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3-dehydroquinate
3-dehydroshikimate + H2O
3-dehydroquinate + NADH + H+
quinate + NAD+
3-dehydroquinate + NADPH + H+
quinate + NADP+
3-dehydroshikimate + NAD(P)H + H+
shikimate + NAD(P)+
3-dehydroshikimate + NADH
shikimate + NAD+
-
SDH reaction, very low activity with NAD+
-
-
r
3-dehydroshikimate + NADH + H+
shikimate + NAD+
3-dehydroshikimate + NADP+
gallate + NADPH + H+
3-dehydroshikimate + NADPH
?
3-dehydroshikimate + NADPH
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
shikimate + NADP+
L-quinate + NAD+
3-dehydroquinate + NADH + H+
L-quinate + NADP+
3-dehydroquinate + NADPH + H+
quinate + NAD(P)+
3-dehydroquinate + NAD(P)H + H+
-
-
-
?
quinate + NAD+
3-dehydroquinate + NADH + H+
quinate + NADP+
3-dehydroquinate + NADPH + H+
shikimate + NAD(P)+
3-dehydroshikimate + NAD(P)H + H+
shikimate + NAD+
3-dehydroshikimate + NADH + H+
shikimate + NADP+
3-dehydroshikimate + NADPH
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
additional information
?
-
3-dehydroquinate

3-dehydroshikimate + H2O
-
-
-
-
r
3-dehydroquinate
3-dehydroshikimate + H2O
-
DQD reaction
-
-
r
3-dehydroquinate
3-dehydroshikimate + H2O
-
-
-
-
r
3-dehydroquinate + NADH + H+

quinate + NAD+
-
-
-
r
3-dehydroquinate + NADH + H+
quinate + NAD+
-
-
-
r
3-dehydroquinate + NADPH + H+

quinate + NADP+
-
-
-
r
3-dehydroquinate + NADPH + H+
quinate + NADP+
-
-
-
r
3-dehydroshikimate + NAD(P)H + H+

shikimate + NAD(P)+
-
-
-
r
3-dehydroshikimate + NAD(P)H + H+
shikimate + NAD(P)+
fourth enzyme involved in the shikimate pathway
-
-
r
3-dehydroshikimate + NAD(P)H + H+
shikimate + NAD(P)+
-
-
-
r
3-dehydroshikimate + NAD(P)H + H+
shikimate + NAD(P)+
fourth enzyme involved in the shikimate pathway
-
-
r
3-dehydroshikimate + NADH + H+

shikimate + NAD+
less than 1% of the rate with 3-dehydroquinate
-
-
r
3-dehydroshikimate + NADH + H+
shikimate + NAD+
less than 1% of the rate with 3-dehydroquinate
-
-
r
3-dehydroshikimate + NADP+

gallate + NADPH + H+
-
-
-
r
3-dehydroshikimate + NADP+
gallate + NADPH + H+
-
-
-
r
3-dehydroshikimate + NADPH

?
-
enzyme of shikimic acid biosynthesis
-
-
r
3-dehydroshikimate + NADPH
?
-
pathway of biosynthesis of aromatic amino acids
-
-
r
3-dehydroshikimate + NADPH

shikimate + NADP+
-
-
-
-
r
3-dehydroshikimate + NADPH
shikimate + NADP+
-
-
-
r
3-dehydroshikimate + NADPH
shikimate + NADP+
-
-
-
-
r
3-dehydroshikimate + NADPH
shikimate + NADP+
-
NADH may substitute for NADPH
-
-
r
3-dehydroshikimate + NADPH
shikimate + NADP+
-
-
-
-
r
3-dehydroshikimate + NADPH
shikimate + NADP+
-
-
-
?
3-dehydroshikimate + NADPH
shikimate + NADP+
-
-
-
?
3-dehydroshikimate + NADPH
shikimate + NADP+
-
-
-
?
3-dehydroshikimate + NADPH
shikimate + NADP+
-
-
-
-
r
3-dehydroshikimate + NADPH
shikimate + NADP+
-
SDH reaction
-
-
r
3-dehydroshikimate + NADPH + H+

shikimate + NADP+
-
structure of the enzyme is a compact alpha/beta sandwich with two distinct domains, responsible for binding substrate and NADP cofactor, respectively
-
-
?
3-dehydroshikimate + NADPH + H+
shikimate + NADP+
-
-
-
r
3-dehydroshikimate + NADPH + H+
shikimate + NADP+
-
-
-
r
3-dehydroshikimate + NADPH + H+
shikimate + NADP+
-
-
-
-
?
3-dehydroshikimate + NADPH + H+
shikimate + NADP+
-
-
-
r
3-dehydroshikimate + NADPH + H+
shikimate + NADP+
catalytic mechanism, residue Lys69 plays a catalytic role and is not involved in substrate binding
-
-
r
3-dehydroshikimate + NADPH + H+
shikimate + NADP+
-
-
-
?, r
3-dehydroshikimate + NADPH + H+
shikimate + NADP+
-
-
-
-
r
L-quinate + NAD+

3-dehydroquinate + NADH + H+
-
-
-
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
-
-
r
L-quinate + NADP+

3-dehydroquinate + NADPH + H+
activity of T381 enzyme mutants, not of wild-type enzyme, see also EC 1.1.1.282
-
-
r
L-quinate + NADP+
3-dehydroquinate + NADPH + H+
-
-
-
r
L-quinate + NADP+
3-dehydroquinate + NADPH + H+
-
activity by only mutant S275G/T318G, not the wild-type enzyme
-
-
r
quinate + NAD+

3-dehydroquinate + NADH + H+
-
-
-
r
quinate + NAD+
3-dehydroquinate + NADH + H+
in contrast to shikimate, quinate may form a hydrogen bond to the NAD+, and the hydroxyl group of a active-site threonine hydrogen bonds to quinate more effectively than shikimate resulting in a lower Michaelis constant and higher catalytic efficiency for quinate
-
-
?
quinate + NAD+
3-dehydroquinate + NADH + H+
-
-
-
r
quinate + NAD+
3-dehydroquinate + NADH + H+
the fourth enzyme in the shikimate pathway
-
-
r
quinate + NAD+
3-dehydroquinate + NADH + H+
the fourth enzyme in the shikimate pathway
-
-
r
quinate + NADP+

3-dehydroquinate + NADPH + H+
-
reversible activity of YdiB, no activity with paralogue HI0607
-
-
r
quinate + NADP+
3-dehydroquinate + NADPH + H+
-
-
-
r
quinate + NADP+
3-dehydroquinate + NADPH + H+
-
-
-
r
shikimate + NAD(P)+

3-dehydroshikimate + NAD(P)H + H+
-
-
-
?
shikimate + NAD(P)+
3-dehydroshikimate + NAD(P)H + H+
-
-
-
?
shikimate + NAD+

3-dehydroshikimate + NADH + H+
-
-
-
-
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
?
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
the enzyme is also active with NAD+
-
-
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
r
shikimate + NADP+

3-dehydroshikimate + NADPH
-
assay at 24°C, pH 9.0
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH
-
SDH reaction
-
-
r
shikimate + NADP+

3-dehydroshikimate + NADPH + H+
-
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Bambusa sp.
-
-
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
analysis of the 3-dehydroshikimate binding site
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
reversible activity of YdiB and AroE, paralogue HI0607 catalyzes the oxidative reaction with low activity
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
the fourth enzyme in the shikimate pathway
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
the fourth enzyme in the shikimate pathway
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
additional information

