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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+
-
-
-
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(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, temperature not specified in the publication
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, temperature not specified in the publication
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, temperature not specified in the publication
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
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
0.038
NADP+
pH 9.0, 30°C, recombinant isozyme VvSDH3
0.0415
NADP+
pH 9.0, temperature not specified in the publication
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, temperature not specified in the publication
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, temperature not specified in the publication
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, temperature not specified in the publication
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
0.0495
NADPH
pH 6.5, temperature not specified in the publication
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
23.1
NADPH
pH 6.5, temperature not specified in the publication
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, temperature not specified in the publication
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, temperature not specified in the publication
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, temperature not specified in the publication
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
-
-
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
kinetic profile of the recombinant AroE, overview
-
additional information
additional information
steady-state kinetics of recombinant AroE
-
additional information
additional information
-
steady-state kinetics of recombinant AroE
-
additional information
additional information
no measurable activity with NAD+
-
additional information
additional information
no measurable activity with NAD+
-
additional information
additional information
no measurable activity with NAD+
-
additional information
additional information
no measurable activity with NAD+
-
additional information
additional information
no measurable activity with NAD+
-
additional information
additional information
no measurable activity with NADH+
-
additional information
additional information
no measurable activity with NADH+
-
additional information
additional information
no measurable activity with NADH+
-
additional information
additional information
no measurable activity with NADH+
-
additional information
additional information
no measurable activity with NADH+
-
additional information
additional information
no measurable activity with quinate
-
additional information
additional information
no measurable activity with quinate
-
additional information
additional information
no measurable activity with quinate
-
additional information
additional information
no measurable activity with quinate
-
additional information
additional information
no measurable activity with quinate
-
additional information
additional information
no measurable activity with shikimate
-
additional information
additional information
no measurable activity with shikimate
-
additional information
additional information
no measurable activity with shikimate
-
additional information
additional information
no measurable activity with shikimate
-
additional information
additional information
no measurable activity with shikimate
-
additional information
additional information
steady-state kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
-
steady-state kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
-
the enzyme shows Michaelis-Menten kinetics toward both substrates shikimate and NADP+, kinetic analysis, sequential random mechanism, overview
-
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0.36 - 114
3-dehydroquinate
0.046 - 329
3-dehydroshikimate
additional information
additional information
-
0.36
3-dehydroquinate
pH 7.0, 30°C
114
3-dehydroquinate
pH 7.0, 30°C
0.046
3-dehydroshikimate
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHd, with NADPH
0.078
3-dehydroshikimate
25°C, pH 7.3
0.168
3-dehydroshikimate
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHc, with NADPH
0.405
3-dehydroshikimate
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHa, with NADPH
0.73
3-dehydroshikimate
mutant K69A, pH 7.3, 25°C
2.14
3-dehydroshikimate
pH 10.5, 30°C, EcDQD/SDH2, gallate formation
2.87
3-dehydroshikimate
pH 10.5, 30°C, EcDQD/SDH2, gallate formation
3.67
3-dehydroshikimate
pH 7.0, 30°C, EcDQD/SDH1, DQD activity
8.62
3-dehydroshikimate
pH 7.0, 30°C, recombinant isozyme VvSDH3
30.9
3-dehydroshikimate
pH 7.0, 30°C, EcDQD/SDH1, DQD activity
47
3-dehydroshikimate
pH 8.5, temperature not specified in the publication
47
3-dehydroshikimate
pH 8.5, 30°C, EcDQD/SDH1, shikimate formation
49
3-dehydroshikimate
pH 7.0, 25°C, recombinant AroE
49
3-dehydroshikimate
-
pH 7.0, 25°C, with NADPH
50
3-dehydroshikimate
wild-type enzyme, pH 7.3, 25°C
57.6
3-dehydroshikimate
pH 6.5, temperature not specified in the publication
57.6
3-dehydroshikimate
pH 6.5, 30°C, EcDQD/SDH1, shikimate formation
60.4
3-dehydroshikimate
pH 7.0, 30°C, EcDQD/SDH1, DQD activity
95.85
3-dehydroshikimate
pH 7.0, 30°C, recombinant isozyme VvSDH1
118
3-dehydroshikimate
pH 9.0, 30°C
118
3-dehydroshikimate
with NADPH, pH 8.6, 30°C
307
3-dehydroshikimate
pH 6.5, temperature not specified in the publication
307
3-dehydroshikimate
pH 6.5, 30°C, EcDQD/SDH1, shikimate formation
329
3-dehydroshikimate
pH 7.0, 30°C
0.062
L-quinate
pH and temperature not specified in the publication, mutant T381S
0.113
L-quinate
pH and temperature not specified in the publication, mutant T381A
6.7
L-quinate
pH and temperature not specified in the publication, mutant S338G/T381G
8.8
L-quinate
pH and temperature not specified in the publication, mutant T381G
5.2
NAD+
pH 8.0, 60°C, recombinant enzyme
6.72
NAD+
pH 8.8, presence of 2 mM shikimate
6.72
NAD+
in the presence of shikimate
40.7
NAD+
pH 8.8, presence of 2 mM quinate
61.1
NAD+
pH 8.8, presence of 2 mM shikimate
97.1
NAD+
pH 8.8, presence of 2 mM shikimate
97.1
NAD+
in the presence of shikimate
0.006
NADP+
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHD, with shikimate
0.008
NADP+
-
pH 7.5, 22°C, mutant K385A
0.036
NADP+
-
pH 7.5, 22°C, mutant K385N/D423N
0.043
NADP+
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHc, with shikimate
0.066
NADP+
-
pH 7.5, 22°C, mutant K385N
0.077
NADP+
in the presence of quinate
0.092
NADP+
-
pH 7.5, 22°C, mutant D423N
0.117
NADP+
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHa, with shikimate
1.86
NADP+
-
pH 7.5, 22°C, mutant Y550A
2.77
NADP+
pH 8.8, 25°C, with shikimate
3.11
NADP+
-
pH 7.5, 22°C, mutant Y550F
4.51
NADP+
-
mutant Q78L, 22°C
5.3
NADP+
pH 8.8, presence of 2 mM shikimate
5.3
NADP+
in the presence of shikimate
5.9
NADP+
pH 7.0, 25°C, recombinant AroE
5.9
NADP+
-
pH 7.0, 25°C, with shikimate
7.1
NADP+
pH 8.0, 60°C, recombinant enzyme
7.1
NADP+
-
with shikimate, pH 8.0, 25°C
11.2
NADP+
-
pH 7.5, 22°C, mutant S338A
15.1
NADP+
-
mutant T381A, 22°C
19.78
NADP+
pH 7.0, 30°C, recombinant isozyme VvSDH3
22.8
NADP+
pH 7.0, 25°C, with shikimate
26.11
NADP+
pH 9.0, 30°C, recombinant isozyme VvSDH3
28.89
NADP+
pH 9.0, 30°C, recombinant isozyme VvSDH4
30.7
NADP+
pH 7.0, 30°C, recombinant isozyme VvSDH1
34
NADP+
-
mutant H335A, 22°C
43.3
NADP+
-
mutant T422S, 22°C
52.1
NADP+
-
mutant T407A, 22°C
52.9
NADP+
-
pH 7.5, 22°C, mutant S336A
55.5
NADP+
with shikimate, pH 9.0, 25°C
70.2
NADP+
pH 9.0, temperature not specified in the publication
70.2
NADP+
pH 9.0, 30°C, EcDQD/SDH1, shikimate oxidation
105
NADP+
-
mutant T381S, 22°C
135
NADP+
pH 9.0, temperature not specified in the publication
135
NADP+
pH 9.0, 30°C, EcDQD/SDH1, shikimate oxidation
146.2
NADP+
-
pH not specified in the publication, 25°C
146.2
NADP+
-
pH not specified in the publication, 25°C, with shikimate
237
NADP+
-
with shikimate, pH 9.0, 20°C
239
NADP+
pH 9.0, 30°C, recombinant isozyme VvSDH1
261.5
NADP+
pH 8.8, presence of 2 mM shikimate
261.5
NADP+
in the presence of shikimate
302
NADP+
pH 8.8, 25°C, with shikimate
390
NADP+
with shikimate, pH 7.3, 87°C
399
NADP+
-
pH 7.5, 22°C, wild-type DELTA88DHQ-SDH enzyme variant
399
NADP+
-
wild-type, 22°C
399
NADP+
pH 8.8, 22°C, with shikimate
399
NADP+
-
pH 9.0, 25°C, with shikimate
792
NADP+
pH 9.0, temperature not specified in the publication
792
NADP+
pH 9.0, 30°C, EcDQD/SDH1, shikimate oxidation
0.049
NADPH
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHD, with 3-dehydroshikimate
0.052
NADPH
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHc, with 3-dehydroshikimate
0.202
NADPH
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHa, with 3-dehydroshikimate
27.6
NADPH
pH 8.5, temperature not specified in the publication
27.6
NADPH
pH 8.5, 30°C, EcDQD/SDH1, shikimate formation
45
NADPH
pH 7.0, 25°C, recombinant AroE
45
NADPH
-
pH 7.0, 25°C, with 3-dehydroshikimate
74.1
NADPH
pH 6.5, temperature not specified in the publication
74.1
NADPH
pH 6.5, 30°C, EcDQD/SDH1, shikimate formation
389
NADPH
pH 6.5, temperature not specified in the publication
389
NADPH
pH 6.5, 30°C, EcDQD/SDH1, shikimate formation
0.16
quinate
in the presence of 2 mM NADP+
37.7
quinate
pH 8.8, presence of 2 mM NAD+
61.9
quinate
pH 9.0, 30°C
0.013
shikimate
-
pH 7.5, 22°C, mutant K385A
0.043
shikimate
-
pH 7.5, 22°C, mutant K385N/D423N
0.063
shikimate
-
pH 7.5, 22°C, mutant K385N
0.066
shikimate
mutant Y211F
0.085
shikimate
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHD, with NADP+
0.107
shikimate
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHc, with NADP+
0.121
shikimate
-
pH 7.5, 22°C, mutant D423N
0.153
shikimate
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHa, with NADP+
0.174
shikimate
-
mutant N406A, 22°C
0.346
shikimate
-
mutant Q582L, 22°C
1.5
shikimate
with NADP+, pH 7.0, 25°C
1.99
shikimate
pH 8.8, presence of 2 mM NAD+
1.99
shikimate
in the presence of 2 mM NAD+
2.1
shikimate
-
pH 7.5, 22°C, mutant Y550A
2.78
shikimate
pH 8.8, 25°C, with NADP+
2.78
shikimate
-
pH 8.8, temperature not specified in the publication
3.9
shikimate
-
pH 7.5, 22°C, mutant Y550F
5.16
shikimate
pH 9.0, 30°C, recombinant isozyme VvSDH3
5.8
shikimate
pH 8.8, presence of 2 mM NADP+
5.8
shikimate
in the presence of 2 mM NADP+
7.3
shikimate
-
mutant Q78L, 22°C
7.56
shikimate
pH 7.0, 30°C, recombinant isozyme VvSDH3
7.7
shikimate
pH 8.0, 60°C, recombinant enzyme
7.7
shikimate
-
with NADP+, pH 8.0, 25°C
8.2
shikimate
pH 7.0, 25°C, recombinant AroE
8.2
shikimate
-
pH 7.0, 25°C, with NADP+
11.72
shikimate
pH 7.0, 30°C, recombinant isozyme VvSDH1
11.8
shikimate
pH and temperature not specified in the publication, mutant T381A
16.8
shikimate
-
mutant T381A, 22°C
22
shikimate
pH and temperature not specified in the publication, mutant S338G/T381G
22.8
shikimate
pH 7.0, 25°C, with NADP+
24
shikimate
pH and temperature not specified in the publication, mutant T381G
26.12
