Inhibitors | Comment | Organism | Structure |
---|---|---|---|
L-quinate | competitive inhibitor with respect to shikimate | Pinus taeda | |
shikimate | competitive inhibitor with respect to L-quinate | Pinus taeda |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.001 | - |
NADP+ | pH 10, 20°C, cosubstrate shikimate, both forms of quinate (shikimate) dehydrogenase | Pinus taeda | |
0.005 | 0.012 | NADPH | pH 10, 20°C, cosubstrate dehydroquinate, both forms of quinate (shikimate) dehydrogenase | Pinus taeda | |
0.007 | - |
NADP+ | pH 10, 20°C, cosubstrate L-quinate, both forms of quinate (shikimate) dehydrogenase | Pinus taeda | |
0.7 | 0.8 | shikimate | pH 10, 20°C, cosubstrate NADP+, both forms of quinate (shikimate) dehydrogenase | Pinus taeda | |
1 | - |
dehydroquinate | pH 10, 20°C, cosubstrate NADPH, form P1 of quinate (shikimate) dehydrogenase | Pinus taeda | |
3.4 | 3.6 | L-quinate | pH 10, 20°C, cosubstrate NADP+, both forms of quinate (shikimate) dehydrogenase | Pinus taeda | |
5.3 | - |
dehydroquinate | pH 10, 20°C, cosubstrate NADPH, form P2 of quinate (shikimate) dehydrogenase | Pinus taeda |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
35000 | - |
two forms of the bifunctional quinate (shikimate) dehydrogenase, gel filtration | Pinus taeda |
53000 | - |
two forms of the bifunctional quinate (shikimate) dehydrogenase, gel filtration | Pinus taeda |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
3-dehydroquinate + NADPH + H+ | Pinus taeda | may be responsible for the synthesis of quinic acid from the intermediate compound of the shikimate pathway, dehydroquinic acid | L-quinate + NADP+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pinus taeda | - |
20 years old | - |
Purification (Comment) | Organism |
---|---|
3000fold, two forms of the bifunctional quinate (shikimate) dehydrogenase: P1 and P2 | Pinus taeda |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
needle | from current-year shoots of 20 years old trees, the youngest basal parts of needles | Pinus taeda | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
- |
Pinus taeda |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
3-dehydroquinate + NADPH + H+ | may be responsible for the synthesis of quinic acid from the intermediate compound of the shikimate pathway, dehydroquinic acid | Pinus taeda | L-quinate + NADP+ | - |
? | |
L-quinate + NADP+ | both quinate and shikimate dehydrogenase activities are catalyzed by a single broad-specificity quinate (shikimate) dehydrogenase with a common substrate binding site, the velocity is 2fold greater with quinate than with shikimate | Pinus taeda | 3-dehydroquinate + NADPH + H+ | - |
r | |
shikimate + NADP+ | both quinate and shikimate dehydrogenase activities are catalyzed by a single broad-specificity quinate (shikimate) dehydrogenase with a common substrate binding site, the velocity is 2fold lower with shikimate than with quinate | Pinus taeda | 3-dehydroshikimate + NADPH + H+ | - |
r |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
20 | - |
assay at | Pinus taeda |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.7 | - |
back reaction, dehydroquinate or dehydroshikimate and NADPH as substrates | Pinus taeda |
10.3 | - |
quinate or shikimate and NADP+ as substrates | Pinus taeda |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADP+ | - |
Pinus taeda | |
NADPH | - |
Pinus taeda |