?
-
-
the bifunctional enzyme performs dehydroquinate dehydratase and shikimate dehydrogenase activities, metabolic channeling
-
-
?
additional information
?
-
-
the bifunctional enzyme performs dehydroquinate dehydratase and shikimate dehydrogenase activities
-
-
?
additional information
?
-
The bifunctional enzyme also catalyzes dehydration of 3-dehydroquinate to 3-dehydroshikimate
-
-
?
additional information
?
-
The bifunctional enzyme also catalyzes dehydration of 3-dehydroquinate to 3-dehydroshikimate
-
-
?
additional information
?
-
-
The bifunctional enzyme also catalyzes dehydration of 3-dehydroquinate to 3-dehydroshikimate
-
-
?
additional information
?
-
no activity with quinate
-
-
?
additional information
?
-
no activity with quinate
-
-
?
additional information
?
-
usage of recombinant shikimate dehydrogenase as sensor reaction for determination of the cytosolic NADPH/NADP ratio in Saccharomyces cerevisiae, quantitative measurements of physiological variables in the cytosolic compartment by GC-MS/MS, cytosolic NADPH/NADP ratio in batch experiments, method, overview
-
-
?
additional information
?
-
product analysis by GC-MS. No or poor quinate dehydrogenase activity
-
-
-
additional information
?
-
product analysis by GC-MS. No or poor quinate dehydrogenase activity
-
-
-
additional information
?
-
product analysis by GC-MS. No or poor quinate dehydrogenase activity
-
-
-
additional information
?
-
-
product analysis by GC-MS. No or poor quinate dehydrogenase activity
-
-
-
additional information
?
-
-
no activity with quinate
-
-
?
additional information
?
-
-
fourth enzyme in the shikimate biosynthetic pathway
-
-
?
additional information
?
-
-
the cytosolic shikimate synthesis cannot complement loss of the plastidial pathway
-
-
?
additional information
?
-
the cytosolic shikimate synthesis cannot complement loss of the plastidial pathway
-
-
?
additional information
?
-
the cytosolic shikimate synthesis cannot complement loss of the plastidial pathway
-
-
?
additional information
?
-
-
the enzyme also shows 3-dehydroquinate dehydratase activity, EC 4.2.1.10
-
-
?
additional information
?
-
the enzyme also shows 3-dehydroquinate dehydratase activity, EC 4.2.1.10
-
-
?
additional information
?
-
the enzyme also shows 3-dehydroquinate dehydratase activity, EC 4.2.1.10
-
-
?
additional information
?
-
-
the bifunctional enzyme dehydroquinate dehydratase/shikimate dehydrogenase (DQD/SDH cf. EC 4.2.1.10 and EC 1.1.1.25) catalyzes the the conversion of 3-dehydroquinate to shikimate via 3-dehydroshikimate
-
-
?
additional information
?
-
-
the bifunctional enzyme dehydroquinate dehydratase/shikimate dehydrogenase (DQD3/SDH cf. EC 4.2.1.10 and EC 1.1.1.25) catalyzes the the conversion of 3-dehydroquinate to shikimate via 3-dehydroshikimate
-
-
?
additional information
?
-
-
The bifunctional enzyme also catalyzes dehydration of 3-dehydroquinate to 3-dehydroshikimate
-
-
?
additional information
?
-
-
The bifunctional enzyme also catalyzes dehydration of 3-dehydroquinate to 3-dehydroshikimate. Under saturating conditions, Poptr5 displays strong activity with shikimate but no detectable activity with quinate even at elevated enzyme concentrations. The isozyme shows no quinate hydrolyase activity
-
-
?
additional information
?
-
-
under saturating conditions, Poptr1 displays strong activity with shikimate but no detectable activity with quinate even at elevated enzyme concentrations. The isozyme shows no quinate hydrolyase activity
-
-
?
additional information
?
-
-
the wild-type enzyme PoptrSDH1 is highly shikimate-specific, only the S275G/T318G mutant shows activity with quinate
-
-
-
additional information
?
-
-
the bifunctional enzyme dehydroquinate dehydratase/shikimate dehydrogenase (DQD/SDH cf. EC 4.2.1.10 and EC 1.1.1.25) catalyzes the the conversion of 3-dehydroquinate to shikimate via 3-dehydroshikimate
-
-
?
additional information
?
-
-
the bifunctional enzyme dehydroquinate dehydratase/shikimate dehydrogenase (DQD3/SDH cf. EC 4.2.1.10 and EC 1.1.1.25) catalyzes the the conversion of 3-dehydroquinate to shikimate via 3-dehydroshikimate
-
-
?
additional information
?
-
-
The bifunctional enzyme also catalyzes dehydration of 3-dehydroquinate to 3-dehydroshikimate. Under saturating conditions, Poptr5 displays strong activity with shikimate but no detectable activity with quinate even at elevated enzyme concentrations. The isozyme shows no quinate hydrolyase activity
-
-
?
additional information
?
-
-
under saturating conditions, Poptr1 displays strong activity with shikimate but no detectable activity with quinate even at elevated enzyme concentrations. The isozyme shows no quinate hydrolyase activity
-
-
?
additional information
?
-
no activity with quinate
-
-
?
additional information
?
-
no activity with quinate
-
-
?
additional information
?
-
broad extent to which the SDH enzyme superfamily has diversified. 5 evolutionarily distinct SDH homologs in the genome of the common soil-inhabiting bacterium, Pseudomonas putida KT2440
-
-
?
additional information
?
-
broad extent to which the SDH enzyme superfamily has diversified. 5 evolutionarily distinct SDH homologs in the genome of the common soil-inhabiting bacterium, Pseudomonas putida KT2440
-
-
?
additional information
?
-
analyzing the catalytic activity of SDH, the enzyme produce shikimate from 3-dehydroshikimate (3-DHS) in the presence of NADPH as a cofactor, whereas it forms gallic acid in the presence of NADP+
-
-
-
additional information
?
-
-
analyzing the catalytic activity of SDH, the enzyme produce shikimate from 3-dehydroshikimate (3-DHS) in the presence of NADPH as a cofactor, whereas it forms gallic acid in the presence of NADP+
-
-
-
additional information
?
-
no activity with quinate
-
-
?
additional information
?
-
no activity with quinate
-
-
?
additional information
?
-
even in the presence of a high concentration of quinate (4 mM), SDH displays no activity using either NADP+ or NAD+ as a cofactor
-
-
?
additional information
?
-
the SDH domain from the Toxoplasma gondii is part of the AROM complex. No activity with quinate
-
-
?
additional information
?
-
isozyme VvSDH1 also produces gallate from shikimate with NADP+
-
-
?
additional information
?
-
isozyme VvSDH1 also produces gallate from shikimate with NADP+
-
-
?
additional information
?
-
isozyme VvSDH1 also produces gallate from shikimate with NADP+
-
-
?
additional information
?
-
isozyme VvSDH1 also produces gallate from shikimate with NADP+
-
-
?
additional information
?
-
isozyme VvSDH2 does not produce gallate from shikimate
-
-
?
additional information
?
-
isozyme VvSDH2 does not produce gallate from shikimate
-
-
?
additional information
?
-
isozyme VvSDH2 does not produce gallate from shikimate
-
-
?
additional information
?
-
isozyme VvSDH2 does not produce gallate from shikimate
-
-
?
additional information
?
-
isozyme VvSDH3 also produces gallate from shikimate with NADP+ with low activity
-
-
?
additional information
?
-
isozyme VvSDH3 also produces gallate from shikimate with NADP+ with low activity
-
-
?
additional information
?
-
isozyme VvSDH3 also produces gallate from shikimate with NADP+ with low activity
-
-
?
additional information
?
-
isozyme VvSDH3 also produces gallate from shikimate with NADP+ with low activity
-
-
?
additional information
?
-
isozyme VvSDH4 also produces gallate from shikimate with NADP+ with low activity
-
-
?
additional information
?
-
isozyme VvSDH4 also produces gallate from shikimate with NADP+ with low activity
-
-
?
additional information
?
-
isozyme VvSDH4 also produces gallate from shikimate with NADP+ with low activity
-
-
?
additional information
?
-
isozyme VvSDH4 also produces gallate from shikimate with NADP+ with low activity
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3-dehydroquinate
3-dehydroshikimate + H2O
3-dehydroshikimate + NAD(P)H + H+
shikimate + NAD(P)+
3-dehydroshikimate + NADP+
gallate + NADPH + H+
-
-
-
r
3-dehydroshikimate + NADPH
?
3-dehydroshikimate + NADPH
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
shikimate + NADP+
L-quinate + NAD+
3-dehydroquinate + NADH + H+
L-quinate + NADP+
3-dehydroquinate + NADPH + H+
-
-
-
r
quinate + NAD+
3-dehydroquinate + NADH + H+
quinate + NADP+
3-dehydroquinate + NADPH + H+
-
reversible activity of YdiB, no activity with paralogue HI0607
-
-
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
additional information
?
-
3-dehydroquinate

