A resolution and it is predicted that active site residue Glu357 is the residue that transfers a proton between C2 and C1 of the proposed cis-enediol(ate) intermediate. Expand
Bifunctional Phosphoglucose/Phosphomannose Isomerases from the Archaea Aeropyrum pernix and Thermoplasma acidophilum Constitute a Novel Enzyme Family within the Phosphoglucose Isomerase Superfamily*
TLDR
Bifunctional PGI/PMI constitutes a novel protein family within the PGI superfamily, and secondary structure predictions and the presence of several conserved amino acids potentially involved in catalysis indicate some structural and functional similarity to the P GI superfamily. Expand
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TLDR
The crystal structure of PGI in the native form from rabbit muscle has been solved at a resolution of 2.5 A by a combination of multiple isomorphous replacement and multi-crystal averaging techniques and a number of conformational changes that may be associated with catalytic function. Expand
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TLDR
The substrate mannose 6-phosphate was found to protect phosphomannose isomerase from inhibition by o-phenanthroline, ethylenediaminetetraacetate, or dithiothreitol, suggesting that the metal is located in the active center of the enzyme. Expand
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TLDR
Data show that the epimerization is enzymatically catalyzed and suggest the involvement of the same active site for all three activities, and the rates of C2-epimerization of G6P and M6P by PGI are shown to be proportional to enzyme concentration and inhibited by 5-phosphoarabinoate, a competitive inhibitor of the previously demonstrated isomerase and anomerase activities of PGI. Expand
Crystallization and preliminary X-ray diffraction analysis of phosphoglucose/phosphomannose isomerase from Pyrobaculum aerophilum.
TLDR
PaPGI/PMI shows virtually no sequence similarity to its counterparts from bacterial and eukaryotic sources and belongs to a unique group within the PGI superfamily, but can also catalyse the isomerization of mannose 6-phosphate. Expand
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TLDR
To prove its coding function, ORF PAE1610 was overexpressed in Escherichia coli, and the recombinant enzyme was characterized, characterizing the enzyme as bifunctional PGI/PMI. Expand
Inhibition of type I and type II phosphomannose isomerases by the reaction intermediate analogue 5-phospho-D-arabinonohydroxamic acid supports a catalytic role for the metal cofactor.
TLDR
The evaluation of two new inhibitors of type I and type II PMIs from baker's yeast and Pseudomonas aeruginosa are evaluated, finding that 5-phospho-D-arabinonohydroxamic acid (5PAH), which is the most potent inhibitor of phosphoglucose isomerase (PGI), is by far the best inhibitor ever reported. Expand
The crystal structure of human phosphoglucose isomerase at 1.6 A resolution: implications for catalytic mechanism, cytokine activity and haemolytic anaemia.
TLDR
The human PGI structure has provided a detailed framework with which to map mutations associated with non-spherocytic haemolytic anaemia, and it is suggested that binding of the phosphate moiety of the substrate may trigger this conformational change. Expand
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