Application | Comment | Organism |
---|---|---|
pharmacology | enzymes of the shikimate pathway has been promoted as a target for the development of antimicrobial agents | Escherichia coli |
Cloned (Comment) | Organism |
---|---|
ydiB gene, expression in Escherichia coli BL21(DE3) | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
3-dehydroshikimate + NAD(P)H + H+ | Escherichia coli | YdiB catalyzes the reduction of 3-dehydroshikimate to shikimate as part of the shikimate pathway | shikimate + NAD(P)+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P0A6D5 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Escherichia coli |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
L-quinate + NAD(P)+ = 3-dehydroquinate + NAD(P)H + H+ | reaction mechanism, in which an aspartate acts as the general acid/base catalyst during the hydride transfer | Escherichia coli | |
shikimate + NAD(P)+ = 3-dehydroshikimate + NAD(P)H + H+ | reaction mechanism, in which an aspartate acts as the general acid/base catalyst during the hydride transfer | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
3-dehydroshikimate + NAD(P)H + H+ | YdiB catalyzes the reduction of 3-dehydroshikimate to shikimate as part of the shikimate pathway | Escherichia coli | shikimate + NAD(P)+ | - |
? | |
L-quinate + NAD(P)+ | detailed strucure of YdiB, specificity for binding NAD+/NADH over NADP+/NADPH | Escherichia coli | 3-dehydroquinate + NAD(P)H + H+ | - |
r | |
shikimate + NAD(P)+ | detailed strucure of YdiB, catalytic mechanism, specificity for binding NAD+/NADH over NADP+/NADPH | Escherichia coli | 3-dehydroshikimate + NAD(P)H + H+ | - |
r |
Subunits | Comment | Organism |
---|---|---|
homodimer | - |
Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
More | YdiB is a class A NAD(P)+-dependent oxidoreductase | Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
10.6 | - |
assay at | Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | NAD+ binding site, bound very tightly, NAD+ is bound to the Rossmann domain in an elongated fashion with the nicotinamide ring in the pro-R conformation, specificity for binding NAD+ over NADP+ | Escherichia coli | |
NADH | specificity for binding NADH over NADPH | Escherichia coli | |
NADP+ | specificity for binding NAD+ over NADP+ | Escherichia coli | |
NADPH | specificity for binding NADH over NADPH | Escherichia coli |