shikimate
pH 9.0, 30°C, recombinant isozyme VvSDH4
31
shikimate
pH 7.0, 30°C
31.2
shikimate
pH 8.8, presence of 2 mM NAD+
31.2
shikimate
in the presence of 2 mM NAD+
33.2
shikimate
-
pH 7.5, 22°C, mutant S338A
42
shikimate
-
mutant H335A, 22°C
46.3
shikimate
-
mutant T422S, 22°C
55
shikimate
25°C, pH 9.0
55.5
shikimate
with NADP+, pH 9.0, 25°C
55.7
shikimate
pH 8.8, presence of 2 mM NAD+
66.6
shikimate
-
mutant T407A, 22°C
80.7
shikimate
pH 9.0, temperature not specified in the publication
80.7
shikimate
pH 9.0, 30°C, EcDQD/SDH1, shikimate oxidation
85.2
shikimate
pH 10.0, 30°C
94.55
shikimate
pH 9.0, 30°C, recombinant isozyme VvSDH1
114
shikimate
-
mutant T381S, 22°C
135.8
shikimate
-
pH not specified in the publication, 25°C
135.8
shikimate
-
pH not specified in the publication, 25°C, with NADP+
140
shikimate
-
pH 7.5, 22°C, mutant S336A
146
shikimate
pH 9.0, temperature not specified in the publication
146
shikimate
pH 9.0, 30°C, EcDQD/SDH1, shikimate oxidation
172
shikimate
pH and temperature not specified in the publication, mutant T381S
190
shikimate
pH 9.0, 25°C, recombinant wild-type enzyme
234
shikimate
pH 9.0, 30°C
234
shikimate
with NADP+, pH 9.0, 30°C
237
shikimate
-
with NADP+, pH 9.0, 20°C
266.2
shikimate
pH 8.8, presence of 2 mM NADP+
266.2
shikimate
in the presence of 2 mM NADP+
307
shikimate
pH 8.8, 25°C, with NADP+
399
shikimate
-
pH 9.0, 25°C
399
shikimate
-
pH 9.0, 25°C, with NADP+
427
shikimate
pH and temperature not specified in the publication, mutant S338G
428
shikimate
-
pH 7.5, 22°C, wild-type DELTA88DHQ-SDH enzyme variant
428
shikimate
-
wild-type, 22°C
428
shikimate
pH 8.8, 22°C, with NADP+
516
shikimate
pH and temperature not specified in the publication, wild-type enzyme
755
shikimate
pH 9.0, temperature not specified in the publication
755
shikimate
pH 9.0, 30°C, EcDQD/SDH1, shikimate oxidation
additional information
additional information
no measurable activity with NAD+
-
additional information
additional information
no measurable activity with NAD+
-
additional information
additional information
no measurable activity with NAD+
-
additional information
additional information
no measurable activity with NAD+
-
additional information
additional information
no measurable activity with NAD+
-
additional information
additional information
no measurable activity with NADH
-
additional information
additional information
no measurable activity with NADH
-
additional information
additional information
no measurable activity with NADH
-
additional information
additional information
no measurable activity with NADH
-
additional information
additional information
no measurable activity with NADH
-
additional information
additional information
no measurable activity with NADH+
-
additional information
additional information
no measurable activity with NADH+
-
additional information
additional information
no measurable activity with NADH+
-
additional information
additional information
no measurable activity with NADH+
-
additional information
additional information
no measurable activity with NADH+
-
additional information
additional information
no measurable activity with quinate
-
additional information
additional information
no measurable activity with quinate
-
additional information
additional information
no measurable activity with quinate
-
additional information
additional information
no measurable activity with quinate
-
additional information
additional information
no measurable activity with quinate
-
additional information
additional information
no measurable activity with shikimate
-
additional information
additional information
no measurable activity with shikimate
-
additional information
additional information
no measurable activity with shikimate
-
additional information
additional information
no measurable activity with shikimate
-
additional information
additional information
no measurable activity with shikimate
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.143 - 272
3-dehydroquinate
0.07 - 1700
3-dehydroshikimate
0.143
3-dehydroquinate
pH 7.0, 30°C
272
3-dehydroquinate
pH 7.0, 30°C
0.07
3-dehydroshikimate
pH 10.5, 30°C, EcDQD/SDH2, gallate formation
0.099
3-dehydroshikimate
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHd, with NADPH
0.304
3-dehydroshikimate
pH 10.5, 30°C, EcDQD/SDH2, gallate formation
0.508
3-dehydroshikimate
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHc, with NADPH
1.411
3-dehydroshikimate
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHa, with NADPH
4.16
3-dehydroshikimate
pH 7.0, 30°C, EcDQD/SDH3, DQD activity
5.32
3-dehydroshikimate
pH 8.5, temperature not specified in the publication
5.32
3-dehydroshikimate
pH 8.5, 30°C, EcDQD/SDH2, shikimate formation
9.6
3-dehydroshikimate
mutant K69A, pH 7.3, 25°C
65.6
3-dehydroshikimate
pH 6.5, 30°C, EcDQD/SDH3, shikimate formation
65.6
3-dehydroshikimate
pH 6.5, temperature not specified in the publication
96
3-dehydroshikimate
pH 7.0, 30°C, EcDQD/SDH2, DQD activity
134.5
3-dehydroshikimate
pH 7.0, 30°C, EcDQD/SDH1, DQD activity
186
3-dehydroshikimate
pH 7.0, 30°C, recombinant isozyme VvSDH3
435
3-dehydroshikimate
pH 9.0, 30°C
611
3-dehydroshikimate
pH 7.0, 30°C, recombinant isozyme VvSDH1
805
3-dehydroshikimate
pH 6.5, temperature not specified in the publication
805.8
3-dehydroshikimate
pH 6.5, 30°C, EcDQD/SDH1, shikimate formation
1650
3-dehydroshikimate
pH 7.0, 30°C
1700
3-dehydroshikimate
wild-type enzyme, pH 7.3, 25°C
0.014
L-quinate
pH and temperature not specified in the publication, mutant T381S
0.022
L-quinate
pH and temperature not specified in the publication, mutant T381A
1.64
L-quinate
pH and temperature not specified in the publication, mutant S338G/T381G
2.64
L-quinate
pH and temperature not specified in the publication, mutant T381G
1.42
NAD+
pH 9.0, 25°C, recombinant wild-type enzyme
1.8
NAD+
pH 9.0, 25°C, recombinant mutant N149D
4.17
NAD+
pH 9.0, 25°C, recombinant mutant N149D/V152F
12.55
NAD+
pH 9.0, 25°C, recombinant mutant S131A/N149D/V152F
16.72
NAD+
pH 9.0, 25°C, recombinant mutant S131A/L135A/N149D/V152F
0.13
NADP+
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHD, with shikimate
0.322
NADP+
pH 9.0, 25°C, recombinant mutant N149D
0.374
NADP+
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHc, with shikimate
0.457
NADP+
pH 9.0, 25°C, recombinant mutant N149D/V152F
0.848
NADP+
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHa, with shikimate
2.217
NADP+
pH 9.0, 25°C, recombinant mutant S131A/N149D/V152F
3.133
NADP+
pH 9.0, 25°C, recombinant mutant S131A/L135A/N149D/V152F
262
NADP+
pH 7.0, 30°C, recombinant isozyme VvSDH1
537
NADP+
pH 9.0, 30°C, recombinant isozyme VvSDH4
680
NADP+
pH 9.0, 30°C, recombinant isozyme VvSDH3
862
NADP+
pH 7.0, 30°C, recombinant isozyme VvSDH3
1113
NADP+
pH 9.0, 30°C, recombinant isozyme VvSDH1
1690
NADP+
pH 9.0, temperature not specified in the publication
1691.6
NADP+
pH 9.0, 30°C, EcDQD/SDH3, shikimate oxidation
2070
NADP+
pH 9.0, temperature not specified in the publication
2070.6
NADP+
pH 9.0, 30°C, EcDQD/SDH2, shikimate oxidation
3200
NADP+
pH 9.0, 25°C, recombinant wild-type enzyme
3430
NADP+
-
pH not specified in the publication, 25°C
14000
NADP+
pH 9.0, temperature not specified in the publication
14017.7
NADP+
pH 9.0, 30°C, EcDQD/SDH1, shikimate oxidation
0.195
NADPH
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHc, with 3-dehydroshikimate
0.197
NADPH
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHD, with 3-dehydroshikimate
0.748
NADPH
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHa, with 3-dehydroshikimate
24
NADPH
mutant K69A, pH 7.3, 25°C
3207.8
NADPH
pH 6.5, 30°C, EcDQD/SDH3, shikimate formation
3210
NADPH
pH 6.5, temperature not specified in the publication
4500
NADPH
wild-type enzyme, pH 7.3, 25°C
6300
NADPH
pH 8.5, temperature not specified in the publication
6301.4
NADPH
pH 8.5, 30°C, EcDQD/SDH2, shikimate formation
7858.6
NADPH
pH 6.5, 30°C, EcDQD/SDH1, shikimate formation
7860
NADPH
pH 6.5, temperature not specified in the publication
0.139
shikimate
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHD, with NADP+
0.535
shikimate
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHc, with NADP+
0.56
shikimate
pH 7.5, 30°C, recombinant isozyme CsDQD/SDHa, with NADP+
4.7
shikimate
pH and temperature not specified in the publication, mutant T381A
14.9
shikimate
pH and temperature not specified in the publication, mutant T381G
18
shikimate
pH 7.0, 30°C, recombinant isozyme VvSDH3
22.17
shikimate
pH 9.0, 30°C, EcDQD/SDH3, shikimate oxidation
22.2
shikimate
pH 9.0, temperature not specified in the publication
24.9
shikimate
pH and temperature not specified in the publication, mutant S338G/T381G
71.2
shikimate
pH 9.0, 30°C, EcDQD/SDH2, shikimate oxidation
71.3
shikimate
pH 9.0, temperature not specified in the publication
76
shikimate
pH 7.0, 30°C, recombinant isozyme VvSDH1
111.8
shikimate
pH and temperature not specified in the publication, mutant T381S
168
shikimate
pH 7.0, 30°C
178
shikimate
pH 9.0, 30°C, recombinant isozyme VvSDH4
189
shikimate
pH 9.0, 30°C, recombinant isozyme VvSDH3
779.2
shikimate
pH and temperature not specified in the publication, mutant S338G
854.3
shikimate
pH and temperature not specified in the publication, wild-type enzyme
1051
shikimate
pH 9.0, 30°C, recombinant isozyme VvSDH1
1461.5
shikimate
pH 9.0, 25°C, recombinant wild-type enzyme
1670
shikimate
pH 9.0, 30°C
3620
shikimate
-
pH not specified in the publication, 25°C
23159.5
shikimate
pH 9.0, 30°C, EcDQD/SDH1, shikimate oxidation
23200
shikimate
pH 9.0, temperature not specified in the publication
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evolution
-
a three-dimensional structural model of TgSDH predicts a high level of conservation in the core structure of the enzyme
evolution
-
members of the same gene family encode enzymes with either shikimate or quinate dehydrogenase activity. The poplar genome encodes five DQD/SDH-like genes (Poptr1 to Poptr5), which have diverged into two distinct groups based on sequence analysis and protein structure prediction. In vitro biochemical assays prove that Poptr1 and -5 are true DQD/SDHs, whereas Poptr2 and -3 instead have QDH activity with only residual DQD/SDH activity, cf. EC 1.1.1.282
evolution
phylogenetic analysis of VvSDH isozymes, isozyme VvSDH1 belongs to group I, and clusters with four characterized DQD/SDHs: AtSDH, Poptr1, JrSDH, and NtSDH1, group members share about 75% sequence identity
evolution
phylogenetic analysis of VvSDH isozymes, isozyme VvSDH2 belongs to group II, and clusters with Poptr2 and Poptr3, two characterized DQD/SDHs, and NtSDH2, group members share about 71% sequence identity
evolution
phylogenetic analysis of VvSDH isozymes, isozyme VvSDH3 belongs to group III, group members share about 85% sequence identity, four of them from different species (VvSDH3, CasSDH2, FvSDH1, and EgSDH3) accumulate gallic acid-based tannins
evolution
phylogenetic analysis of VvSDH isozymes, isozyme VvSDH4 belongs to group IV, and clusters with with Poptr5, a DQD/SDH characterized in Populus trichocarpa, group members share about 77% sequence identity