3-dehydroshikimate + H2O
-
-
-
-
r
3-dehydroquinate
3-dehydroshikimate + H2O
-
-
-
-
r
3-dehydroshikimate + NAD(P)H + H+

shikimate + NAD(P)+
fourth enzyme involved in the shikimate pathway
-
-
r
3-dehydroshikimate + NAD(P)H + H+
shikimate + NAD(P)+
fourth enzyme involved in the shikimate pathway
-
-
r
3-dehydroshikimate + NADPH

?
-
enzyme of shikimic acid biosynthesis
-
-
r
3-dehydroshikimate + NADPH
?
-
pathway of biosynthesis of aromatic amino acids
-
-
r
3-dehydroshikimate + NADPH

shikimate + NADP+
-
-
-
-
r
3-dehydroshikimate + NADPH
shikimate + NADP+
-
-
-
r
3-dehydroshikimate + NADPH
shikimate + NADP+
-
-
-
-
r
3-dehydroshikimate + NADPH
shikimate + NADP+
-
-
-
-
r
3-dehydroshikimate + NADPH
shikimate + NADP+
-
-
-
-
r
3-dehydroshikimate + NADPH + H+

shikimate + NADP+
-
-
-
r
3-dehydroshikimate + NADPH + H+
shikimate + NADP+
-
-
-
?
L-quinate + NAD+

3-dehydroquinate + NADH + H+
-
-
-
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
-
-
-
r
quinate + NAD+

3-dehydroquinate + NADH + H+
the fourth enzyme in the shikimate pathway
-
-
r
quinate + NAD+
3-dehydroquinate + NADH + H+
the fourth enzyme in the shikimate pathway
-
-
r
shikimate + NAD+

3-dehydroshikimate + NADH + H+
-
-
-
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
the enzyme is also active with NAD+
-
-
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
-
-
-
r
shikimate + NADP+

3-dehydroshikimate + NADPH + H+
-
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
Bambusa sp.
-
-
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
reversible activity of YdiB and AroE, paralogue HI0607 catalyzes the oxidative reaction with low activity
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
the fourth enzyme in the shikimate pathway
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
the fourth enzyme in the shikimate pathway
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
-
?
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
-
-
-
r
additional information

