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Literature summary for 5.4.2.8 extracted from

  • Lee, Y.; Villar, M.T.; Artigues, A.; Beamer, L.J.
    Promotion of enzyme flexibility by dephosphorylation and coupling to the catalytic mechanism of a phosphohexomutase (2014), J. Biol. Chem., 289, 4674-4682.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression of N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3) Pseudomonas aeruginosa

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant detagged enzyme, hanging drop vapor diffusion and microseeding techniques, 1.3 to 1.4 M sodium/potassium tartrate and 100 mM HEPES, pH 7.5, X-ray diffraction structure determination and analysis at 1.8 A resolution, modeling Pseudomonas aeruginosa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Pseudomonas aeruginosa bifunctional enzyme with phosphoglucomutase, EC 5.4.2.2, and phosphomannomutase activities ?
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?

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa
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-
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Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein phosphorylation of conserved catalytic active site residue Ser108 has broad effects on residues in multiple domains. Dephosphorylation of the enzyme may play two critical functional roles: a direct role in the chemical step of phosphoryl transfer and secondly through propagation of structural flexibility. Dephosphorylation has minimal effects on crystal structure of the enzyme Pseudomonas aeruginosa

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3), removal of the His-tag, purification by nickel affinity chromatography and dialysis Pseudomonas aeruginosa

Reaction

Reaction Comment Organism Reaction ID
alpha-D-glucose 1-phosphate = D-glucose 6-phosphate acid-base catalysis mechanism, key role for conformational change in its multistep reaction, which requires a dramatic 180 degree reorientation of the intermediate within the active site. Modeling shows that increased enzyme flexibility facilitates the reorientation of the reaction intermediate, coupling changes in structural dynamics with the unique catalytic mechanism of this enzyme Pseudomonas aeruginosa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information bifunctional enzyme with phosphoglucomutase, EC 5.4.2.2, and phosphomannomutase activities Pseudomonas aeruginosa ?
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?

Subunits

Subunits Comment Organism
More structure analysis of the active phosphoenzyme, the inactive dephosphoenzyme, and the phosphoenzyme in complex with the substrate analog xylose 1-phosphate, overview Pseudomonas aeruginosa

Synonyms

Synonyms Comment Organism
phosphomannomutase/phosphoglucomutase
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Pseudomonas aeruginosa
PMM/PGM
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Pseudomonas aeruginosa

General Information

General Information Comment Organism
additional information analysis of conformational flexibility of different forms of phosphoglucomutase/phosphomannomutase in solution, including its active, phosphorylated state and the unphosphorylated state that occurs transiently during the catalytic cycle, by hydrogen-deuterium exchange by mass spectrometry and small angle x-ray scattering. Both ligand binding and phosphorylation of the catalytic phosphoserine affect the overall flexibility of the enzyme in solution Pseudomonas aeruginosa
physiological function the enzyme catalyzes an intramolecular phosphoryl transfer across its phosphosugar substrates, which are precursors in the synthesis of exoproducts involved in bacterial virulence Pseudomonas aeruginosa