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
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
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
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
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
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
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
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
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
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
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
evolution
Escherichia coli constitutively expresses two shikimate dehydrogenase paralogues, AroE and the NAD+ -dependent enzyme quinate/shikimate dehydrogenase (YdiB), sharing 25% sequence identity. While AroE is NADP+-dependent, YdiB uses NADP+ or NAD+. Contrary to AroE, YdiB displays a clear activity on quinate, with either NADP+ or NAD+ as a cofactor in addition to shikimate
evolution
four CsDQD/SDH isozyme proteins are cloned from Camellia sinensis. Three CsDQD/SDH isozymes show 3-dehydroshikimate (3-DHS) reduction and shikimate (SA) oxidation functions with individual differences between the catalytic efficiency of 3-DHS reduction and SA oxidation. Isozyme CsDQD/SDHa has higher catalytic efficiency for 3-DHS reduction than for SA oxidation, isozyme CsDQD/SDHd shows the opposite tendency, and isozyme CsDQD/SDHc has almost equal catalytic efficiency for 3-DHS reduction and SA oxidation. In vitro, Gallic acid (GA) is mainly generated from 3-DHS through nonenzymatic conversion. Isozymes CsDQD/SDHc and CsDQD/ SDHd genes are involved in GA synthesis
evolution
plant QDHs arose directly from bifunctional dehydroquinate dehydratase-shikimate dehydrogenases (DHQD-SDHs) through different convergent evolutionary events, detailed phylogenetic analysis, overview. Eudicot and conifer QDHs arose early in vascular plant evolution whereas Brassicaceae QDHs emerged late, process of recurrent evolution of QDH. This family of proteins independently evolved NAD+ and NADP+ specificity in eudicots. The acquisition of QDH activity by these proteins is accompanied by the inactivation or functional evolution of the DHQD domain, as verified by enzyme activity assays and as reflected in the loss of key DHQD active site residues
evolution
plant SDH enzymes are fused to dehydroquinate dehydratases (DQDs, EC 4.2.1.10) to form bifunctional DQD/SDH enzymes. The DQD activity is observed for EcDQD/SDH1, 2, and 3, but not for EcDQD/SDH4a. Among the active enzymes, EcDQD/SDH1 exhibits the highest DQD activity, followed by EcDQD/SDH2 (about 50% of the EcDQD/SDH1 activity) and EcDQD/SDH3 (about 5% of the EcDQD/SDH1 activity). For shikimate formation from 3-DHS as well as shikimate oxidation to 3-DHS, measurable catalytic activities are detected for EcDQD/SDH1-3, but the activities of EcDQD/SDH2 and 3 are less than 20% of those of EcDQD/SDH1. Regarding the cofactor, EcDQD/SDH1-3 have a clear preference for NADPH/NADP+ over NADH/ NAD+. In contrast, EcDQD/SDH4a and b lack shikimate formation activity. For the reverse reaction, the conversion of shikimate to 3-DHS, EcDQD/SDH4a and b display low enzymatic activity with a preference for NAD+ as the cofactor. Both EcDQD/SDH2 and 3 exhibit relatively high gallate formation activity, in contrast to the low activity of EcDQD/SDH1. The preferred cofactor in this reaction is NADP+
evolution
-
the enzyme belongs to the QDH family, phylogenetic reconstruction of the SDH/QDH gene family across land plants, overview. SDH and QDH belong to the same gene family, which diverged into two phylogenetic clades after a defining gene duplication just prior to the angiosperm/gymnosperm split. Non-seed plants that diverged before this duplication harbour only a single gene of this family. Extant representatives from the chlorophytes (Chlamydomonas reinhardtii), bryophytes (Physcomitrella patens) and lycophytes (Selaginella moellendorfii) encoded almost exclusively SDH activity in vitro. A reconstructed ancestral sequence representing the node just prior to the gene duplication also encoded SDH activity. Quinate dehydrogenase activity was gained only in seed plants following gene duplication. Quinate dehydrogenases of gymnosperms, e.g. Pinus taeda, may be reminiscent of an evolutionary intermediate since they encode equal SDH and QDH activities. The second copy in Pinus taeda maintains specificity for shikimate similar to the activity found in the angiosperm SDH sister clade. The codon for a tyrosine residue within the active site displays a signature of positive selection at the node defining the QDH clade, where it changed to a glycine. Replacing the tyrosine with a glycine in a highly shikimate-specific angiosperm SDH is sufficient to gain some QDH function. Thus, very few mutations are necessary to facilitate the evolution of QDH genes. The two proteins from Pinus taeda are chosen to represent the post-duplication SDH and QDH clades from gymnosperms. The single-copy genes from Selaginella moellendorffii, Physcomitrella patens and Chlamydomonas reinhardtii are selected to represent the pre-duplication lycopod, bryophyte and green algal clades, respectively. Thr381 is conserved in most members across all SDH clades but was replaced under positive selection by Gly in the branch leading into the seed plant QDH clade
evolution
-
the enzyme belongs to the QDH family, phylogenetic reconstruction of the SDH/QDH gene family across land plants, overview. SDH and QDH belong to the same gene family, which diverged into two phylogenetic clades after a defining gene duplication just prior to the angiosperm/gymnosperm split. Non-seed plants that diverged before this duplication harbour only a single gene of this family. Extant representatives from the chlorophytes (Chlamydomonas reinhardtii), bryophytes (Physcomitrella patens) and lycophytes (Selaginella moellendorfii) encoded almost exclusively SDH activity in vitro. A reconstructed ancestral sequence representing the node just prior to the gene duplication also encoded SDH activity. Quinate dehydrogenase activity was gained only in seed plants following gene duplication. Quinate dehydrogenases of gymnosperms, e.g. Pinus taeda, may be reminiscent of an evolutionary intermediate since they encode equal SDH and QDH activities. The second copy in Pinus taeda maintains specificity for shikimate similar to the activity found in the angiosperm SDH sister clade. The codon for a tyrosine residue within the active site displays a signature of positive selection at the node defining the QDH clade, where it changed to a glycine. Replacing the tyrosine with a glycine in a highly shikimate-specific angiosperm SDH is sufficient to gain some QDH function. Thus, very few mutations are necessary to facilitate the evolution of QDH genes. The two proteins from Pinus taeda are chosen to represent the post-duplication SDH and QDH clades from gymnosperms. The single-copy genes from Selaginella moellendorffii, Physcomitrella patens and Chlamydomonas reinhardtii are selected to represent the pre-duplication lycopod, bryophyte and green algal clades, respectively. Thr381 is conserved in most members across all SDH clades but was replaced under positive selection by Gly in the branch leading into the seed plant QDH clade
evolution
-
the enzyme belongs to the QDH family, phylogenetic reconstruction of the SDH/QDH gene family across land plants, overview. SDH and QDH belong to the same gene family, which diverged into two phylogenetic clades after a defining gene duplication just prior to the angiosperm/gymnosperm split. Non-seed plants that diverged before this duplication harbour only a single gene of this family. Extant representatives from the chlorophytes (Chlamydomonas reinhardtii), bryophytes (Physcomitrella patens) and lycophytes (Selaginella moellendorfii) encoded almost exclusively SDH activity in vitro. A reconstructed ancestral sequence representing the node just prior to the gene duplication also encoded SDH activity. Quinate dehydrogenase activity was gained only in seed plants following gene duplication. Quinate dehydrogenases of gymnosperms, e.g. Pinus taeda, may be reminiscent of an evolutionary intermediate since they encode equal SDH and QDH activities. The second copy in Pinus taeda maintains specificity for shikimate similar to the activity found in the angiosperm SDH sister clade. The codon for a tyrosine residue within the active site displays a signature of positive selection at the node defining the QDH clade, where it changed to a glycine. Replacing the tyrosine with a glycine in a highly shikimate-specific angiosperm SDH is sufficient to gain some QDH function. Thus, very few mutations are necessary to facilitate the evolution of QDH genes. The two proteins from Pinus taeda are chosen to represent the post-duplication SDH and QDH clades from gymnosperms. The single-copy genes from Selaginella moellendorffii, Physcomitrella patens and Chlamydomonas reinhardtii are selected to represent the pre-duplication lycopod, bryophyte and green algal clades, respectively. Thr381 is conserved in most members across all SDH clades but was replaced under positive selection by Gly in the branch leading into the seed plant QDH clade
evolution
-
the enzyme belongs to the QDH family, phylogenetic reconstruction of the SDH/QDH gene family across land plants, overview. SDH and QDH belong to the same gene family, which diverged into two phylogenetic clades after a defining gene duplication just prior to the angiosperm/gymnosperm split. Non-seed plants that diverged before this duplication harbour only a single gene of this family. Extant representatives from the chlorophytes (Chlamydomonas reinhardtii), bryophytes (Physcomitrella patens) and lycophytes (Selaginella moellendorfii) encoded almost exclusively SDH activity in vitro. A reconstructed ancestral sequence representing the node just prior to the gene duplication also encoded SDH activity. Quinate dehydrogenase activity was gained only in seed plants following gene duplication. Quinate dehydrogenases of gymnosperms, e.g. Pinus taeda, may be reminiscent of an evolutionary intermediate since they encode equal SDH and QDH activities. The second copy in Pinus taeda maintains specificity for shikimate similar to the activity found in the angiosperm SDH sister clade. The codon for a tyrosine residue within the active site displays a signature of positive selection at the node defining the QDH clade, where it changed to a glycine. Replacing the tyrosine with a glycine in a highly shikimate-specific angiosperm SDH is sufficient to gain some QDH function. Thus, very few mutations are necessary to facilitate the evolution of QDH genes. The two proteins from Pinus taeda are chosen to represent the post-duplication SDH and QDH clades from gymnosperms. The single-copy genes from Selaginella moellendorffii, Physcomitrella patens and Chlamydomonas reinhardtii are selected to represent the pre-duplication lycopod, bryophyte and green algal clades, respectively. Thr381 is conserved in most members across all SDH clades but was replaced under positive selection by Gly in the branch leading into the seed plant QDH clade