?
-
-
the bifunctional enzyme performs dehydroquinate dehydratase and shikimate dehydrogenase activities, metabolic channeling
-
-
?
additional information
?
-
-
fourth enzyme in the shikimate biosynthetic pathway
-
-
?
additional information
?
-
-
the cytosolic shikimate synthesis cannot complement loss of the plastidial pathway
-
-
?
additional information
?
-
the cytosolic shikimate synthesis cannot complement loss of the plastidial pathway
-
-
?
additional information
?
-
the cytosolic shikimate synthesis cannot complement loss of the plastidial pathway
-
-
?
additional information
?
-
-
the bifunctional enzyme dehydroquinate dehydratase/shikimate dehydrogenase (DQD/SDH cf. EC 4.2.1.10 and EC 1.1.1.25) catalyzes the the conversion of 3-dehydroquinate to shikimate via 3-dehydroshikimate
-
-
?
additional information
?
-
-
the bifunctional enzyme dehydroquinate dehydratase/shikimate dehydrogenase (DQD3/SDH cf. EC 4.2.1.10 and EC 1.1.1.25) catalyzes the the conversion of 3-dehydroquinate to shikimate via 3-dehydroshikimate
-
-
?
additional information
?
-
-
the bifunctional enzyme dehydroquinate dehydratase/shikimate dehydrogenase (DQD/SDH cf. EC 4.2.1.10 and EC 1.1.1.25) catalyzes the the conversion of 3-dehydroquinate to shikimate via 3-dehydroshikimate
-
-
?
additional information
?
-
-
the bifunctional enzyme dehydroquinate dehydratase/shikimate dehydrogenase (DQD3/SDH cf. EC 4.2.1.10 and EC 1.1.1.25) catalyzes the the conversion of 3-dehydroquinate to shikimate via 3-dehydroshikimate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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(3E)-3-[2-(4-bromophenyl)hydrazinylidene]piperidine-2,4,6-trione
-
(3R,3'R,4S,4'S,5R,5'R)-N,N'-(butane-1,4-diyl)bis(3,4,5-trihydroxycyclohex-1-ene-1-carboxamide)
-
(3R,3'R,4S,4'S,5R,5'R)-N,N'-(ethane-1,2-diyl)bis(3,4,5-trihydroxycyclohex-1-ene-1-carboxamide)
-
(3R,3'R,4S,4'S,5R,5'R)-N,N'-(propane-1,3-diyl)bis(3,4,5-trihydroxycyclohex-1-ene-1-carboxamide)
-
(3R,4S,5R)-3,4,5-trihydroxy-N-(3-hydroxypropyl)cyclohex-1-ene-1-carboxamide
-
(3R,4S,5R)-3,4,5-trihydroxy-N-(4-hydroxybutyl)cyclohex-1-ene-1-carboxamide
-
(3R,4S,5R)-3,4,5-trihydroxy-N-(5-hydroxypentyl)cyclohex-1-ene-1-carboxamide
-
(3R,4S,5R)-3,4,5-trihydroxy-N-(6-hydroxyhexyl)cyclohex-1-ene-1-carboxamide
-
(3R,4S,5R)-3,4,5-tri[(tert-butyldimethylsilyl)oxy]cyclohex-1-enecarboxylic acid
-
(4Z)-4-[2-(3-hydroxyphenyl)triazan-1-ylidene]-5-methyl-2-[(piperidin-1-yl)methyl]-2,4-dihydro-3H-pyrazol-3-one
-
(azepan-1-yl)(3-methyl-4,5-dinitrophenyl)methanone
-
1,2,4-triazolo[3,4-b][1,3,4]thiadiazole
-
half-maximal inhibition at 0.023 mg/ml
1,3-benzodioxole-5-carbothioamide
-
the compound shows higher affinity for the shikimate binding site than for the NADP+ binding site, mixed full inhibition mechanism versus shikimate, non-competitive full inhibition mechanism versus NADP+, interaction analysis and enzyme-bound structure, overview. 75% inhibition at 0.4 mM
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
2,2-bisepigallocatechin gallate
about 50% inhibition at 0.0025 mM
2,4-Dichlorophenoxyacetic acid
-
-
2,5-dimethyl-1,4-phenylene bis(trifluoroacetate)
-
2-(3,4-dihydroxyphenyl)-3,4-dihydro-2H-1-benzopyran-3,5,7-triol
-
2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-4-oxo-4H-1-benzopyran-3-yl 6-deoxy-alpha-L-mannopyranoside
-
2-(3,4-dihydroxyphenyl)ethyl 6-O-[(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl]-beta-D-glucopyranoside
-
2-([2-([2-([2-(2,3-dimethylanilino)-2-oxoethyl]sulfanyl)-1,3-benzothiazol-6-yl]amino)2-oxoethyl]sulfanyl)-N-(2-naphthyl)acetamide
IC50: 0.0029 mM, competitive inhibition with respect to shikimate, noncompetitive to NADP+, potent antibacterial activity
2-[4-(trifluoromethyl)phenyl]-1,3-thiazole-4-carboxylic acid
2-[methyl[3-(trifluoromethyl)naphthalen-1-yl]amino]ethan-1-ol
3,3,3-trifluoro-N-(2-nitrophenyl)-2-(trifluoromethyl)propanamide
-
3,5,7-trihydroxy-3'-(4-hydroxy-3-methoxyphenyl)-2'-(hydroxymethyl)-2,3,3',4'-tetrahydro-2'H,4H-[2,6'-bi-1-benzopyran]-4-one
-
3,5-dihydroxy-4-methylbenzoic acid
-
3,5-Dihydroxybenzoate
-
moderate
3-(2-naphthyloxy)-4-oxo-2-(trifluoromethyl)-4H-chromen-7-yl 3-chlorobenzoate
IC50: 0.0039 mM, noncompetitive inhibition with respect to shikimate, competitive to NADP+
3-(3,4-dihydroxyphenyl)-2-[[(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl]oxy]propanoic acid
-
3-(3-fluoropyridin-4-yl)-6-(phenoxymethyl)-1,2,4-triazolo[3,4-b]-1,3,4-thiadiazole
-
-
3-(4-bromophenyl)-6-((2,4-dichlorophenoxy)methyl)-[1,2,4]-triazolo[3,4-b][1,3,4]thiadiazole
-
half-maximal inhibition at 0.0396 mg/ml
3-(4-bromophenyl)-6-((2-methyl-4-chlorophenoxy)methyl)-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazole
-
half-maximal inhibition at 0.0216 mg/ml
3-(4-bromophenyl)-6-((4-chlorophenoxy)methyl)-[1,2,4]triazolo-[3,4-b][1,3,4]thiadiazole
-
half-maximal inhibition at 0.0363 mg/ml
3-(4-bromophenyl)-6-((4-fluorophenoxy)methyl)-[1,2,4]triazolo-[3,4-b][1,3,4]thiadiazole
-
half-maximal inhibition at 0.0795 mg/ml
3-(4-bromophenyl)-6-((4-methoxyphenoxy)methyl)-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazole
-
half-maximal inhibition at 0.0120 mg/ml
3-(4-bromophenyl)-6-((4-nitrophenoxy)methyl)-[1,2,4]triazolo-[3,4-b][1,3,4]thiadiazole
-
half-maximal inhibition at 0.0586 mg/ml
3-(4-chlorophenyl)-6-((2-naphthyloxy)methyl)-[1,2,4]triazolo-[3,4-b][1,3,4]thiadiazole
-
half-maximal inhibition at 0.168 mg/ml
3-(4-chlorophenyl)-6-((4-fluorophenoxy)methyl)-[1,2,4]triazolo-[3,4-b][1,3,4]thiadiazole
-
half-maximal inhibition at 5.052 mg/ml
3-(4-chlorophenyl)-6-((4-nitrophenoxy)methyl)-[1,2,4]triazolo-[3,4-b][1,3,4]thiadiazole
-
half-maximal inhibition at 0.00937 mg/ml
3-(4-fluorophenyl)-6-((2-naphthyloxy)methyl)-[1,2,4]triazolo-[3,4-b][1,3,4]thiadiazole
-
-
3-(4-fluorophenyl)-6-((4-methoxyphenoxy)methyl)-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazole
-
half-maximal inhibition at 0.0663 mg/ml
3-(4-hydroxyphenyl)-4-oxo-4H-1-benzopyran-7-yl hexopyranosiduronic acid
-
3-(beta-naphthylmethyl)-6-((4-nitrophenoxy)methyl)-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazole
-
half-maximal inhibition at 0.0407 mg/ml
3-ethyl-3,4-dihydro-2H-1-benzopyran
3-hydroxy-4-(methoxycarbonyl)-2,5-dimethylphenyl 3-formyl-2,4-dihydroxy-6-methylbenzoate
-
3-[[(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl]oxy]-1,4,5-trihydroxycyclohexane-1-carboxylic acid
-
4,4'-methylenebis(2,6-dibromo-3,5-dihydroxybenzoic acid)
-
4-hydroxy-6-methyl-2-oxo-1-(2-phenylethyl)-1,2-dihydropyridine-3-carbaldehyde
-
4-[(morpholin-4-yl)methyl]benzoic acid
4-[[(E)-(2-ethoxy-6-methyl-4-oxo-2H-1-benzopyran-3(4H)-ylidene)methyl]amino]-2-hydroxybenzoic acid
-
5-(6-hydroxy-1-benzofuran-2-yl)-2-[(1E)-3-methylbut-1-en-1-yl]benzene-1,3-diol
-
5-(hex-1-yn-1-yl)furan-2-carboxylic acid
5-[4-(1H-imidazol-2-ylcarbonyl)phenyl]thiophene-2-carboxylic acid
-
the compound shows higher affinity for the shikimate binding site than for the NADP+ binding site, uncompetitive full inhibition versus shikimate and mixed full inhibition versus NADP+, interaction analysis and enzyme-bound structure, overview. 98% inhibition at 0.4 mM
5-[[5-(4-chlorophenyl)furan-2-yl]methylidene]-2,2-dimethyl-1,3-dioxane-4,6-dione
-
6-((2,4-dichlorophenoxy)methyl)-3-(3-fluoropyridin-4-yl)-[1,2,4]-triazolo[3,4-b][1,3,4]thiadiazole
-
-
6-((4-bromophenoxy)methyl)-3-(4-bromophenyl)-[1,2,4]triazolo-[3,4-b][1,3,4]thiadiazole
-
half-maximal inhibition at 0.0144 mg/ml
6-((4-bromophenoxy)methyl)-3-(4-chlorophenyl)-[1,2,4]triazolo-[3,4-b][1,3,4]thiadiazole
-
half-maximal inhibition at 0.00682 mg/ml
6-((4-fluorophenoxy)methyl)-3-(beta-naphthylmethyl)-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazole
-
half-maximal inhibition at 0.0277 mg/ml
6-(2,6-dichlorophenoxy) pyridin-3-amine
-
60% inhibition at 0.4 mM
6-amino-1,2,3,4-tetrahydronaphthalen-1-one
-
the compound presents a higher affinity for NADP+ binding site than for shikimate binding, mixed partial inhibition mechanism versus NADP+ and mixed full versus shikimate, interaction analysis and enzyme-bound structure, overview. 91% inhibition at 0.4 m
6-hydroxy-1-benzofuran-3(2H)-one
-
-
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
6-hydroxy-7-methyl-1-benzofuran-3(2H)-one
-
mixed partial inhibition mechanism versus NADP+ and shikimate, interaction analysis and enzyme bound structure, overview. 98% inhibition at 0.4 mM
7-hydroxy-2,2,8-trimethyl-2,3-dihydro-4H-1-benzopyran-4-one
-
-
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
ajmalicine
-
(19alpha)-16,17-didehydro-19-methyloxayohimban-16-carboxylic acid methyl ester, from Rauwolfia serpentina leaves and roots, interacting residues are Asp131 and Arg130
aurintricarboxylic acid
lower inhibitry potency, about 25% inhibition at 0.0025 mM
baicalein
about 25% inhibition at 0.0025 mM
butyl 2-([3-(2-naphthyloxy)4-oxo-2-(trifluoromethyl)4H-chromen-7-yl]oxy)propanoate
IC50: 0.0134 mM, noncompetitive inhibition with respect to shikimate, competitive to NADP+, potent antibacterial activity
cardiolipin
lower inhibitry potency, about 25% inhibition at 0.0025 mM
cyclopropyl(5-hydroxy-1-benzofuran-3-yl)methanone
-
32% inhibition at 0.4 mM
dianthrol
about 50% inhibition at 0.0025 mM
-
diethylenetriamine pentaacetic acid
lower inhibitry potency, about 25% inhibition at 0.0025 mM
ebselen
lower inhibitry potency, about 25% inhibition at 0.0025 mM
ellagic acid
about 50% inhibition at 0.0025 mM
epigallocatechin-3,5-digallate
about 50% inhibition at 0.0025 mM
epitheaflavin monogallate
about 50% inhibition at 0.0025 mM
ethyl 5-(1H-pyrazol-3-yl)thiophene-2-carboxylate
-
28% inhibition at 0.4 mM
HgCl2
-
complete inhibition at concentration 0.05 mM
hydroquinone
lower inhibitry potency, about 25% inhibition at 0.0025 mM
limonin
-
7,16-dioxo-7,16-dideoxylimondiol, from Citrus sp. fruits, interacting residues are Thr75, Thr78, Val71, Gln101, and Pro103
maesaquinone diacetate
IC50: 0.0035 mM, noncompetitive inhibition with respect to shikimate and NADP+
merbromin
lower inhibitry potency, about 25% inhibition at 0.0025 mM
methyl 3-hydroxy-1-benzothiophene-2-carboxylate
N-methyl-N-(quinolin-6-ylmethyl)amine
-
63% inhibition at 0.4 mM
N-[2,2-dimethyl-6-(1-methyldioxidan-1-ium-1-yl)-3,4-dihydro-2H-1-benzopyran-4-yl]-N2-methyl-N2-[(pyridin-2-yl)methyl]glycinamide
-
34% inhibition at 0.4 mM
NADP+
product inhibition, competitive versus NADPH, noncompetitive versus 3-dehydroshikimate
nordihydroguaiaretic acid
lower inhibitry potency, about 25% inhibition at 0.0025 mM
p-hydroxymercuribenzoate
-
moderate
purpurogallin
about 50% inhibition at 0.0025 mM
pyridoxine
lower inhibitry potency, about 25% inhibition at 0.0025 mM
pyrogallin
about 50% inhibition at 0.0025 mM
quercetin
about 25% inhibition at 0.0025 mM
SDS
-
nearly complete inactivation of AroE at 0.02%
strictamin
-
akuammilan-17-oic acid methyl ester, from Alstonia scholaris leaves, interacting residues are Tyr129, Gln126, and Leu125
taxifolin
about 25% inhibition at 0.0025 mM
theaflavanin
about 25% inhibition at 0.0025 mM
theaflavin monogallate
about 50% inhibition at 0.0025 mM
theaflavin-3,3-digallate
about 25% inhibition at 0.0025 mM
[2,2'-bithiophene]-5-carboxylic acid
-
-
[2-[2-(dimethylamino)ethoxy]phenyl]methanol
[4-(4-methylperhydro-1,4-diazepin-1-yl)phenyl]methanol
-
67% inhibition at 0.4 mM
2-[4-(trifluoromethyl)phenyl]-1,3-thiazole-4-carboxylic acid

