Application | Comment | Organism |
---|---|---|
drug development | the enzyme is a target for antibacterial drug development | Staphylococcus aureus |
Cloned (Comment) | Organism |
---|---|
gene aroE, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS | Staphylococcus aureus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
2,2'-bithiophene-5-carboxylic acid | the inhibitor is identified by virtual screeening, 87% inhibition at 0.2 mM, competitive versus shikimate, uncompetitive versus NADP+. Flexible docking studies reveal that the inhibitor molecule makes interactions with catalytic residues | Staphylococcus aureus | |
2-[4-(trifluoromethyl)phenyl]-1,3-thiazole-4-carboxylic acid | 31% inhibition at 0.2 mM | Staphylococcus aureus | |
2-[methyl[3-(trifluoromethyl)naphthalen-1-yl]amino]ethan-1-ol | 49% inhibition at 0.2 mM | Staphylococcus aureus | |
3-ethyl-3,4-dihydro-2H-1-benzopyran | 31% inhibition at 0.2 mM | Staphylococcus aureus | |
4-[(morpholin-4-yl)methyl]benzoic acid | 31% inhibition at 0.2 mM | Staphylococcus aureus | |
5-(hex-1-yn-1-yl)furan-2-carboxylic acid | 29% inhibition at 0.2 mM | Staphylococcus aureus | |
6-hydroxy-2,3-dihydrobenzo[b]furan-3-one | the inhibitor is identified by virtual screeening, 99% inhibition at 0.2 mM, mixed-type inhibition versus shikimate, uncompetitive versus NADP+. Flexible docking studies reveal that the inhibitor molecule makes interactions with catalytic residues | Staphylococcus aureus | |
7-hydroxy-2,2,8-trimethyl-2,3-dihydro-4H-chromen-4-one | the inhibitor is identified by virtual screeening, 87% inhibition at 0.2 mM, competitive versus shikimate, uncompetitive versus NADP+. Flexible docking studies reveal that the inhibitor molecule makes interactions with catalytic residues | Staphylococcus aureus | |
methyl 3-hydroxy-1-benzothiophene-2-carboxylate | 33% inhibition at 0.2 mM | Staphylococcus aureus | |
[2-[2-(dimethylamino)ethoxy]phenyl]methanol | 45% inhibition at 0.2 mM | Staphylococcus aureus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | the enzyme shows Michaelis-Menten kinetics toward both substrates shikimate and NADP+, kinetic analysis, sequential random mechanism, overview | Staphylococcus aureus | |
0.03746 | - |
shikimate | pH not specified in the publication, 25°C | Staphylococcus aureus | |
0.04255 | - |
NADP+ | pH not specified in the publication, 25°C | Staphylococcus aureus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
29000 | - |
gel filtration | Staphylococcus aureus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
shikimate + NADP+ | Staphylococcus aureus | - |
3-dehydroshikimate + NADPH + H+ | - |
? | |
shikimate + NADP+ | Staphylococcus aureus ATCC MRSA252 | - |
3-dehydroshikimate + NADPH + H+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Staphylococcus aureus | - |
- |
- |
Staphylococcus aureus ATCC MRSA252 | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography | Staphylococcus aureus |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+ | the enzyme catalysis follows a sequential random mechanism, enzyme catalysis depends on acid-basic amino acids | Staphylococcus aureus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
shikimate + NADP+ | - |
Staphylococcus aureus | 3-dehydroshikimate + NADPH + H+ | - |
? | |
shikimate + NADP+ | - |
Staphylococcus aureus ATCC MRSA252 | 3-dehydroshikimate + NADPH + H+ | - |
? |
Subunits | Comment | Organism |
---|---|---|
monomer | 1 * 29000, SDS-PAGE | Staphylococcus aureus |
More | three-dimensional structure determination by homology modelling and validation | Staphylococcus aureus |
Synonyms | Comment | Organism |
---|---|---|
AroE | - |
Staphylococcus aureus |
SDH | - |
Staphylococcus aureus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
65 | - |
- |
Staphylococcus aureus |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
10 | 60 | activity range, maximum activity at 65°C, inactivation at 70°C | Staphylococcus aureus |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
135.8 | - |
shikimate | pH not specified in the publication, 25°C | Staphylococcus aureus | |
146.2 | - |
NADP+ | pH not specified in the publication, 25°C | Staphylococcus aureus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
9 | 11 | - |
Staphylococcus aureus |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
6.5 | 12.5 | activity range, overview | Staphylococcus aureus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADP+ | - |
Staphylococcus aureus |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetic study of the enzyme-inhibitor complexes | Staphylococcus aureus |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
3430 | - |
NADP+ | pH not specified in the publication, 25°C | Staphylococcus aureus | |
3620 | - |
shikimate | pH not specified in the publication, 25°C | Staphylococcus aureus |