Inhibitors | Comment | Organism | Structure |
---|---|---|---|
2,2'-(2-hydroxy-1,3-phenylene)bis(2-oxoacetic acid) | slow-tight inhibition | Escherichia coli | |
2,2'-benzene-1,3-diylbis(oxoacetic acid) | slow inhibition | Escherichia coli | |
dimethyl-(2E,2'E)-2,2'-benzene-1,3-diylbis[(hydroxyimino)ethanoate] | slow inhibition | Escherichia coli | |
dimethyl-2,2'-(2-hydroxy-1,3-phenylene)bis(2-oxoacetate) | slow-tight inhibition | Escherichia coli | |
additional information | 1,3-phenylene bis(ketoacid) derivatives as enzyme inhibitors, overview. Ketoacid derivatives act as slow and slow-tight binding inhibitors with either an encounter complex or a condensation product for the slow and slow-tight binding inhibitors, respectively, modeling, overview. No or poor inhibition by dimethyl 2,2'-benzene-1,3-diylbis(oxoacetate), (2E,2'E)-2,2'-benzene-1,3-diylbis[(hydroxyimino)ethanoic acid], and dimethyl-2,2'-(2-methoxy-1,3-phenylene)bis(2-oxoacetate) | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
(S)-aspartate-4-semialdehyde + pyruvate | Escherichia coli | the enzyme-catalyzed reaction is initiated by condensation of pyruvate with an active site Lys161 forming a Schiff base. Subsequent tautomerization to the enamine and aldol-type reaction with (S)-aspartate-4-semialdehyde then generates an acyclic enzyme-bound intermediate. Transimination of the acyclic intermediate yields the cyclic alcohol (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid, with simultaneous release of the active site lysine residue | (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid + H2O | - |
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Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(S)-aspartate-4-semialdehyde + pyruvate | - |
Escherichia coli | (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid + H2O | - |
? | |
(S)-aspartate-4-semialdehyde + pyruvate | the enzyme-catalyzed reaction is initiated by condensation of pyruvate with an active site Lys161 forming a Schiff base. Subsequent tautomerization to the enamine and aldol-type reaction with (S)-aspartate-4-semialdehyde then generates an acyclic enzyme-bound intermediate. Transimination of the acyclic intermediate yields the cyclic alcohol (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid, with simultaneous release of the active site lysine residue | Escherichia coli | (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid + H2O | - |
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Synonyms | Comment | Organism |
---|---|---|
DHDPS | - |
Escherichia coli |
dihydrodipicolinate synthase | - |
Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Escherichia coli |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.04 | - |
dimethyl-2,2'-(2-hydroxy-1,3-phenylene)bis(2-oxoacetate) | pH 8.0, 30°C | Escherichia coli | |
0.29 | - |
2,2'-(2-hydroxy-1,3-phenylene)bis(2-oxoacetic acid) | pH 8.0, 30°C | Escherichia coli | |
0.33 | - |
dimethyl-(2E,2'E)-2,2'-benzene-1,3-diylbis[(hydroxyimino)ethanoate] | pH 8.0, 30°C | Escherichia coli | |
2.96 | - |
2,2'-benzene-1,3-diylbis(oxoacetic acid) | pH 8.0, 30°C | Escherichia coli |
General Information | Comment | Organism |
---|---|---|
metabolism | dihydrodipicolinate synthase is a key enzyme in the lysine biosynthesis pathway that catalyzes the condensation of pyruvate and aspartate semi-aldehyde | Escherichia coli |