-
31% inhibition at 0.2 mM
2-[4-(trifluoromethyl)phenyl]-1,3-thiazole-4-carboxylic acid
-
31% inhibition at 0.2 mM
2-[methyl[3-(trifluoromethyl)naphthalen-1-yl]amino]ethan-1-ol

-
49% inhibition at 0.2 mM
2-[methyl[3-(trifluoromethyl)naphthalen-1-yl]amino]ethan-1-ol
-
49% inhibition at 0.2 mM
3-ethyl-3,4-dihydro-2H-1-benzopyran

-
31% inhibition at 0.2 mM
3-ethyl-3,4-dihydro-2H-1-benzopyran
-
31% inhibition at 0.2 mM
4-[(morpholin-4-yl)methyl]benzoic acid

-
31% inhibition at 0.2 mM
4-[(morpholin-4-yl)methyl]benzoic acid
-
31% inhibition at 0.2 mM
5-(hex-1-yn-1-yl)furan-2-carboxylic acid

-
29% inhibition at 0.2 mM
5-(hex-1-yn-1-yl)furan-2-carboxylic acid
-
29% inhibition at 0.2 mM
Cu2+

-
-
curcumin

IC50: 0.0154 mM, noncompetitive inhibition with respect to shikimate and NADP+
curcumin
-
a noncompetitive inhibitor
epicatechin gallate

inhibits the AroE domain of the bifunctional dehydroquinate dehydratase-shikimate dehydrogenase (DHQ-SDH) from Arabidopsis thaliana
epicatechin gallate
over 75% inhibition at 0.0025 mM
epigallocatechin gallate

inhibits the AroE domain of the bifunctional dehydroquinate dehydratase-shikimate dehydrogenase (DHQ-SDH) from Arabidopsis thaliana
epigallocatechin gallate
over 75% inhibition at 0.0025 mM
epigallocatechin gallate
-
-
Hg2+

-
-
iodoacetate

-
-
methyl 3-hydroxy-1-benzothiophene-2-carboxylate

-
33% inhibition at 0.2 mM
methyl 3-hydroxy-1-benzothiophene-2-carboxylate
-
33% inhibition at 0.2 mM
p-chloromercuribenzoate

-
-
p-chloromercuribenzoate
-
biphasic inhibition: first rapid inhibition leading to loss of 70% activity, then within 5 min loss of the remaining 30% activity, inhibition can be partially hindered by thiols and chloride
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
protocatechuic acid

-
competitive inhibition
protocatechuic acid
-
moderate
shikimate

shikimate synthesis decreases with increasing shikimate concentration. The relative activity halves at about 1.4 mM shikimate; shikimate synthesis decreases with increasing shikimate concentration. The relative activity halves at about 1.4 mM shikimate
shikimate
product inhibition, noncompetitive versus NADPH, competitive versus 3-dehydroshikimate
Zn2+