evolution
-
the enzyme belongs to the QDH family, phylogenetic reconstruction of the SDH/QDH gene family across land plants, overview. SDH and QDH belong to the same gene family, which diverged into two phylogenetic clades after a defining gene duplication just prior to the angiosperm/gymnosperm split. Non-seed plants that diverged before this duplication harbour only a single gene of this family. Extant representatives from the chlorophytes (Chlamydomonas reinhardtii), bryophytes (Physcomitrella patens) and lycophytes (Selaginella moellendorfii) encoded almost exclusively SDH activity in vitro. A reconstructed ancestral sequence representing the node just prior to the gene duplication also encoded SDH activity. Quinate dehydrogenase activity was gained only in seed plants following gene duplication. Quinate dehydrogenases of gymnosperms, e.g. Pinus taeda, may be reminiscent of an evolutionary intermediate since they encode equal SDH and QDH activities. The second copy in Pinus taeda maintains specificity for shikimate similar to the activity found in the angiosperm SDH sister clade. The codon for a tyrosine residue within the active site displays a signature of positive selection at the node defining the QDH clade, where it changed to a glycine. Replacing the tyrosine with a glycine in a highly shikimate-specific angiosperm SDH is sufficient to gain some QDH function. Thus, very few mutations are necessary to facilitate the evolution of QDH genes. The two proteins from Pinus taeda are chosen to represent the post-duplication SDH and QDH clades from gymnosperms. The single-copy genes from Selaginella moellendorffii, Physcomitrella patens and Chlamydomonas reinhardtii are selected to represent the pre-duplication lycopod, bryophyte and green algal clades, respectively. Thr381 is conserved in most members across all SDH clades but was replaced under positive selection by Gly in the branch leading into the seed plant QDH clade
evolution
-
the enzyme belongs to the QDH family, phylogenetic reconstruction of the SDH/QDH gene family across land plants, overview. SDH and QDH belong to the same gene family, which diverged into two phylogenetic clades after a defining gene duplication just prior to the angiosperm/gymnosperm split. Non-seed plants that diverged before this duplication harbour only a single gene of this family. Extant representatives from the chlorophytes (Chlamydomonas reinhardtii), bryophytes (Physcomitrella patens) and lycophytes (Selaginella moellendorfii) encoded almost exclusively SDH activity in vitro. A reconstructed ancestral sequence representing the node just prior to the gene duplication also encoded SDH activity. Quinate dehydrogenase activity was gained only in seed plants following gene duplication. Quinate dehydrogenases of gymnosperms, e.g. Pinus taeda, may be reminiscent of an evolutionary intermediate since they encode equal SDH and QDH activities. The second copy in Pinus taeda maintains specificity for shikimate similar to the activity found in the angiosperm SDH sister clade. The codon for a tyrosine residue within the active site displays a signature of positive selection at the node defining the QDH clade, where it changed to a glycine. Replacing the tyrosine with a glycine in a highly shikimate-specific angiosperm SDH is sufficient to gain some QDH function. Thus, very few mutations are necessary to facilitate the evolution of QDH genes. The two proteins from Pinus taeda are chosen to represent the post-duplication SDH and QDH clades from gymnosperms. The single-copy genes from Selaginella moellendorffii, Physcomitrella patens and Chlamydomonas reinhardtii are selected to represent the pre-duplication lycopod, bryophyte and green algal clades, respectively. Thr381 is conserved in most members across all SDH clades but was replaced under positive selection by Gly in the branch leading into the seed plant QDH clade
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
-
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
-
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
-
evolution
-
members of the same gene family encode enzymes with either shikimate or quinate dehydrogenase activity. The poplar genome encodes five DQD/SDH-like genes (Poptr1 to Poptr5), which have diverged into two distinct groups based on sequence analysis and protein structure prediction. In vitro biochemical assays prove that Poptr1 and -5 are true DQD/SDHs, whereas Poptr2 and -3 instead have QDH activity with only residual DQD/SDH activity, cf. EC 1.1.1.282
-
evolution
-
Escherichia coli constitutively expresses two shikimate dehydrogenase paralogues, AroE and the NAD+ -dependent enzyme quinate/shikimate dehydrogenase (YdiB), sharing 25% sequence identity. While AroE is NADP+-dependent, YdiB uses NADP+ or NAD+. Contrary to AroE, YdiB displays a clear activity on quinate, with either NADP+ or NAD+ as a cofactor in addition to shikimate
-
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
-
malfunction
a contact with the shikimate C1-carboxyl is formed by the phenol hydroxyl of a tyrosine. Substitution of this residue in Arabidopsis thaliana DHQ-SDH causes a substantial reduction in turnover rate
malfunction
in the ydiB knockout mutant, QA production is 6.17% relative to SA (mol/mol), indicating that the inactivation of ydiB is a suitable strategy to reduce QA production below 10% (mol/mol) relative to SA in culture fermentations for SA production. The inactivation of ydiB in Escherichia coli strain PB12.SA22 and the reduction in QA production support the role of YdiB in the synthesis of this compound from DHQ. In the absence of YdiB, the DHS concentration detected in supernatant cultures is maintained relatively constant during the stationary phase
malfunction
-
mutation of Lys69 to alanine significantly reduces the catalytic efficiency of Helicobacter pylori SDH. Mutation of Lys69 triggers the movement of shikimate away from the active site of SDH, thereby disrupting the catalytic activity
malfunction
the mutation of residues Ser338 and NRT to Gly and DI/LD in the SDH unit is the reason for the low activity of isozyme CsDQD/SDHb for 3-DHS reduction and SA oxidation
malfunction
-
in the ydiB knockout mutant, QA production is 6.17% relative to SA (mol/mol), indicating that the inactivation of ydiB is a suitable strategy to reduce QA production below 10% (mol/mol) relative to SA in culture fermentations for SA production. The inactivation of ydiB in Escherichia coli strain PB12.SA22 and the reduction in QA production support the role of YdiB in the synthesis of this compound from DHQ. In the absence of YdiB, the DHS concentration detected in supernatant cultures is maintained relatively constant during the stationary phase
-
metabolism
aroE-encoded shikimate dehydrogenase catalyzes the forth reaction in the shikimate pathway
metabolism
-
SKDH is one of the crucial enzymes in the biosynthesis of anthocyanin metabolites, overview
metabolism
in plants, 3-dehydroshikimate from the shikimate pathway is thought to be the immediate precursor of gallate, a component of hydrolysable tannins. Metabolic pathways involving SDH family proteins: (A) the shikimate pathway, (B) the quinate pathway, (C) the aminoshikimate pathway, overview
metabolism
-
in plants, 3-dehydroshikimate from the shikimate pathway is thought to be the immediate precursor of gallate, a component of hydrolysable tannins. Metabolic pathways involving SDH family proteins: (A) the shikimate pathway. (B) the quinate pathway. (C) the aminoshikimate pathway, overview
metabolism
in plants, the shikimate pathway provides aromatic amino acids that are used to generate numerous secondary metabolites, including phenolic compounds. In this pathway, shikimate dehydrogenases catalyse the reversible dehydrogenation of 3-dehydroshikimate to shikimate
metabolism
in plants, the shikimate pathway provides aromatic amino acids that are used to generate numerous secondary metabolites, including phenolic compounds. In this pathway, shikimate dehydrogenases catalyse the reversible dehydrogenation of 3-dehydroshikimate to shikimate. Gallic acid metabolism in grape berry tissues along development, overview
metabolism
the enzyme catalyze the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
metabolism
-
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
metabolism
-
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
metabolism
-
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
metabolism
-
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
metabolism
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
metabolism
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
metabolism
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
metabolism
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
metabolism
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
metabolism
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites. SDH is part of the Arom complex, that catalyzes both the third and fourth reactions in the shikimate pathway. This large enzyme complex contains five functional domains that are equivalent to the monofunctional enzymes (in bacteria) catalyzing reactions two through six of the shikimate pathway
metabolism
-
the enzyme is part of the AROM complex, a large pentafunctional polypeptide, which catalyzes steps two through six of the shikimate pathway in fungi. This complex has the following functional domains (from N- to C-terminus): dehydroquinate synthase, 5-enolypyruvylshikimate-3-phosphate synthase, shikimate kinase, dehydroquinate dehydratase, and SDH. These domains catalyze steps 2, 6, 5, 3, and 4 of the pathway, respectively. The first and last enzymes of the fungal shikimate pathway,3-deoxy-D-arabinoheptulosonate 7-phosphate synthase and chorismate synthase, are discrete enzymes
metabolism
-
the shikimate pathway leads to the biosynthesis of aromatic amino acids essential for protein biosynthesis and the production of a wide array of plant secondary metabolites. 3-Dehydroquinate is the substrate for shikimate biosynthesis through the sequential actions of dehydroquinate dehydratase (DQD) and shikimate dehydrogenase (SDH) contained in a single protein in plants. Reactions comprising the shikimate/quinate cycle, overview
metabolism
3-dehydroquinate dehydratase/shikimate dehydrogenase (DQD/SDH) is a key enzyme for catalyzing the conversion of 3-dehydroshikimate (3-DHS) to shikimate (SA). It also potentially participates in gallic acid (GA) synthesis in a branch of the SA pathway. Gallic acid (GA) is a precursor for polyphenol synthesis. The CsDQD/SDHc and CsDQD/ SDHd genes are involved in GA synthesis. In plants, DQD/SDH, a bifunctional enzyme, is crucial in the third and fourth reversible reactions in the SA pathway. Biosynthetic pathway of gallic acid and shikimic acid in plants, overview. GA could be spontaneously generated from 3-DHS in the enzymatic or nonenzymatic CsDQD/SDHs assay when using 3-DHS and the coenzyme NADP+ as substrates
