D-ribose-5-phosphate isomerase from spinach: heterologous overexpression, purification, characterization, and site-directed mutagenesis of the recombinant enzyme.

@article{Jung2000Dribose5phosphateIF,
  title={D-ribose-5-phosphate isomerase from spinach: heterologous overexpression, purification, characterization, and site-directed mutagenesis of the recombinant enzyme.},
  author={Christine Jung and Fred C. Hartman and T Y Lu and Frank W. Larimer},
  journal={Archives of biochemistry and biophysics},
  year={2000},
  volume={373 2},
  pages={
          409-17
        }
}
A cDNA encoding spinach chloroplastic ribose-5-phosphate isomerase (RPI) was cloned and overexpressed in Escherichia coli, and a purification scheme for the recombinant enzyme was developed. The purified recombinant RPI is a homodimer of 25-kDa subunits and shows kinetic properties similar to those of the homodimeric enzyme isolated from spinach leaves (A. C. Rutner, 1970, Biochemistry 9, 178-184). Phosphate, used as a buffer in previous studies, is a competitive inhibitor of RPI with a K(i) of… 
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Crystal structure of D‐ribose‐5‐phosphate isomerase (RpiA) from Escherichia coli
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A hyperthermostable D-ribose-5-phosphate isomerase from Pyrococcus horikoshii characterization and three-dimensional structure.
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A gene homologous to D-ribose-5-phosphate isomerase (PRI) was found in the genome of Pyrococcus horikoshii, and the resulting enzyme showed activity at high temperatures with an optimum over 90 degrees C.
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The present paper contributes to the know-ledge of the mechanism of the Rpi reaction; in addition, the absence of RpiBs in the genomes of higher animals makes this enzyme a possible target for chemotherapy of Chagas disease.
Competitive Inhibitors of Mycobacterium tuberculosis Ribose-5-phosphate Isomerase B Reveal New Information about the Reaction Mechanism*
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Studies of RpiB from Mycobacterium tuberculosis together with small molecules designed to resemble the enediolate intermediate are presented, to outline the reaction mechanism for RpiBs.
Mycobacterium tuberculosis ribose-5-phosphate isomerase has a known fold, but a novel active site.
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It is demonstrated that the RpiB from Mycobacterium tuberculosis has catalytic properties very similar to those previously reported for the Escherichia coli RPIB enzyme, and the structure of the mycobacterial enzyme is reported, solved by molecular replacement and refined to 1.88A resolution.
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Kinetic studies indicate that RpiB is nearly as efficient as RpiA, despite its completely different catalytic machinery, and the sequence and structural results suggest that the two homologous components of LacAB will compose a bi-functional enzyme; the second activity is unknown.
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A mutation in an Arabidopsis ribose 5-phosphate isomerase reduces cellulose synthesis and is rescued by exogenous uridine.
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The Arabidopsis radial swelling mutant rsw10 showed ballooning of root trichoblasts, a lower than wild-type level of cellulose and altered levels of some monosaccharides in non-cellulosic polysaccharides, while fusion of the RSW10 promoter region to the GUS reporter gene established that the gene is expressed in many aerial tissues as well as the roots.
Enhanced isomerization of rare sugars by ribose-5-phosphate isomerase A from Ochrobactrum sp. CSL1.
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This study highlights the potential of OsRpiA as a biocatalyst for rare sugar preparation, and provides distinct evidences for its catalytic mechanism.
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