-
-
[2-[2-(dimethylamino)ethoxy]phenyl]methanol

-
45% inhibition at 0.2 mM
[2-[2-(dimethylamino)ethoxy]phenyl]methanol
-
45% inhibition at 0.2 mM
additional information

-
ten clinical isolates of Acinetobacter baumannii are used for inhibitor screening. Ajmalicine, strictamin, and limonin exhibit promising binding towards multiple drug targets of Acinetobacter baumannii in comparison with the binding between standard drugs and their targets. The tested isolates exhibit resistance to antibiotics clinafloxacin, imipenem and polymyxin-E, and the herbal preparations (crude extracts) demonstrate a significant antibacterial potential. Docking study and molecular dynamic simulations, model refinement and validation, overview. Acinetobacter baumannii exhibits resistance to a broad range of antibiotics due to the presence of a protective capsule, lipopolysaccharide, AbaR resistance islands, OmpA, efflux pumps, biofilms formation, and other mechanisms. Evaluation of drug targets in Acinetobacter baumannii. The toxicity prediction for ajmalicine (Rauvolfia serpentina) and strictamin (Alstonia scholaris) are predicted to be non-carcinogenic in both mouse and rat models making them potential leads
-
additional information
screening for polyphenolc enzyme inhibitors, overview
-
additional information
-
screening for polyphenolc enzyme inhibitors, overview
-
additional information
not inhibitory: quinate; not inhibitory: quinate
-
additional information
not inhibitory: quinate; not inhibitory: quinate
-
additional information
-
not inhibitory: quinate; not inhibitory: quinate
-
additional information
synthesis, biological activity and molecular modelling studies of shikimic acid derivatives as inhibitors of the shikimate dehydrogenase enzyme of Escherichia coli, evaluation for in vitro SDH inhibition and antibacterial activity against Escherichia coli, molecular docking studies, overview. All tested compounds are mixed-type inhibitors, diamide derivatives display more inhibitory activity than synthesised monoamides
-
additional information
-
synthesis, biological activity and molecular modelling studies of shikimic acid derivatives as inhibitors of the shikimate dehydrogenase enzyme of Escherichia coli, evaluation for in vitro SDH inhibition and antibacterial activity against Escherichia coli, molecular docking studies, overview. All tested compounds are mixed-type inhibitors, diamide derivatives display more inhibitory activity than synthesised monoamides
-
additional information
-
no inhibition of paralogue HI0607 by EDTA
-
additional information
antibacterial activity of inhibitors, overview
-
additional information
-
antibacterial activity of inhibitors, overview
-
additional information
-
inhibitor screening
-
additional information
integrated virtual screening/molecular docking-based virtual screening, and antibacterial test for identification of enzyme inhibitors, screening of ZINC database. The HpSDH active site prefers to accommodate amphipathic and polar inhibitors that consist of an aromatic core as well as a number of oxygen-rich polar/charged substituents such as hydroxyl, carbonyl, and carboxyl groups. Subpockets 1- and 2-specific inhibitors exhibit a generally higher activity than subpocket 3-specific inhibitors. Molecular dynamics simulations revealed an intense nonbonded network of hydrogen bonds, Pi-Pi stacking, and van der Waals contacts at the tightly packed complex interfaces of active-site subpockets with their cognate inhibitors, conferring strong stability and specificity to these complex systems. Binding energetic analysis demonstrates that the identified potent inhibitors can target their cognate subpockets with an effective selectivity over noncognate ones. Determination of MIC values of the compounds against Helicobacter strains ATCC43504 and ATCC700392, and structural and energetic analysis of subpocket-inhibitor interactions, overview
-
additional information
-
integrated virtual screening/molecular docking-based virtual screening, and antibacterial test for identification of enzyme inhibitors, screening of ZINC database. The HpSDH active site prefers to accommodate amphipathic and polar inhibitors that consist of an aromatic core as well as a number of oxygen-rich polar/charged substituents such as hydroxyl, carbonyl, and carboxyl groups. Subpockets 1- and 2-specific inhibitors exhibit a generally higher activity than subpocket 3-specific inhibitors. Molecular dynamics simulations revealed an intense nonbonded network of hydrogen bonds, Pi-Pi stacking, and van der Waals contacts at the tightly packed complex interfaces of active-site subpockets with their cognate inhibitors, conferring strong stability and specificity to these complex systems. Binding energetic analysis demonstrates that the identified potent inhibitors can target their cognate subpockets with an effective selectivity over noncognate ones. Determination of MIC values of the compounds against Helicobacter strains ATCC43504 and ATCC700392, and structural and energetic analysis of subpocket-inhibitor interactions, overview
-
additional information
-
structure-activity relationship studies on 1,2,4-triazolo[3,4-b][1,3,4]thiadiazoles as inhibitors of shikimate dehydrogenase, 3,6-disubstituted triazolothiadiazoles synthesis, overview. The compounds exhibit cytotoxicity against Vero and Hep-G2 cellss, IC50 and MIC values
-
additional information
simulations of shikimate dehydrogenase from Mycobacterium tuberculosis in complex with 3-dehydroshikimate and NADPH for MtbSDH inhibition strategy, overview. Rational design of hybrid MtbSDH inhibitors able to bind in both the substrate (DHS) and cofactor (NADPH) pockets
-
additional information
-
simulations of shikimate dehydrogenase from Mycobacterium tuberculosis in complex with 3-dehydroshikimate and NADPH for MtbSDH inhibition strategy, overview. Rational design of hybrid MtbSDH inhibitors able to bind in both the substrate (DHS) and cofactor (NADPH) pockets
-
additional information
screening for polyphenolc enzyme inhibitors, overview. No inhibition by gallic acid, epigallocatechin and epicatechin
-
additional information
-
screening for polyphenolc enzyme inhibitors, overview. No inhibition by gallic acid, epigallocatechin and epicatechin
-
additional information
-
structure-based inhibitor design, small-molecule library screening, inhibition mechanism analysis
-
additional information
-
no inhibition by curcumin
-
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0.00036 - 0.42
3-dehydroquinate
0.029 - 186
3-dehydroshikimate
0.05 - 0.087
shikimic acid
additional information
additional information
-
0.00036
3-dehydroquinate

pH 7.0, 30°C
0.42
3-dehydroquinate
pH 7.0, 30°C
0.029
3-dehydroshikimate

-
-
0.029
3-dehydroshikimate
wild-type enzyme, pH 7.3, 25°C
0.031
3-dehydroshikimate
pH 7.0, 25°C, recombinant AroE
0.031
3-dehydroshikimate
-
pH 7.0, 25°C, with NADPH
0.044
3-dehydroshikimate
25°C, pH 7.3
0.046
3-dehydroshikimate
pH 7.0, 30°C, recombinant isozyme VvSDH3
0.076
3-dehydroshikimate
mutant K69A, pH 7.3, 25°C
0.157
3-dehydroshikimate
pH 7.0, 30°C, recombinant isozyme VvSDH1
0.2
3-dehydroshikimate
pH 7.0, 30°C
0.272
3-dehydroshikimate
pH 9.0, 30°C
0.272
3-dehydroshikimate
with NADPH, pH 8.6, 30°C
0.287
3-dehydroshikimate
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHa, with NADPH
0.322
3-dehydroshikimate
pH 7.0, 30°C, EcDQD/SDH2, DQD activity
0.331
3-dehydroshikimate
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHc, with NADPH
0.381
3-dehydroshikimate
pH 6.5, 30°C, EcDQD/SDH1, shikimate formation
0.449
3-dehydroshikimate
pH 7.0, 30°C, EcDQD/SDH1, DQD activity
0.466
3-dehydroshikimate
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHd, with NADPH
0.878
3-dehydroshikimate
pH 6.5, 30°C, EcDQD/SDH3, shikimate formation
0.882
3-dehydroshikimate
pH 7.0, 30°C, EcDQD/SDH3, DQD activity
8.83
3-dehydroshikimate
pH 8.5, 30°C, EcDQD/SDH2, shikimate formation
9.44
3-dehydroshikimate
pH 10.5, 30°C, EcDQD/SDH2, gallate formation
30.6
3-dehydroshikimate
pH 10.5, 30°C, EcDQD/SDH2, gallate formation
186
3-dehydroshikimate
pH 7.0, 30°C, recombinant isozyme VvSDH4
2.351
L-quinate