metabolism
-
link between reactions catalysed by the shikimate pathway enzyme dehydroquinate dehydratase (DQD)/shikimate dehydrogenase (SDH) and quinate dehydrogenase (QDH) involved in quinate metabolism. Shikimate is produced from dehydroquinate via a two-step reaction and subsequently channelled to downstream reactions in the pathway. Quinate is reversibly formed from a side branch of the shikimate pathway from dehydroquinate and may be converted to more structurally complex secondary metabolites or to dehydroquinate to fuel the shikimate pathway
metabolism
-
link between reactions catalysed by the shikimate pathway enzyme dehydroquinate dehydratase (DQD)/shikimate dehydrogenase (SDH) and quinate dehydrogenase (QDH) involved in quinate metabolism. Shikimate is produced from dehydroquinate via a two-step reaction and subsequently channelled to downstream reactions in the pathway. Quinate is reversibly formed from a side branch of the shikimate pathway from dehydroquinate and may be converted to more structurally complex secondary metabolites or to dehydroquinate to fuel the shikimate pathway
metabolism
-
link between reactions catalysed by the shikimate pathway enzyme dehydroquinate dehydratase (DQD)/shikimate dehydrogenase (SDH) and quinate dehydrogenase (QDH) involved in quinate metabolism. Shikimate is produced from dehydroquinate via a two-step reaction and subsequently channelled to downstream reactions in the pathway. Quinate is reversibly formed from a side branch of the shikimate pathway from dehydroquinate and may be converted to more structurally complex secondary metabolites or to dehydroquinate to fuel the shikimate pathway
metabolism
-
link between reactions catalysed by the shikimate pathway enzyme dehydroquinate dehydratase (DQD)/shikimate dehydrogenase (SDH) and quinate dehydrogenase (QDH) involved in quinate metabolism. Shikimate is produced from dehydroquinate via a two-step reaction and subsequently channelled to downstream reactions in the pathway. Quinate is reversibly formed from a side branch of the shikimate pathway from dehydroquinate and may be converted to more structurally complex secondary metabolites or to dehydroquinate to fuel the shikimate pathway
metabolism
-
link between reactions catalysed by the shikimate pathway enzyme dehydroquinate dehydratase (DQD)/shikimate dehydrogenase (SDH) and quinate dehydrogenase (QDH) involved in quinate metabolism. Shikimate is produced from dehydroquinate via a two-step reaction and subsequently channelled to downstream reactions in the pathway. Quinate is reversibly formed from a side branch of the shikimate pathway from dehydroquinate and may be converted to more structurally complex secondary metabolites or to dehydroquinate to fuel the shikimate pathway
metabolism
-
link between reactions catalysed by the shikimate pathway enzyme dehydroquinate dehydratase (DQD)/shikimate dehydrogenase (SDH) and quinate dehydrogenase (QDH) involved in quinate metabolism. Shikimate is produced from dehydroquinate via a two-step reaction and subsequently channelled to downstream reactions in the pathway. Quinate is reversibly formed from a side branch of the shikimate pathway from dehydroquinate and may be converted to more structurally complex secondary metabolites or to dehydroquinate to fuel the shikimate pathway
metabolism
shikimate dehydrogenase (HpSDH) is a key enzyme in the shikimate pathway of Helicobacter pylori, which catalyzes the NADPH-dependent reversible reduction of 3-dehydroshikimate to shikimate
metabolism
-
shikimate dehydrogenase is one of the enzymes involved in the initial steps of the biosynthesis of amino acids such as histidine, tryptophan, tyrosine, phenylalanine, lysine, and aspartic acid
metabolism
shikimate, quinate, and gallate biosynthesis catalyzed by DQD/SDH family enzymes, overview. Plant DQD/SDHs are proposed to link the shikimate pathway to gallate and quinate metabolism
metabolism
shikimate, quinate, and gallate biosynthesis catalyzed by DQD/SDH family enzymes, overview. Plant DQD/SDHs are proposed to link the shikimate pathway to gallate and quinate metabolism. Isozymes EcDQD/SDH2 and 3 from Eucalyptus camaldulensis catalyze the NADP+-dependent oxidation of 3-dehydroshikimate to produce gallate. In Eucalyptus camaldulensis, EcDQD/SDH2 and 3 are co-expressed with UGT84A25a/b and UGT84A26a/b involved in hydrolyzable tannin biosynthesis, catalyze the synthesis of beta-glucogallin
metabolism
shikimate, quinate, and gallate biosynthesis catalyzed by DQD/SDH family enzymes, overview. Plant DQD/SDHs are proposed to link the shikimate pathway to gallate and quinate metabolism. Isozymes EcDQD/SDH2 and 3 from Eucalyptus camaldulensis catalyze the NADP+-dependent oxidation of 3-dehydroshikimate to produce gallate. In Eucalyptus camaldulensis, EcDQD/SDH2 and 3 are co-expressed with UGT84A25a/b and UGT84A26a/b involved in hydrolyzable tannin biosynthesis, they catalyze the synthesis of beta-glucogallin
metabolism
the enzyme is active in the shikimic acid pathway, which is present in bacteria, fungi, plants and in certain apicomplexan parasites but is absent from humans, pathway overview
metabolism
the outer peels of Punica granatum fruits possess two groups of polyphenols: anthocyanins (ATs) and hydrolysable tannins (HTs). Their biosynthesis intersects at 3-dehydroshikimate (3-DHS) in the shikimate pathway by the activity of shikimate dehydrogenase (SDH), which converts 3-DHS to shikimate (providing the precursor for AT biosynthesis) or to gallic acid (the precursor for HTs biosynthesis) using NADPH or NADP+ as a cofactor. The outer fruit peel is subjected to light/dark treatment and osmotic stresses (imposed by different sucrose concentrations) showing that light with high sucrose promotes the synthesis of ATs, while dark at the same sucrose concentration promotes the synthesis of HTs. Role of PgSDH in the branch point leading to gallic acid and shikimate, detailed overview. The activity of isozymes PgSDH3, PgSDH3a and PgSDH4 may lead to the synthesis of phenols required for protecting the cells from osmotic stress. Since PgSDH3.2 has a plastid transit peptide, it may mainly use the NADP+ that accumulates in the dark in plastids, while PgSDH3.1, PgSDH3a and PgSDH4 use this cofactor that mainly accumulates during stress
metabolism
-
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
-
metabolism
-
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites. SDH is part of the Arom complex, that catalyzes both the third and fourth reactions in the shikimate pathway. This large enzyme complex contains five functional domains that are equivalent to the monofunctional enzymes (in bacteria) catalyzing reactions two through six of the shikimate pathway
-
metabolism
-
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
-
metabolism
-
the shikimate pathway leads to the biosynthesis of aromatic amino acids essential for protein biosynthesis and the production of a wide array of plant secondary metabolites. 3-Dehydroquinate is the substrate for shikimate biosynthesis through the sequential actions of dehydroquinate dehydratase (DQD) and shikimate dehydrogenase (SDH) contained in a single protein in plants. Reactions comprising the shikimate/quinate cycle, overview
-
metabolism
-
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
-
physiological function
a strain deficient in isoform qsuD does not grow on either shikimate or quinate as sole carbon sources but grows largely unhindered on glucose
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
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
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
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
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
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
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
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
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
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
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 enzyme reaction represents the fourth step of the shikimate pathway
physiological function
-
the conversion of 3-dehydroquinate to shikimate via 3-dehydroshikimate is catalyzed by the bifunctional enzyme dehydroquinate dehydratase/shikimate dehydrogenase (DQD/SDH, EC 4.2.1.10 and E.C. 1.1.1.25). The DQD domain constitutes the N-terminal half of the protein and the SDH domain the C-terminal half. Poplar DQD/SDHs have distinct expression profiles suggesting separate roles in protein and lignin biosynthesis. Shikimate is essential for protein biosynthesis
physiological function
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the conversion of 3-dehydroquinate to shikimate via 3-dehydroshikimate is catalyzed by the bifunctional enzyme dehydroquinate dehydratase/shikimate dehydrogenase (DQD/SDH, EC 4.2.1.10 and EC 1.1.1.25). The DQD domain constitutes the N-terminal half of the protein and the SDH domain the C-terminal half. Poplar DQD/SDHs have distinct expression profiles suggesting separate roles in protein and lignin biosynthesis. Shikimate is essential for protein biosynthesis
physiological function
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Toxoplasma gondii encodes a large pentafunctional polypeptide known as the AROM complex which catalyzes five reactions in the shikimate pathway, a metabolic pathway required for the biosynthesis of the aromatic amino acids and a promising target for anti-parasitic agents. The shikimate dehydrogenase domain (TgSDH) from the Toxoplasma gondii AROM complex catalyzes the NADP+-dependent oxidation of shikimate in the absence of the remaining AROM domains
physiological function
3-dehydroquinate dehydratase/shikimate dehydrogenase (DQD/SDH) is a key enzyme for catalyzing the conversion of 3-dehydroshikimate (3-DHS) to shikimate (SA). It also potentially participates in gallic acid (GA) synthesis in a branch of the SA pathway. Quantitative RT-PCR analysis shows that CsDQD/SDHc and CsDQD/SDHd expression is correlated with GA and 1-O-galloyl-beta-D-glucose accumulation in Camellia sinensis. The SA pathway is important to plant growth, development, and defense. Polyphenols in tea plants, including phenolic acids, catechins, and flavonol derivatives, not only determine the mouthfeel of tea infusions but also provide health benefits
physiological function
role of shikimate dehydrogenase in controlling the production of anthocyanins (ATs) and hydrolysable tannins (HTs) in the outer peels of pomegranate, Punica granatum. The biosynthesis of HTs and ATs competes for the same substrate, 3-DHS, and that SDH activity is regulated not only by the NADPH/NADP+ ratio, but also by the expression of the PgSDHs
physiological function
-
