Enzymes
UniProtKB help_outline | 17,289 proteins |
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Reaction participants Show >> << Hide
- Name help_outline D-mannose 6-phosphate Identifier CHEBI:58735 (Beilstein: 4704942) help_outline Charge -2 Formula C6H11O9P InChIKeyhelp_outline NBSCHQHZLSJFNQ-QTVWNMPRSA-L SMILEShelp_outline OC1O[C@H](COP([O-])([O-])=O)[C@@H](O)[C@H](O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 7 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline D-fructose 6-phosphate Identifier CHEBI:61527 Charge -2 Formula C6H11O9P InChIKeyhelp_outline BGWGXPAPYGQALX-VRPWFDPXSA-L SMILEShelp_outline OCC1(O)O[C@H](COP([O-])([O-])=O)[C@@H](O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 5 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:12356 | RHEA:12357 | RHEA:12358 | RHEA:12359 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Phosphomannose isomerase.
SLEIN M.W.
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Studies on phosphomannose isomerase. II. Characterization as a zinc metalloenzyme.
Gracy R.W., Noltmann E.A.
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[Phosphomannose isomerase. I. Activity measurement and dependence of enzyme action on sulfhydryl groups and metals in some animal tissues].
BRUNS F.H., NOLTMANN E., WILLEMSEN A.
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Structural and functional investigations of Pcal_0606, a bifunctional phosphoglucose/phosphomannose isomerase from Pyrobaculum calidifontis.
Maqsood A., Shakir N.A., Aslam M., Rahman M., Rashid N.
We are investigating the glycolytic pathway in Pyrobaculum calidifontis whose genome sequence contains homologues of all the enzymes involved in this pathway. We have characterized most of them. An open reading frame, Pcal_0606, annotated as a putative phosphoglucose/phosphomannose isomerase has t ... >> More
We are investigating the glycolytic pathway in Pyrobaculum calidifontis whose genome sequence contains homologues of all the enzymes involved in this pathway. We have characterized most of them. An open reading frame, Pcal_0606, annotated as a putative phosphoglucose/phosphomannose isomerase has to be characterized yet. In silico analysis indicated the presence of more than one substrate binding pockets at the dimeric interface of Pcal_0606. The gene encoding Pcal_0606 was cloned and expressed in Escherichia coli. Recombinant Pcal_0606, produced in soluble form, exhibited highest enzyme activity at 90 °C and pH 8.5. Presence or absence of metal ions or EDTA did not significantly affect the enzyme activity. Under optimal conditions, Pcal_0606 displayed apparent K<sub>m</sub> values of 0.33, 0.34, and 0.29 mM against glucose 6-phosphate, mannose 6-phosphate and fructose 6-phosphate, respectively. In the same order, V<sub>max</sub> values against these substrates were 290, 235, and 240 μmol min<sup>-1</sup> mg<sup>-1</sup>, indicating that Pcal_0606 catalyzed the reversible isomerization of these substrates with nearly same catalytic efficiency. These results characterize Pcal_0606 a bifunctional phosphoglucose/phosphomannose isomerase, which displayed high thermostability with a half-life of ∼50 min at 100 °C. To the best of our knowledge, Pcal_0606 is the most active and thermostable bifunctional phosphoglucose/phosphomannose isomerase characterized to date. << Less
Int. J. Biol. Macromol. 279:135127-135127(2024) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.