-
mutant S275G/T318G, pH and temperature not specified in the publication
3.33
L-quinate
pH and temperature not specified in the publication, mutant T381G
4.075
L-quinate
pH and temperature not specified in the publication, mutant S338G/T381G
4.485
L-quinate
pH and temperature not specified in the publication, mutant T381S
5.135
L-quinate
pH and temperature not specified in the publication, mutant T381A
0.572
NAD+

pH 8.8, presence of 2 mM shikimate
1.083
NAD+
pH 8.8, presence of 2 mM quinate
2.9
NAD+
pH 8.0, 60°C, recombinant enzyme
5.4
NAD+
pH 8.8, presence of 2 mM shikimate
5.43
NAD+
pH 8.8, presence of 2 mM shikimate
5.43
NAD+
in the presence of shikimate
11.4
NAD+
-
87°C, pH 7.3
0.007
NADP+

-
-
0.0073
NADP+
pH 8.8, presence of 2 mM shikimate
0.0091
NADP+
-
pH 8.8, temperature not specified in the publication
0.0091
NADP+
pH 8.8, 25°C, with shikimate
0.0135
NADP+
with shikimate, pH 7.0, 25°C
0.017
NADP+
-
pH 7.5, 22°C, mutant K385A
0.022
NADP+
pH 7.0, 25°C, recombinant AroE
0.022
NADP+
-
pH 7.5, 22°C, mutant K385N/D423N
0.022
NADP+
-
pH 7.0, 25°C, with shikimate
0.023
NADP+
pH 7.0, 30°C, recombinant isozyme VvSDH3
0.0295
NADP+
-
pH 9.0, 25°C
0.031
NADP+
22°C, pH 9.0
0.038
NADP+
pH 9.0, 30°C, recombinant isozyme VvSDH3
0.0415
NADP+
pH 9.0, 30°C, EcDQD/SDH3, shikimate oxidation
0.0424
NADP+
25°C, pH 9.0
0.0424
NADP+
with shikimate, pH 9.0, 25°C
0.04255
NADP+
-
pH not specified in the publication, 25°C
0.0426
NADP+
-
pH not specified in the publication, 25°C, with shikimate
0.046
NADP+
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHD, with shikimate
0.053
NADP+
-
pH 7.5, 22°C, mutant K385N
0.0538
NADP+
pH 9.0, 30°C, recombinant isozyme VvSDH4
0.055
NADP+
pH 8.8, 25°C, with shikimate
0.056
NADP+
-
with shikimate, pH 9.0, 20°C
0.0565
NADP+
pH 9.0, 30°C, EcDQD/SDH1, shikimate oxidation
0.062
NADP+
-
mutant T381S, 22°C
0.063
NADP+
-
pH 9.0, 25°C, with shikimate
0.0652
NADP+
pH 9.0, 30°C, EcDQD/SDH2, shikimate oxidation
0.068
NADP+
-
mutant H335A, 22°C
0.079
NADP+
-
pH 7.5, 22°C, mutant D423N
0.0928
NADP+
-
mutant T381A, 22°C
0.1
NADP+
pH 7.0, 25°C, with shikimate
0.107
NADP+
-
mutant T422S, 22°C
0.112
NADP+
pH 8.8, presence of 2 mM shikimate
0.112
NADP+
in the presence of shikimate
0.114
NADP+
-
pH 7.5, 22°C, mutant S338A
0.114
NADP+
pH 9.0, 30°C, recombinant isozyme VvSDH1
0.115
NADP+
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHc, with shikimate
0.131
NADP+
-
pH 7.5, 22°C, wild-type DELTA88DHQ-SDH enzyme variant
0.131
NADP+
-
wild-type, 22°C
0.131
NADP+
pH 8.8, 22°C, with shikimate
0.132
NADP+
-
pH 7.5, 22°C, mutant Y550F
0.138
NADP+
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHa, with shikimate
0.152
NADP+
-
pH 7.5, 22°C, mutant S336A
0.156
NADP+
-
mutant T407A, 22°C
0.157
NADP+
-
pH 7.5, 22°C, mutant Y550A
0.159
NADP+
-
mutant Q78L, 22°C
0.182
NADP+
pH 8.0, 60°C, recombinant enzyme
0.182
NADP+
-
with shikimate, pH 8.0, 25°C
0.19
NADP+
-
87°C, pH 7.3
0.19
NADP+
with shikimate, pH 7.3, 87°C
0.217
NADP+
pH 7.0, 30°C, recombinant isozyme VvSDH1
0.00438
NADPH

pH 8.5, 30°C, EcDQD/SDH2, shikimate formation
0.01
NADPH
pH 7.0, 25°C, recombinant AroE
0.011
NADPH
wild-type enzyme, pH 7.3, 25°C
0.0231
NADPH
pH 6.5, 30°C, EcDQD/SDH3, shikimate formation
0.03
NADPH
mutant K69A, pH 7.3, 25°C
0.031
NADPH
-
pH 7.0, 25°C, with 3-dehydroshikimate
0.034
NADPH
25°C, pH 7.3
0.0495
NADPH
pH 6.5, 30°C, EcDQD/SDH1, shikimate formation
0.249
NADPH
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHD, with 3-dehydroshikimate
0.267
NADPH
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHc, with 3-dehydroshikimate
0.27
NADPH
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHa, with 3-dehydroshikimate
0.783
quinate