shikimate dehydrogenase (SDH) catalyzes the reversible, NADPH-dependent reduction of 3-dehydroshikimate to shikimate, involved in the shikimate pathway
physiological function
shikimate dehydrogenase (SDH) from Mycobacterium tuberculosis (MtbSDH), encoded by the aroE gene, is essential for viability of Mycobacterium tuberculosis
physiological function
the tree species Eucalyptus camaldulensis shows exceptionally high tolerance against aluminum, a widespread toxic metal in acidic soils. In the roots of Eucalyptus camaldulensis, aluminum is detoxified via the complexation with oenothein B, a hydrolyzable tannin. The biosynthesis of oenothein B involves dehydroquinate dehydratase/shikimate dehydrogenases (EcDQD/SDHs) which catalyzes the formation of gallate, the phenolic constituent of hydrolyzable tannins
physiological function
the tree species Eucalyptus camaldulensis shows exceptionally high tolerance against aluminum, a widespread toxic metal in acidic soils. In the roots of Eucalyptus camaldulensis, aluminum is detoxified via the complexation with oenothein B, a hydrolyzable tannin. The biosynthesis of oenothein B involves dehydroquinate dehydratase/shikimate dehydrogenases (EcDQD/SDHs) which catalyzes the formation of gallate, the phenolic constituent of hydrolyzable tannins. Two enzymes, EcDQD/SDH2 and 3, in Eucalyptus camaldulensis catalyze the NADP+-dependent oxidation of 3-dehydroshikimate to produce gallate. EcDQD/SDH2 and 3 maintain DQD and SDH activities, resulting in a 3-dehydroshikimate supply for gallate formation
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
-
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
-
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
-
physiological function
-
the conversion of 3-dehydroquinate to shikimate via 3-dehydroshikimate is catalyzed by the bifunctional enzyme dehydroquinate dehydratase/shikimate dehydrogenase (DQD/SDH, EC 4.2.1.10 and E.C. 1.1.1.25). The DQD domain constitutes the N-terminal half of the protein and the SDH domain the C-terminal half. Poplar DQD/SDHs have distinct expression profiles suggesting separate roles in protein and lignin biosynthesis. Shikimate is essential for protein biosynthesis
-
physiological function
-
the conversion of 3-dehydroquinate to shikimate via 3-dehydroshikimate is catalyzed by the bifunctional enzyme dehydroquinate dehydratase/shikimate dehydrogenase (DQD/SDH, EC 4.2.1.10 and EC 1.1.1.25). The DQD domain constitutes the N-terminal half of the protein and the SDH domain the C-terminal half. Poplar DQD/SDHs have distinct expression profiles suggesting separate roles in protein and lignin biosynthesis. Shikimate is essential for protein biosynthesis
-
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
-
physiological function
-
a strain deficient in isoform qsuD does not grow on either shikimate or quinate as sole carbon sources but grows largely unhindered on glucose
-
additional information
the shikimate pathway is an attractive target for the development of antitubercular agents because it is essential in Mycobacterium tuberculosis, the causative agent of tuberculosis, but absent in humans
additional information
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the shikimate pathway is an attractive target for the development of antitubercular agents because it is essential in Mycobacterium tuberculosis, the causative agent of tuberculosis, but absent in humans
additional information
in plants such as Arabidopsis thaliana and Populus trichocarpa, shikimate dehydrogenase SDH is fused to an anabolic (type I) dehydroquinate dehydratase (DHQ), forming a bifunctional protein known as the DHQ-SDH complex, cf. EC 4.2.1.10 and EC 1.1.1.25. The close proximity of domains in the DHQ-SDH complex may facilitate substrate channeling between enzyme active sites, minimizing the loss of shikimate pathway intermediates to competing processe. Crystallization of the Arabidopsis thaliana protein with shikimate bound in the SDH domain and tartrate (a component of the crystallization solution) in the DHQ domain reveals a V-shaped orientation of the domains. Addition of NADP+ to DHQSDH crystals already containing shikimate in the SDH domain results in the production of 3-dehydroshikimate by the SDH domain and the transfer of the compound to the DHQ active sites
additional information
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in plants such as Arabidopsis thaliana and Populus trichocarpa, shikimate dehydrogenase SDH is fused to an anabolic (type I) dehydroquinate dehydratase (DHQ), forming a bifunctional protein known as the DHQSDH complex, cf. EC 4.2.1.10 and EC 1.1.1.25. The close proximity of domains in the DHQSDH complex may facilitate substrate channeling between enzyme active sites, minimizing the loss of shikimate pathway intermediates to competing processes
additional information
modelling of steady state and dynamic fluxes into pentose phosphate pathway and the flux split ratio into glycolysis and pentose phosphate pathway in Saccharomyces recombinantly expressing Escherichia coli shikimate dehydrogenase, overview
additional information
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three-dimensional protein structures homology modelling of the five putative poplar DQD/SDHs using Arabidopsis DQD/SDH enzyme structure, PDB ID c2o7qA, of the enzyme coupled with either 3-dehydroshikimate and tartrate or shikimate, as a template
additional information
analysis of the catalytic active site in the crystal structure of HpSDH in complex with its substrate NADPH and product shikimate. The site can be divided into three spatially separated subpockets that separately correspond to the binding regions of shikimate, NADPH dihydronicotinamide moiety, and NADPH adenine moiety
additional information
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analysis of the catalytic active site in the crystal structure of HpSDH in complex with its substrate NADPH and product shikimate. The site can be divided into three spatially separated subpockets that separately correspond to the binding regions of shikimate, NADPH dihydronicotinamide moiety, and NADPH adenine moiety
additional information
EcDQD/SDH1 enzyme structure homology modeling using the structure of Arabidopsis thaliana AtDQD/SDH (Uniprot ID Q9SQT8) as template, docking of 3-dehydroshikimate into the active site of the models as well as the crystal structure of PDB ID 2O7S, molecular dynamics simulation of protein-ligand interaction
additional information
EcDQD/SDH1 enzyme structure homology modeling using the structure of Arabidopsis thaliana AtDQD/SDH (Uniprot ID Q9SQT8) as template, docking of 3-dehydroshikimate into the active site of the models as well as the crystal structure of PDB ID 2O7S, molecular dynamics simulation of protein-ligand interaction
additional information
EcDQD/SDH1 enzyme structure homology modeling using the structure of Arabidopsis thaliana AtDQD/SDH (Uniprot ID Q9SQT8) as template, docking of 3-dehydroshikimate into the active site of the models as well as the crystal structure of PDB ID 2O7S, molecular dynamics simulation of protein-ligand interaction
additional information
-
EcDQD/SDH1 enzyme structure homology modeling using the structure of Arabidopsis thaliana AtDQD/SDH (Uniprot ID Q9SQT8) as template, docking of 3-dehydroshikimate into the active site of the models as well as the crystal structure of PDB ID 2O7S, molecular dynamics simulation of protein-ligand interaction
additional information
EcDQD/SDH2 enzyme structure homology modeling using the structure of Arabidopsis thaliana AtDQD/SDH (Uniprot ID Q9SQT8) as template, docking of 3-dehydroshikimate into the active site of the models as well as the crystal structure of PDB ID 2O7S, molecular dynamics simulation of protein-ligand interaction
additional information
EcDQD/SDH2 enzyme structure homology modeling using the structure of Arabidopsis thaliana AtDQD/SDH (Uniprot ID Q9SQT8) as template, docking of 3-dehydroshikimate into the active site of the models as well as the crystal structure of PDB ID 2O7S, molecular dynamics simulation of protein-ligand interaction
additional information
EcDQD/SDH2 enzyme structure homology modeling using the structure of Arabidopsis thaliana AtDQD/SDH (Uniprot ID Q9SQT8) as template, docking of 3-dehydroshikimate into the active site of the models as well as the crystal structure of PDB ID 2O7S, molecular dynamics simulation of protein-ligand interaction
additional information
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EcDQD/SDH2 enzyme structure homology modeling using the structure of Arabidopsis thaliana AtDQD/SDH (Uniprot ID Q9SQT8) as template, docking of 3-dehydroshikimate into the active site of the models as well as the crystal structure of PDB ID 2O7S, molecular dynamics simulation of protein-ligand interaction
additional information
EcDQD/SDH3 enzyme structure homology modeling using the structure of Arabidopsis thaliana AtDQD/SDH (Uniprot ID Q9SQT8) as template, docking of 3-dehydroshikimate into the active site of the models as well as the crystal structure of PDB ID 2O7S, molecular dynamics simulation of protein-ligand interaction
additional information
EcDQD/SDH3 enzyme structure homology modeling using the structure of Arabidopsis thaliana AtDQD/SDH (Uniprot ID Q9SQT8) as template, docking of 3-dehydroshikimate into the active site of the models as well as the crystal structure of PDB ID 2O7S, molecular dynamics simulation of protein-ligand interaction
additional information
EcDQD/SDH3 enzyme structure homology modeling using the structure of Arabidopsis thaliana AtDQD/SDH (Uniprot ID Q9SQT8) as template, docking of 3-dehydroshikimate into the active site of the models as well as the crystal structure of PDB ID 2O7S, molecular dynamics simulation of protein-ligand interaction
additional information
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EcDQD/SDH3 enzyme structure homology modeling using the structure of Arabidopsis thaliana AtDQD/SDH (Uniprot ID Q9SQT8) as template, docking of 3-dehydroshikimate into the active site of the models as well as the crystal structure of PDB ID 2O7S, molecular dynamics simulation of protein-ligand interaction
additional information
molecular docking calculations and molecular dynamics (MD) simulations for enzyme-substrate interaction and binding structure analysis, model of DHS/NADPH/MtbSDH ternary complex, wild-type and mutant enzymes, detailed overview. Lys69 plays a dual role, in positioning NADPH and in catalysis. Asp105 plays a crucial role in positioning both the epsilon-amino group of Lys69 and nicotinamide ring of NADPH for MtbSDH catalysis but makes no direct contribution to DHS binding. Ala213 is the selection key for NADPH binding with the nicotinamide ring in the proS, rather than proR, conformation in the MtbSDH complex. Residues Ser18, Thr65, Lys69, Gln243, and Gln247 forming hydrogen bonds to 3-dehydroshikimate (DHS)
additional information
