Gene Ontology</a> 'Molecular Function' concepts classify proteins according to their functions, e.g. the activity to catalyze a given reaction.<br />Source: GO consortium biocuration.</p> </div> "> help_outline KEGG help_outline MetaCyc help_outline EcoCyc help_outline

Publications

e synthase, a key enzyme involved in the cyclization of 1-(o-carboxyphenylamino)-1-deoxyribulose 5-phosphate, from Pyrococcus furiosus was cloned and expressed in Escherichia coli. The gene product was produced in the soluble and actid <strong>M</strong>olecular-<strong>I</strong>nput <strong>L</strong>ine-<strong>E</strong>ntry <strong>S</strong>ystem (SMILES) is a line notation describing the structure of chemical species using short ASCII strings. <a href="/help/smiles">More</a>...<br />Source: ChEBI biocuration.</p> </div> ">help_outline O=C=O 2D coordinates Mol file for the small molecule Search links Involved in 966 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
  • Name help_outline (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate Identifier CHEBI:58866 Charge -2 Formula C11H12NO6P InChIKeyhelp_outline NQEQTYPJSIEPHW-MNOVXSKESA-L SMILEShelp_outline O[C@H](COP([O-])([O-])=O)[C@@H](O)C(=O)CNc1ccccc1C([O-])=O 2D coordinates Mol ve form. The recombinant protein, purified to apparent homogeneity, displayed highest activity at 100 °C and pH of 5.5. The recombinant enzyme followed Michaelis-Menten kinetics exhibiting apparent V<sub>max</sub> and K<sub>m</sub> values of 20 ± 0.5 μmol min<sup>-1</sup> mg<sup>-1</sup> and 140 ± 10 µM, respectively. The activation energy, determined from the linear Arrhenius plot, was 17 ± 0.5 kJ mol<sup>-1</sup>. A unique property of PfInGPS is its stability against denaturants and temperature. There was no significant change in activity even in the presence of 8 M urea or 5 M guanidine hydrochloride. Furthermore, recombinant PfInGPS was highly thermostable with a half-life of 200 min at 100 °C. To the best of our knowledge, this is the most stable indole-3-glycerol phosphate synthase characterized to date. << Less

    Extremophiles 23:69-77(2019) [PubMed] [EuropePMC]

    • e synthase, a key enzyme involved in the cyclization of 1-(o-carboxyphenylamino)-1-deoxyribulose 5-phosphate, from Pyrococcus furiosus was cloned and expressed in Escherichia coli. The gene product was produced in the soluble and actid <strong>M</strong>olecular-<strong>I</strong>nput <strong>L</strong>ine-<strong>E</strong>ntry <strong>S</strong>ystem (SMILES) is a line notation describing the structure of chemical species using short ASCII strings. <a href="/help/smiles">More</a>...<br />Source: ChEBI biocuration.</p> </div> ">help_outline O=C=O 2D coordinates Mol file for the small molecule Search links Involved in 966 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
  • Name help_outline (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate Identifier CHEBI:58866 Charge -2 Formula C11H12NO6P InChIKeyhelp_outline NQEQTYPJSIEPHW-MNOVXSKESA-L SMILES << Less

    Extremophiles 23:69-77(2019) [PubMed] [EuropePMC]

    • ve form. The recombinant protein, purified to apparent homogeneity, displayed highest activity at 100 °C and pH of 5.5. The recombinant enzyme followed Michaelis-Menten kinetics exhibiting apparent V<sub>max</sub> and K<sub>m</sub> values of 20 ± 0.5 μmol min<sup>-1</sup> mg<sup>-1</sup> and 140 ± 10 µM, respectively. The activation energy, determined from the linear Arrhenius plot, was 17 ± 0.5 kJ mol<sup>-1</sup>. A unique property of PfInGPS is its stability against denaturants and temperature. There was no significant change in activity even in the presence of 8 M urea or 5 M guanidine hydrochloride. Furthermore, recombinant PfInGPS was highly thermostable with a half-life of 200 min at 100 °C. To the best of our knowledge, this is the most stable indole-3-glycerol phosphate synthase characterized to date. << Less

    Extremophiles 23:69-77(2019) [PubMed] [EuropePMC]

    e synthase, a key enzyme involved in the cyclization of 1-(o-carboxyphenylamino)-1-deoxyribulose 5-phosphate, from Pyrococcus furiosus was cloned and expressed in Escherichia coli. The gene product was produced in the soluble and actid <strong>M</strong>olecular-<strong>I</strong>nput <strong>L</strong>ine-<strong>E</strong>ntry <strong>S</strong>ystem (SMILES) is a line notation describing the structure of chemical species using short ASCII strings. <a href="/help/smiles">More</a>...<br />Source: ChEBI biocuration.</p> </div> ">help_outline O=C=O 2D coordinates Mol file for the small molecule Search links Involved in 966 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
  • Name help_outline KEGG help_outline MetaCyc help_outline e synthase, a key enzyme involved in the cyclization of 1-(o-carboxyphenylamino)-1-deoxyribulose 5-phosphate, from Pyrococcus furiosus was cloned and expressed in Escherichia coli. The gene product was produced in the soluble and active form. The recombinant protein, purified to apparent homogeneity, displayed highest activity at 100 °C and pH of 5.5. The recombinant enzyme followed Michaelis-Menten kinetics exhibiting apparent V<sub>max</sub> and K<sub>m</sub> values of 20 ± 0.5 μmol min<sup>-1</sup> mg<sup>-1</sup> and 140 ± 10 µM, respectively. The activation energy, determined from the linear Arrhenius plot, was 17 ± 0.5 kJ mol<sup>-1</sup>. A unique property of PfInGPS is its stability against denaturants and temperature. There was no significant change in activity even in the presence of 8 M urea or 5 M guanidine hydrochloride. Furthermore, recombinant PfInGPS was highly thermostable with a half-life of 200 min at 100 °C. To the best of our knowledge, this is the most stable indole-3-glycerol phosphate synthase characterized to date. << Less

    Extremophiles 23:69-77(2019) [PubMed] [EuropePMC]