Application | Comment | Organism |
---|---|---|
drug development | the essential enzyme is a potential target for herbicides and antimicrobials | Corynebacterium glutamicum |
Cloned (Comment) | Organism |
---|---|
gene cgR_0495, recombinant expression | Corynebacterium glutamicum |
gene qsuD, recombinant expression | Corynebacterium glutamicum |
Crystallization (Comment) | Organism |
---|---|
crystal structure analysis of binary and ternary complexes of enzyme and substrates, PDB IDs 3JYP, 2NLO, 3JYO, and 3JYQ | Corynebacterium glutamicum |
crystal structure determination as enzyme in binary complex with NAD+ (PDB ID 3JYO), or in ternary complex with shikimate and NADH (PDB ID 3JYQ), or in ternary complex with quinate and NADH (PDB ID 3JYP) | Corynebacterium glutamicum |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.018 | - |
NAD+ | with shikimate, pH 8.6, 30°C | Corynebacterium glutamicum | |
0.187 | - |
shikimate | with NADP+, pH 7.0, 30°C | Corynebacterium glutamicum | |
0.2 | - |
3-dehydroshikimate | with NADPH, pH 7.0, 30°C | Corynebacterium glutamicum | |
0.26 | - |
shikimate | with NAD+, pH 8.6, 30°C | Corynebacterium glutamicum | |
2.541 | - |
L-quinate | with NADPH, pH 7.0, 30°C | Corynebacterium glutamicum |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-quinate + NAD+ | Corynebacterium glutamicum | - |
3-dehydroquinate + NADH + H+ | - |
r | |
L-quinate + NAD+ | Corynebacterium glutamicum ATCC 13032 | - |
3-dehydroquinate + NADH + H+ | - |
r | |
L-quinate + NADP+ | Corynebacterium glutamicum | - |
3-dehydroquinate + NADPH + H+ | - |
r | |
shikimate + NAD+ | Corynebacterium glutamicum | - |
3-dehydroshikimate + NADH + H+ | - |
r | |
shikimate + NAD+ | Corynebacterium glutamicum ATCC 13032 | - |
3-dehydroshikimate + NADH + H+ | - |
r | |
shikimate + NADP+ | Corynebacterium glutamicum | - |
3-dehydroshikimate + NADPH + H+ | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Corynebacterium glutamicum | A4QB65 | - |
- |
Corynebacterium glutamicum | Q9X5C9 | - |
- |
Corynebacterium glutamicum ATCC 13032 | Q9X5C9 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
L-quinate + NAD(P)+ = 3-dehydroquinate + NAD(P)H + H+ | catalytic reaction mechanism | Corynebacterium glutamicum | |
shikimate + NAD(P)+ = 3-dehydroshikimate + NAD(P)H + H+ | catalytic reaction mechanism | Corynebacterium glutamicum |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-quinate + NAD+ | - |
Corynebacterium glutamicum | 3-dehydroquinate + NADH + H+ | - |
r | |
L-quinate + NAD+ | - |
Corynebacterium glutamicum ATCC 13032 | 3-dehydroquinate + NADH + H+ | - |
r | |
L-quinate + NADP+ | - |
Corynebacterium glutamicum | 3-dehydroquinate + NADPH + H+ | - |
r | |
additional information | the enzyme is capable of recognizing both quinate and shikimate, it is usually considered to have dual substrate specificity | Corynebacterium glutamicum | ? | - |
? | |
additional information | the enzyme is capable of recognizing both quinate and shikimate, it is usually considered to have dual substrate specificity | Corynebacterium glutamicum ATCC 13032 | ? | - |
? | |
shikimate + NAD+ | - |
Corynebacterium glutamicum | 3-dehydroshikimate + NADH + H+ | - |
r | |
shikimate + NAD+ | - |
Corynebacterium glutamicum ATCC 13032 | 3-dehydroshikimate + NADH + H+ | - |
r | |
shikimate + NADP+ | - |
Corynebacterium glutamicum | 3-dehydroshikimate + NADPH + H+ | - |
r |
Subunits | Comment | Organism |
---|---|---|
dimer | - |
Corynebacterium glutamicum |
Synonyms | Comment | Organism |
---|---|---|
quinate/shikimate dehydrogenase | - |
Corynebacterium glutamicum |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Corynebacterium glutamicum |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.036 | - |
L-quinate | with NADPH, pH 7.0, 30°C | Corynebacterium glutamicum | |
9.6 | - |
shikimate | with NAD+, pH 8.6, 30°C | Corynebacterium glutamicum | |
31.1 | - |
shikimate | with NADP+, pH 7.0, 30°C | Corynebacterium glutamicum | |
329 | - |
3-dehydroshikimate | with NADPH, pH 7.0, 30°C | Corynebacterium glutamicum |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Corynebacterium glutamicum |
8.6 | - |
assay at | Corynebacterium glutamicum |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | dependent on | Corynebacterium glutamicum | |
NADH | dependent on | Corynebacterium glutamicum | |
NADP+ | - |
Corynebacterium glutamicum | |
NADPH | - |
Corynebacterium glutamicum |
General Information | Comment | Organism |
---|---|---|
evolution | SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences | Corynebacterium glutamicum |
malfunction | disruption of the qdh gene in prevents growth on both compounds, demonstrating the important role of the enzyme in hydroaromatic catabolism | Corynebacterium glutamicum |
metabolism | the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites | Corynebacterium glutamicum |
physiological function | shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes. The reduced efficiency of Corynebacterium glutamicum enzyme with shikimate as a substrate may also result in part from the flexibility of the catalytic group, Lys73, which adopts multiple conformations in the shikimate-liganded enzyme structure | Corynebacterium glutamicum |