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molecular docking calculations and molecular dynamics (MD) simulations for enzyme-substrate interaction and binding structure analysis, model of DHS/NADPH/MtbSDH ternary complex, wild-type and mutant enzymes, detailed overview. Lys69 plays a dual role, in positioning NADPH and in catalysis. Asp105 plays a crucial role in positioning both the epsilon-amino group of Lys69 and nicotinamide ring of NADPH for MtbSDH catalysis but makes no direct contribution to DHS binding. Ala213 is the selection key for NADPH binding with the nicotinamide ring in the proS, rather than proR, conformation in the MtbSDH complex. Residues Ser18, Thr65, Lys69, Gln243, and Gln247 forming hydrogen bonds to 3-dehydroshikimate (DHS)
additional information
only four amino acid residues likely to contribute to specificity for one substrate instead of the other, namely S336, S338, T381 and Y550, all of which would be in the direct vicinity of the quinate C1-hydroxyl. Amino acid S336 has previously been shown by mutational analysis to be critical for shikimate binding. The size of the amino acid side chain at position 381 is a key determinant of substrate specificity
additional information
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the conserved Lys69 plays an important role in the catalytic activity of Helicobacter pylori SDH, structure-function analysis using the structure of SDH in complex with shikimate and NADP+ (PDB ID 3PHI). Two-layered ONIOM-based quantum mechanics/molecular mechanics (QM/MM) calculation and molecular dynamics (MD) simulations are performed to explore the role of Lys69 in SDH activity, overview. In addition to act as a catalytic base, the conserved Lys69 plays an additional, important role in the maintenance of the substrate shikimate in the active site, facilitating the catalytic reaction between the cofactor NADP+ and shikimate. Shikimate forms hydrogen bonds with Ser16, Ser18, and Tyr210. The C3-hydroxyl group of shikimate is hydrogen bonded to the side chain amide group of Gln237. The C4-hydroxyl group of shikimate donates hydrogen bonds with both the side chain amide group of Asn90 and the carboxylate group of Asp105. The C5-hydroxyl group of shikimate makes hydrogen bonds with the side chain hydroxyl group of Thr65 and the side chain ammonium group of Lys69. Comparison of active site structures of wild-type and mutant K69A enzymes
additional information
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three-dimensional stucture homology modelling (PMDB ID PM0080741), model refinement and validation, overview
additional information
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three-dimensional protein structures homology modelling of the five putative poplar DQD/SDHs using Arabidopsis DQD/SDH enzyme structure, PDB ID c2o7qA, of the enzyme coupled with either 3-dehydroshikimate and tartrate or shikimate, as a template
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x * 30000, SDS-PAGE
?
-
x * 30000, SDS-PAGE
-
?
x * 31691, recombinant AroE, mass spectrometry
?
-
x * 27200, SDS-PAGE
-
?
-
x * 50000-60000, recombinant enzyme, SDS-PAGE
dimer
-
dimer
-
2 * 32000, SDS-PAGE, 2 * 29140, deduced from gene sequence
dimer
2 * 30202, calculated
dimer
-
2 * 30202, calculated
-
dimer
-
2 * 30000, native PAGE
dimer
-
2 * 30000, native PAGE
-
dimer
-
recombinant paralogue HI0607, SDS-PAGE and gel filtration
dimer
2 * 54150, recombinant AroE, mass spectrometry
dimer
-
2 * 54150, recombinant AroE, mass spectrometry
-
monomer
in solution
monomer
-
1 * 32000, SDS-PAGE
monomer
-
1 * 29400, mass spectrometry and gel filtration
monomer
-
1 * 29414, mass spectrometry
monomer
-
1 * 30000, native PAGE
monomer
-
1 * 30000, native PAGE
-
monomer
1 * 27000, recombinant AroE, SDS-PAGE, 1 * 27076, recombinant AroE, mass spectrometry
monomer
-
1 * 27000, recombinant AroE, SDS-PAGE, 1 * 27076, recombinant AroE, mass spectrometry
-
monomer
-
1 * 29000, SDS-PAGE
monomer
-
1 * 29000, SDS-PAGE
-
monomer
1 * 28889, calculated
monomer
-
1 * 28889, calculated
-
additional information
SDH enzymes exist in opened and closed conformational states. In the ternary structure of Aquifex aeolicus SDH (PDB ID 2HK9), three loops in the shikimate binding domain are shifted about 5 A toward the NADP++ binding site compared to their position in an unliganded structure of the same enzyme (PDB ID 2HK8). The closed form of the structure thus brings the bound shikimate and NADP+ molecules into close proximity, facilitating a hydride transfer between the shikimate C5-hydroxyl and C4 of the NADP+ nicotinamide ring
additional information
the SDH domain is connected via its N-terminus to the DHQ module
additional information
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structure analysis, dynamic light scattering measurements
additional information
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three-dimensional structure analysis of AroE
additional information
three-dimensional structure analysis of AroE
additional information
analysis of secondary structure
additional information
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analysis of secondary structure
additional information
the active subpocket 1 is formed by residues Val8, Ser16, Ser18, Asn63, Val64, Thr65, Lys69, Asn90, Asp105, and Gln237, subpocket 2 by residues Asp105, Ser129, Ala179, Thr180, Ser181, Leu184, Leu208, Tyr210, Gly230, Met233, and Leu234, and subpocket 3 by residues Gly125, Ala126, Gly127, Asn148, Arg149, Ser150, Thr180, Ser181, Ala182, and Pro189
additional information
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the active subpocket 1 is formed by residues Val8, Ser16, Ser18, Asn63, Val64, Thr65, Lys69, Asn90, Asp105, and Gln237, subpocket 2 by residues Asp105, Ser129, Ala179, Thr180, Ser181, Leu184, Leu208, Tyr210, Gly230, Met233, and Leu234, and subpocket 3 by residues Gly125, Ala126, Gly127, Asn148, Arg149, Ser150, Thr180, Ser181, Ala182, and Pro189
additional information
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analysis of secondary structure
-
additional information
the enzyme shows an alpha/beta sandwich with two distinct domains, responsible for binding substrate and the NADP cofactor, respectively, a phylogenetically conserved deep cleft on the protein surface corresponds to the enzyme active site, the structure reveals a topologically unique domain fold within the N-terminal segment of the polypeptide chain, which binds substrate and supports dimerization, homology modeling, overview
additional information
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the enzyme shows an alpha/beta sandwich with two distinct domains, responsible for binding substrate and the NADP cofactor, respectively, a phylogenetically conserved deep cleft on the protein surface corresponds to the enzyme active site, the structure reveals a topologically unique domain fold within the N-terminal segment of the polypeptide chain, which binds substrate and supports dimerization, homology modeling, overview
additional information
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the structure reveals an enzyme with a deep cleft, which contains the active site, formed at the junction of two domains. The C-terminal domain is easily recognizable as a Rossmann fold dinucleotide binding domain, responsible for binding the NADP cofactor. The N-terminal substrate binding and dimerization domain, an alpha-beta-alpha sandwich, represents a unique topological fold, structure modeling
additional information
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secondary structure analysis of ARoE, percentages for alpha-helix, beta-sheet, beta-turn, and random coil are 29.2%, 9.3%, 32.7%, and 28.8%, respectively, contains the highly conserved motif G-X-(N/S)-V-(T/S)-X-PX-K
additional information
three-dimensional structure analysis of wild-type and mutant enzymes with bound substrates, overview
additional information
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three-dimensional structure analysis of wild-type and mutant enzymes with bound substrates, overview
additional information
the overall structure of SDH comprises two alpha/beta domains linked centrally by two alpha-helices. A deep groove between these two domains contains the active site for the binding of substrate and cofactor
additional information
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the overall structure of SDH comprises two alpha/beta domains linked centrally by two alpha-helices. A deep groove between these two domains contains the active site for the binding of substrate and cofactor
additional information
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the DQD domain constitutes the N-terminal half of the protein and the SDH domain the C-terminal half. Three-dimensional protein structures homology modelling of the five putative poplar DQD/SDHs using Arabidopsis DQD/SDH enzyme structure, PDB ID c2o7qA, of the enzyme coupled with either 3-dehydroshikimate and tartrate or shikimate, as a template
additional information
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three-dimensional protein structures homology modelling of the five putative poplar DQD/SDHs using Arabidopsis DQD/SDH enzyme structure, PDB ID c2o7qA, of the enzyme coupled with either 3-dehydroshikimate and tartrate or shikimate, as a template
additional information
-
the DQD domain constitutes the N-terminal half of the protein and the SDH domain the C-terminal half. Three-dimensional protein structures homology modelling of the five putative poplar DQD/SDHs using Arabidopsis DQD/SDH enzyme structure, PDB ID c2o7qA, of the enzyme coupled with either 3-dehydroshikimate and tartrate or shikimate, as a template
-
additional information
-
three-dimensional protein structures homology modelling of the five putative poplar DQD/SDHs using Arabidopsis DQD/SDH enzyme structure, PDB ID c2o7qA, of the enzyme coupled with either 3-dehydroshikimate and tartrate or shikimate, as a template
-
additional information
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three-dimensional structure determination by homology modelling and validation
additional information
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three-dimensional structure determination by homology modelling and validation
-
additional information
-
structural modeling of TgSDH suggests that the protein's three large amino acid insertions form surface-exposed loops with alpha-helical character, structure modelling and structure comparisons, overview
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D423A
-
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, inactive mutant
D423N
-
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, highly reduced activity compared to the wild-type enzyme
H335A
-
site-directed mutagenesis, tenfold decrease in kcat value
K385A
-
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, highly reduced activity compared to the wild-type enzyme
K385N
-
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, highly reduced activity compared to the wild-type enzyme
K385N/D423N
-
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, highly reduced activity compared to the wild-type enzyme