pH 8.8, presence of 2 mM NAD+
10.2
quinate
pH 9.0, 30°C
0.0046
shikimate

pH 8.8, presence of 2 mM NADP+
0.027
shikimate
pH 9.0, 30°C, recombinant isozyme VvSDH3
0.03
shikimate
-
pH 9.0, 25°C, with NADP+
0.0326
shikimate
pH 9.0, 30°C, EcDQD/SDH1, shikimate oxidation
0.03746
shikimate
-
pH not specified in the publication, 25°C
0.0375
shikimate
-
pH not specified in the publication, 25°C, with NADP+
0.0424
shikimate
25°C, pH 9.0
0.0425
shikimate
with NADP+, pH 9.0, 25°C
0.05
shikimate
pH 7.0, 25°C, recombinant AroE
0.0502
shikimate
-
pH 7.0, 25°C, with NADP+
0.0527
shikimate
-
pH 8.8, temperature not specified in the publication
0.0527
shikimate
pH 8.8, 25°C, with NADP+
0.063
shikimate
-
pH 9.0, 25°C
0.065
shikimate
-
with NADP+, pH 9.0, 20°C
0.07
shikimate
pH 9.0, 30°C, recombinant isozyme VvSDH1
0.073
shikimate
wild-type
0.073
shikimate
pH 7.0, 25°C, with NADP+
0.0786
shikimate
pH 8.8, presence of 2 mM NAD+
0.0786
shikimate
in the presence of 2 mM NAD+
0.101
shikimate
-
pH and temperature not specified in the publication
0.105
shikimate
pH 8.8, presence of 2 mM NADP+
0.105
shikimate
in the presence of 2 mM NADP+
0.12
shikimate
-
pH and temperature not specified in the publication
0.13
shikimate
pH 9.0, 25°C, recombinant wild-type enzyme
0.13
shikimate
22°C, pH 9.0
0.131
shikimate
-
pH 7.5, 22°C, mutant K385N/D423N
0.14
shikimate
pH 9.0, 30°C
0.14
shikimate
with NADP+, pH 9.0, 30°C
0.1468
shikimate
pH 9.0, 30°C, recombinant isozyme VvSDH4
0.148
shikimate
pH 8.0, 60°C, recombinant enzyme
0.148
shikimate
-
with NADP+, pH 8.0, 25°C
0.155
shikimate
pH 7.0, 30°C, recombinant isozyme VvSDH1
0.17
shikimate
-
87°C, pH 7.3
0.17
shikimate
with NADP+, pH 7.3, 87°C
0.178
shikimate
pH 8.8, 25°C, with NADP+
0.187
shikimate
pH 7.0, 30°C
0.19 - 0.28
shikimate
-
-
0.2
shikimate
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHc, with NADP+
0.218
shikimate
-
pH and temperature not specified in the publication
0.22
shikimate
-
2 KM-values
0.223
shikimate
-
pH 8.5, 22°C, with NADP+, isozyme Poptr1
0.223
shikimate
-
with NADP+, pH 8.5, 22°C, recombinant His-tagged Poptr1
0.227
shikimate
mutant Y211F
0.239
shikimate
-
pH and temperature not specified in the publication
0.263
shikimate
-
pH 7.5, 22°C, mutant K385A
0.273
shikimate
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHa, with NADP+
0.279
shikimate
-
pH and temperature not specified in the publication
0.311
shikimate
with NADP+, pH 7.0, 25°C
0.321
shikimate
-
with NADP+, pH 8.5, 22°C, recombinant His-tagged Poptr1
0.346
shikimate
-
pH 8.5, 22°C, with NADP+, isozyme Poptr5
0.346
shikimate
-
with NAD+, pH 8.5, 22°C, recombinant His-tagged Poptr1
0.351
shikimate
pH 8.8, presence of 2 mM NAD+
0.422
shikimate
pH 7.0, 30°C, recombinant isozyme VvSDH3
0.427
shikimate
-
with NAD+, pH 8.5, 22°C, recombinant His-tagged Poptr1
0.459
shikimate
-
mutant T381S, 22°C
0.47
shikimate
-
pH 7.5, 22°C, mutant K385N
0.548
shikimate
pH and temperature not specified in the publication, mutant S338G
0.555
shikimate
-
pH 7.5, 22°C, mutant D423N
0.556
shikimate
-
mutant T381A, 22°C
0.604
shikimate
pH and temperature not specified in the publication, wild-type enzyme
0.611
shikimate
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHD, with NADP+
0.626
shikimate
-
mutant H335A, 22°C
0.685
shikimate
-
pH 7.5, 22°C, wild-type DELTA88DHQ-SDH enzyme variant
0.685
shikimate
-
wild-type, 22°C
0.685
shikimate
pH 8.8, 22°C, with NADP+
0.882
shikimate
pH and temperature not specified in the publication, mutant S338G/T381G
0.91
shikimate
-
2 KM-values
0.92
shikimate
-
mutant Q78L, 22°C
1.022
shikimate
-
mutant T407A, 22°C
1.03
shikimate
-
pH 7.5, 22°C, mutant Y550A
1.06
shikimate
-
pH 7.5, 22°C, mutant Y550F
1.09
shikimate
-
mutant T422S, 22°C
1.539
shikimate
pH and temperature not specified in the publication, mutant T381S
1.613
shikimate
pH and temperature not specified in the publication, mutant T381G
2.05
shikimate
pH 9.0, 30°C, EcDQD/SDH2, shikimate oxidation
2.512
shikimate
pH and temperature not specified in the publication, mutant T381A
3.64
shikimate
pH 9.0, 30°C, EcDQD/SDH3, shikimate oxidation
4.2
shikimate
pH 8.8, presence of 2 mM NAD+
4.466
shikimate
-
mutant Q582L, 22°C
6.2
shikimate
-
pH 7.5, 22°C, mutant S338A
7.12
shikimate
-
mutant N406A, 22°C
8.74
shikimate
-
pH 7.5, 22°C, mutant S336A
46.6
shikimate
pH 10.0, 30°C
0.05
shikimic acid

-
NADP+
0.087
shikimic acid
-
NADP+
additional information
additional information

-
-
-
additional information
additional information
-
-
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additional information
additional information
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Michaelis-Menten kinetics
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additional information
additional information
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Michaelis-Menten kinetics
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additional information
additional information
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Michaelis-Menten kinetics
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additional information
additional information
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Michaelis-Menten kinetics
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additional information
additional information
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Michaelis-Menten kinetics
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additional information
additional information
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Michaelis-Menten kinetics
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additional information
additional information
Michaelis-Menten kinetics
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additional information
additional information
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Michaelis-Menten kinetics
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additional information
additional information
Michaelis-Menten kinetics
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additional information
additional information
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Michaelis-Menten kinetics
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additional information
additional information
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Michaelis-Menten kinetics
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additional information
additional information
Michaelis-Menten kinetics
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additional information
additional information
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Michaelis-Menten kinetics
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additional information
additional information
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kinetic profile of the recombinant AroE, overview
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additional information
additional information
steady-state kinetics of recombinant AroE
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additional information
additional information
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steady-state kinetics of recombinant AroE
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additional information
additional information
no measurable activity with NAD+
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additional information
additional information
no measurable activity with NAD+
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additional information
additional information
no measurable activity with NAD+
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additional information
additional information
no measurable activity with NAD+
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additional information
additional information
no measurable activity with NAD+
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additional information
additional information
no measurable activity with NADH+
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additional information
additional information
no measurable activity with NADH+
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additional information
additional information
no measurable activity with NADH+
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additional information
additional information
no measurable activity with NADH+
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additional information
additional information
no measurable activity with NADH+
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additional information
additional information
no measurable activity with quinate
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additional information
additional information
no measurable activity with quinate
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additional information
additional information
no measurable activity with quinate
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additional information
additional information
no measurable activity with quinate
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additional information
additional information
no measurable activity with quinate
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additional information
additional information
no measurable activity with shikimate
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additional information
additional information
no measurable activity with shikimate
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additional information
additional information
no measurable activity with shikimate
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additional information
additional information
no measurable activity with shikimate
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additional information
additional information
no measurable activity with shikimate
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additional information
additional information
steady-state kinetics of wild-type and mutant enzymes, overview
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additional information
additional information
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steady-state kinetics of wild-type and mutant enzymes, overview
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additional information
additional information
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the enzyme shows Michaelis-Menten kinetics toward both substrates shikimate and NADP+, kinetic analysis, sequential random mechanism, overview
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