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Literature summary extracted from

  • Foret, J.; de Courcy, B.; Gresh, N.; Piquemal, J.P.; Salmon, L.
    Synthesis and evaluation of non-hydrolyzable D-mannose 6-phosphate surrogates reveal 6-deoxy-6-dicarboxymethyl-D-mannose as a new strong inhibitor of phosphomannose isomerases (2009), Bioorg. Med. Chem., 17, 7100-7107.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.3.1.8 5-deoxy-5-(dihydrogenophosphonomethyl)-D-arabinono-1,4-lactone
-
 Escherichia coli
5.3.1.8 5-deoxy-5-(dihydrogenophosphonomethyl)-D-arabinono-1,4-lactone
-
 Saccharomyces cerevisiae
5.3.1.8 5-deoxy-5-phosphonomethyl-D-arabinonate
-
 Escherichia coli
5.3.1.8 5-deoxy-5-phosphonomethyl-D-arabinonate
-
 Saccharomyces cerevisiae
5.3.1.8 5-deoxy-5-phosphonomethyl-D-arabinonohydrazide
-
 Escherichia coli
5.3.1.8 5-deoxy-5-phosphonomethyl-D-arabinonohydrazide
-
 Saccharomyces cerevisiae
5.3.1.8 5-deoxy-5-phosphonomethyl-D-arabinonohydroxamic acid
-
 Escherichia coli
5.3.1.8 5-deoxy-5-phosphonomethyl-D-arabinonohydroxamic acid
-
 Saccharomyces cerevisiae
5.3.1.8 6-deoxy-6-carboxymethyl-D-mannose
-
 Escherichia coli
5.3.1.8 6-deoxy-6-carboxymethyl-D-mannose
-
 Saccharomyces cerevisiae
5.3.1.8 6-deoxy-6-dicarboxymethyl-D-mannose
-
 Escherichia coli
5.3.1.8 6-deoxy-6-dicarboxymethyl-D-mannose
-
 Saccharomyces cerevisiae
5.3.1.8 6-deoxy-6-dimethylmalonate-D-mannopyranose
-
 Escherichia coli
5.3.1.8 6-deoxy-6-dimethylmalonate-D-mannopyranose
-
 Saccharomyces cerevisiae
5.3.1.8 6-deoxy-6-phosphonomethyl-D-mannose
-
 Escherichia coli
5.3.1.8 6-deoxy-6-phosphonomethyl-D-mannose
-
 Saccharomyces cerevisiae
5.3.1.8 benzyl 2,3,4-tri-O-benzyl-6-deoxy-6-dimethylmalonate-alpha-D-mannopyranoside
-
 Escherichia coli
5.3.1.8 benzyl 2,3,4-tri-O-benzyl-6-deoxy-6-dimethylmalonate-alpha-D-mannopyranoside
-
 Saccharomyces cerevisiae
5.3.1.8 benzyl 2,3,4-tri-O-benzyl-6-O-trifluoromethanesulfonyl-alpha-D-mannose
-
 Escherichia coli
5.3.1.8 benzyl 2,3,4-tri-O-benzyl-6-O-trifluoromethanesulfonyl-alpha-D-mannose
-
 Saccharomyces cerevisiae
5.3.1.8 benzyl 2,3,4-tri-O-benzyl-alpha-D-mannose
-
 Escherichia coli
5.3.1.8 benzyl 2,3,4-tri-O-benzyl-alpha-D-mannose
-
 Saccharomyces cerevisiae
5.3.1.8 additional information synthesis of a non-hydrolyzable D-mannose 6-phosphate surrogates as strong competitive enzyme inhibitors. Effective binding to the catalytic site occurs with retention of the Zn(II)-bound water molecule. Molecular mechanics study of enzyme substrate and inhibitors, overview Escherichia coli
5.3.1.8 additional information synthesis of a non-hydrolyzable D-mannose 6-phosphate surrogates as strong competitive inhibitors of the enzyme. Effective binding to the catalytic site occurs with retention of the Zn(II)-bound water molecule. Molecular mechanics study of enzyme substrate and inhibitors, overview Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.3.1.8 D-Mannose 6-phosphate Escherichia coli
-
 D-Fructose 6-phosphate
-
 r
5.3.1.8 D-Mannose 6-phosphate Saccharomyces cerevisiae
-
 D-Fructose 6-phosphate
-
 r

Organism

EC Number Organism UniProt Comment Textmining
5.3.1.8 Escherichia coli
-
-
-
5.3.1.8 Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.3.1.8 D-Mannose 6-phosphate
-
 Escherichia coli D-Fructose 6-phosphate
-
 r
5.3.1.8 D-Mannose 6-phosphate
-
 Saccharomyces cerevisiae D-Fructose 6-phosphate
-
 r
5.3.1.8 additional information Molecular mechanics study of enzyme substrate and inhibitors, overview Escherichia coli ?
-
 ?
5.3.1.8 additional information Molecular mechanics study of enzyme substrate and inhibitors, overview Saccharomyces cerevisiae ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
5.3.1.8 Phosphomannose isomerase
-
 Escherichia coli
5.3.1.8 Phosphomannose isomerase
-
 Saccharomyces cerevisiae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
5.3.1.8 25
-
 assay at Escherichia coli
5.3.1.8 25
-
 assay at Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.3.1.8 7.1
-
 assay at Escherichia coli
5.3.1.8 7.1
-
 assay at Saccharomyces cerevisiae

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
5.3.1.8 0.0105
-
 6-deoxy-6-dicarboxymethyl-D-mannose pH 7.1, 25°C, recombinant enzyme Saccharomyces cerevisiae
5.3.1.8 0.115
-
 6-deoxy-6-dicarboxymethyl-D-mannose pH 7.1, 25°C, recombinant enzyme Escherichia coli

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
5.3.1.8 0.0181
-
 pH 7.1, 25°C, recombinant enzyme Saccharomyces cerevisiae 6-deoxy-6-dicarboxymethyl-D-mannose
5.3.1.8 0.199
-
 pH 7.1, 25°C, recombinant enzyme Escherichia coli 6-deoxy-6-dicarboxymethyl-D-mannose
5.3.1.8 0.37
-
 pH 7.1, 25°C, recombinant enzyme Escherichia coli 5-deoxy-5-phosphonomethyl-D-arabinonohydroxamic acid
5.3.1.8 0.9
-
 pH 7.1, 25°C, recombinant enzyme Saccharomyces cerevisiae 6-deoxy-6-carboxymethyl-D-mannose
5.3.1.8 1.61
-
 pH 7.1, 25°C, recombinant enzyme Saccharomyces cerevisiae 6-deoxy-6-phosphonomethyl-D-mannose
5.3.1.8 2.2
-
 pH 7.1, 25°C, recombinant enzyme Saccharomyces cerevisiae 5-deoxy-5-phosphonomethyl-D-arabinonohydroxamic acid
5.3.1.8 3
-
 above, pH 7.1, 25°C, recombinant enzyme Escherichia coli 5-deoxy-5-phosphonomethyl-D-arabinonate
5.3.1.8 3
-
 above, pH 7.1, 25°C, recombinant enzyme Escherichia coli 5-deoxy-5-phosphonomethyl-D-arabinonohydrazide
5.3.1.8 4.6
-
 pH 7.1, 25°C, recombinant enzyme Escherichia coli 6-deoxy-6-carboxymethyl-D-mannose
5.3.1.8 4.7
-
 pH 7.1, 25°C, recombinant enzyme Escherichia coli 6-deoxy-6-phosphonomethyl-D-mannose