Inhibitors | Comment | Organism | Structure |
---|---|---|---|
5-deoxy-5-(dihydrogenophosphonomethyl)-D-arabinono-1,4-lactone | - |
Escherichia coli | |
5-deoxy-5-(dihydrogenophosphonomethyl)-D-arabinono-1,4-lactone | - |
Saccharomyces cerevisiae | |
5-deoxy-5-phosphonomethyl-D-arabinonate | - |
Escherichia coli | |
5-deoxy-5-phosphonomethyl-D-arabinonate | - |
Saccharomyces cerevisiae | |
5-deoxy-5-phosphonomethyl-D-arabinonohydrazide | - |
Escherichia coli | |
5-deoxy-5-phosphonomethyl-D-arabinonohydrazide | - |
Saccharomyces cerevisiae | |
5-deoxy-5-phosphonomethyl-D-arabinonohydroxamic acid | - |
Escherichia coli | |
5-deoxy-5-phosphonomethyl-D-arabinonohydroxamic acid | - |
Saccharomyces cerevisiae | |
6-deoxy-6-carboxymethyl-D-mannose | - |
Escherichia coli | |
6-deoxy-6-carboxymethyl-D-mannose | - |
Saccharomyces cerevisiae | |
6-deoxy-6-dicarboxymethyl-D-mannose | - |
Escherichia coli | |
6-deoxy-6-dicarboxymethyl-D-mannose | - |
Saccharomyces cerevisiae | |
6-deoxy-6-dimethylmalonate-D-mannopyranose | - |
Escherichia coli | |
6-deoxy-6-dimethylmalonate-D-mannopyranose | - |
Saccharomyces cerevisiae | |
6-deoxy-6-phosphonomethyl-D-mannose | - |
Escherichia coli | |
6-deoxy-6-phosphonomethyl-D-mannose | - |
Saccharomyces cerevisiae | |
benzyl 2,3,4-tri-O-benzyl-6-deoxy-6-dimethylmalonate-alpha-D-mannopyranoside | - |
Escherichia coli | |
benzyl 2,3,4-tri-O-benzyl-6-deoxy-6-dimethylmalonate-alpha-D-mannopyranoside | - |
Saccharomyces cerevisiae | |
benzyl 2,3,4-tri-O-benzyl-6-O-trifluoromethanesulfonyl-alpha-D-mannose | - |
Escherichia coli | |
benzyl 2,3,4-tri-O-benzyl-6-O-trifluoromethanesulfonyl-alpha-D-mannose | - |
Saccharomyces cerevisiae | |
benzyl 2,3,4-tri-O-benzyl-alpha-D-mannose | - |
Escherichia coli | |
benzyl 2,3,4-tri-O-benzyl-alpha-D-mannose | - |
Saccharomyces cerevisiae | |
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 | |
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 | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-Mannose 6-phosphate | Escherichia coli | - |
D-Fructose 6-phosphate | - |
r | |
D-Mannose 6-phosphate | Saccharomyces cerevisiae | - |
D-Fructose 6-phosphate | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Saccharomyces cerevisiae | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-Mannose 6-phosphate | - |
Escherichia coli | D-Fructose 6-phosphate | - |
r | |
D-Mannose 6-phosphate | - |
Saccharomyces cerevisiae | D-Fructose 6-phosphate | - |
r | |
additional information | Molecular mechanics study of enzyme substrate and inhibitors, overview | Escherichia coli | ? | - |
? | |
additional information | Molecular mechanics study of enzyme substrate and inhibitors, overview | Saccharomyces cerevisiae | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
Phosphomannose isomerase | - |
Escherichia coli |
Phosphomannose isomerase | - |
Saccharomyces cerevisiae |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Escherichia coli |
25 | - |
assay at | Saccharomyces cerevisiae |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.1 | - |
assay at | Escherichia coli |
7.1 | - |
assay at | Saccharomyces cerevisiae |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0105 | - |
6-deoxy-6-dicarboxymethyl-D-mannose | pH 7.1, 25°C, recombinant enzyme | Saccharomyces cerevisiae | |
0.115 | - |
6-deoxy-6-dicarboxymethyl-D-mannose | pH 7.1, 25°C, recombinant enzyme | Escherichia coli |
IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|
0.0181 | - |
pH 7.1, 25°C, recombinant enzyme | Saccharomyces cerevisiae | 6-deoxy-6-dicarboxymethyl-D-mannose | |
0.199 | - |
pH 7.1, 25°C, recombinant enzyme | Escherichia coli | 6-deoxy-6-dicarboxymethyl-D-mannose | |
0.37 | - |
pH 7.1, 25°C, recombinant enzyme | Escherichia coli | 5-deoxy-5-phosphonomethyl-D-arabinonohydroxamic acid | |
0.9 | - |
pH 7.1, 25°C, recombinant enzyme | Saccharomyces cerevisiae | 6-deoxy-6-carboxymethyl-D-mannose | |
1.61 | - |
pH 7.1, 25°C, recombinant enzyme | Saccharomyces cerevisiae | 6-deoxy-6-phosphonomethyl-D-mannose | |
2.2 | - |
pH 7.1, 25°C, recombinant enzyme | Saccharomyces cerevisiae | 5-deoxy-5-phosphonomethyl-D-arabinonohydroxamic acid | |
3 | - |
above, pH 7.1, 25°C, recombinant enzyme | Escherichia coli | 5-deoxy-5-phosphonomethyl-D-arabinonate | |
3 | - |
above, pH 7.1, 25°C, recombinant enzyme | Escherichia coli | 5-deoxy-5-phosphonomethyl-D-arabinonohydrazide | |
4.6 | - |
pH 7.1, 25°C, recombinant enzyme | Escherichia coli | 6-deoxy-6-carboxymethyl-D-mannose | |
4.7 | - |
pH 7.1, 25°C, recombinant enzyme | Escherichia coli | 6-deoxy-6-phosphonomethyl-D-mannose |