N406A
-
site-directed mutagenesis, very strong decrease in kcat value
Q578L
-
site-directed mutagenesis, sixtyfold decrease in kcat value
Q582L
-
site-directed mutagenesis, very strong decrease in kcat value
S336A
-
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, reduced activity compared to the wild-type enzyme
S338A
-
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, reduced activity compared to the wild-type enzyme
S338G
site-directed mutagenesis, the mutant is not active with quinate like the wild-type
S338G/T381G
site-directed mutagenesis, the double mutant does not show improved enzymatic activity with quinate compared with the T381G mutant
T381G
site-directed mutagenesis, mutant shows increased activity with quinate compared to wild-type, it catalyzes the oxidation of quinate with a turnover rate of 8.8/s and a KM of 3.33 mM
T407A
-
site-directed mutagenesis, 6.5fold decrease in kcat value, increase in Km-value
T422S
-
site-directed mutagenesis, tenfold decrease in kcat value
Y550A
-
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, reduced activity compared to the wild-type enzyme
Y550F
-
site-directed mutagenesis of enzyme variant DELTA88DHQ-SDH, reduced activity compared to the wild-type enzyme
G338S/G381T/D483N/L484R/D485T
site-directed mutagenesis, mutant MTCsDQD/SDHb has a similar reduction activity of 3-DHS and had six times higher oxidation activity of SA than wild-type isozyme CsDQD/SDHb, suggesting that the mutation of residues Ser338 and NRT to Gly and DI/LD in the SDH unit is the reason for the low activity of CsDQD/SDHb, respectively
A243G
site-directed mutagenesis, the mutant shows altered cofactor specificity compared to wild-type enzyme
D195E
site-directed mutagenesis, the mutant shows altered cofactor specificity compared to wild-type enzyme
N149D
site-directed mutagenesis, the mutant shows altered cofactor specificity compared to wild-type enzyme
N149D/V152F
site-directed mutagenesis, the mutant shows altered cofactor specificity compared to wild-type enzyme
S131A
site-directed mutagenesis, the mutant shows altered cofactor specificity compared to wild-type enzyme
S131A/L135A
site-directed mutagenesis, the mutant shows altered cofactor specificity compared to wild-type enzyme
S131A/L135A/N149D/V152F
site-directed mutagenesis, the mutant shows altered cofactor specificity compared to wild-type enzyme
S131A/N149D/V152F
site-directed mutagenesis, the mutant shows altered cofactor specificity compared to wild-type enzyme
D103X
-
site-directed mutagenesis of paralogue HI0607, inactive mutant
K67H
-
site-directed mutagenesis of paralogue HI0607, inactive mutant
K69A
-
site-directed mutagenesis, the mutant shows significantly reduced the catalytic efficiency compared to wild-type enzyme
Q237A
-
site-directed mutagenesis
Q237K
-
site-directed mutagenesis
Q237N
-
site-directed mutagenesis
Y210A
-
site-directed mutagenesis
Y210S
-
site-directed mutagenesis
A213L
site-directed mutagenesis, analysis of substrate and cofactor binding compared to wild-type enzyme
D105A
-
the freeze-thaw method is able to yield the mutant protein in soluble form, after growth at 37°C for 24 h with IPTG induction of Escherichia coli C41 (DE3) cells harboring the recombinant plasmid
K69H
-
the freeze-thaw method is able to yield the mutant protein in soluble form, after growth at 37°C for 24 h with IPTG induction of Escherichia coli C41 (DE3) cells harboring the recombinant plasmid
K69I
-
the freeze-thaw method is able to yield the mutant protein in soluble form, after growth at 37°C for 24 h with IPTG induction of Escherichia coli C41 (DE3) cells harboring the recombinant plasmid
K69Q
-
the freeze-thaw method is able to yield the mutant protein in soluble form, after growth at 37°C for 24 h with IPTG induction of Escherichia coli C41 (DE3) cells harboring the recombinant plasmid
S275G
-
site-directed mutagenesis, the mutant shows only slightly reduced maximum activity with shikimate compared with wild-type PoptrSDH1
S275G/T318G
-
site-directed mutagenesis, the double mutant is well expressed in Escherichia coli and shows bona fide QDH activity besides its original SDH activity, which is severely reduced. Although the Ser275Gly/Thr318Gly double mutant is clearly sufficient to confer gain of activity with quinate, its activity is lower than the QDH activities of PintaQDH and PoptrQDH2 activity
T318G
-
site-directed mutagenesis, the Thr318Gly mutant yields only a very small amount of enzyme when recombinantly expressed in Escherichia coli
Y211F
results in a remarkable reduction in enzyme activity, leads to a significant decrease in kcat (345fold) and a minor increase in the Km (3fold) for shikimate. Tyr211 may play a major role in the catalytic process and a minor role in the initial substrate binding
T381A
-
site-directed mutagenesis, more than twentyfold decrease in kcat value
T381A
site-directed mutagenesis, the mutant accepts quinate as a substrate but is much less efficient than the T381G variant
T381S
-
site-directed mutagenesis, fourfold decrease in kcat value, slight decrease in Km value
T381S
site-directed mutagenesis, the mutant accepts quinate as a substrate but is much less efficient than the T381G variant
D105N
-
the freeze-thaw method is able to yield the mutant protein in soluble form, after growth at 37°C for 24 h with IPTG induction of Escherichia coli C41 (DE3) cells harboring the recombinant plasmid
D105N
site-directed mutagenesis, analysis of substrate and cofactor binding compared to wild-type enzyme
K69A
-
the freeze-thaw method is able to yield the mutant protein in soluble form, after growth at 37°C for 24 h with IPTG induction of Escherichia coli C41 (DE3) cells harboring the recombinant plasmid. Best recombinant protein expression protocol of the K69A mutant in insoluble form is using Escherichia coli C41(DE3) strain, grown at 37°C for 24 h after induction with 1 mM IPTG, and cell disruption by sonication
K69A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme, overview
K69A
site-directed mutagenesis, analysis of substrate and cofactor binding compared to wild-type enzyme
additional information
-
construction of deletion variant DELTA88DHQ-SDH, thermal denaturation analysis, overview
additional information
absence of the T381 side chain creates sufficient space in the active site to accommodate the quinate C1-hydroxyl. The K385 and D423 catalytic dyad which interacts with C4-OH and participates in proton transfer during the reduction/oxidation of NADP+/NADPH is retained in the T381G mutant
additional information
referring to the model of Arabidopsis thaliana protein crystal structure, the amino acid residue sites of Gly338, Gly381, Asp483, Leu484, and Asp485 in CsDQD/SDHb are mutated to Ser338, Thr381, Asn483, Arg484, and Thr485, respectively, the mutant protein is named MTCsDQD/SDHb
additional information
-
referring to the model of Arabidopsis thaliana protein crystal structure, the amino acid residue sites of Gly338, Gly381, Asp483, Leu484, and Asp485 in CsDQD/SDHb are mutated to Ser338, Thr381, Asn483, Arg484, and Thr485, respectively, the mutant protein is named MTCsDQD/SDHb
additional information
steady state cytosolic free and whole cell NADPH/NADP ratio in different Saccharomycs cerevisiae strains, with or without recombinant expression of shikimate dehydrogenase from Escherichia coli, thermodynamics and kinetics, overview
additional information
invertion of the cofactor specificity from NADP+ to NAD+ on the Escherichia coli wild-type enzyme, effect of consensus mutations, overview. Mutant structure modeling
additional information
-
invertion of the cofactor specificity from NADP+ to NAD+ on the Escherichia coli wild-type enzyme, effect of consensus mutations, overview. Mutant structure modeling
additional information
ydiB-encoded enzyme knockout in Escherichia coli strain PB12
additional information
-
ydiB-encoded enzyme knockout in Escherichia coli strain PB12
-
additional information
-
cytosolic isoform cannot complement loss of the plastidial isoform
additional information
cytosolic isoform cannot complement loss of the plastidial isoform
additional information
cytosolic isoform cannot complement loss of the plastidial isoform
additional information
-
expression of endogenous DHD/SHD-1 is suppressed by RNAi in transgenic tobacco plants, the transgenic lines with less than 40% of wild-type activity display severe growth retardation and reduced content of aromatic amino acids and downstream products such as cholorogenic acid and lignin, but accumulation of dehydroquinate and shikimate, possibly due to existence of a parallel extra-plastidic shikimate pathway into which dehydroquinate is diverted with a second gene DHD/SHD-2 in tobacco lacking a plastidic targeting sequence, the cytosolic shikimate synthesis cannot complement loss of the plastidial pathway, phenotype, overview
additional information
expression of endogenous DHD/SHD-1 is suppressed by RNAi in transgenic tobacco plants, the transgenic lines with less than 40% of wild-type activity display severe growth retardation and reduced content of aromatic amino acids and downstream products such as cholorogenic acid and lignin, but accumulation of dehydroquinate and shikimate, possibly due to existence of a parallel extra-plastidic shikimate pathway into which dehydroquinate is diverted with a second gene DHD/SHD-2 in tobacco lacking a plastidic targeting sequence, the cytosolic shikimate synthesis cannot complement loss of the plastidial pathway, phenotype, overview
additional information
expression of endogenous DHD/SHD-1 is suppressed by RNAi in transgenic tobacco plants, the transgenic lines with less than 40% of wild-type activity display severe growth retardation and reduced content of aromatic amino acids and downstream products such as cholorogenic acid and lignin, but accumulation of dehydroquinate and shikimate, possibly due to existence of a parallel extra-plastidic shikimate pathway into which dehydroquinate is diverted with a second gene DHD/SHD-2 in tobacco lacking a plastidic targeting sequence, the cytosolic shikimate synthesis cannot complement loss of the plastidial pathway, phenotype, overview
additional information
-
suppression of shikimate dehydrogenase activity by RNAi. Transgenic lines with less than 40% of wild-type activity display severe growth retardation and reduced content of aromatic amino acids and downstream products such as cholorogenic acid and lignin. Dehydroquinate, the substrate of the enzyme, accumulates, and due to a second, cytosolic enzyme, the product, shikimate accumulates
additional information
suppression of shikimate dehydrogenase activity by RNAi. Transgenic lines with less than 40% of wild-type activity display severe growth retardation and reduced content of aromatic amino acids and downstream products such as cholorogenic acid and lignin. Dehydroquinate, the substrate of the enzyme, accumulates, and due to a second, cytosolic enzyme, the product, shikimate accumulates
additional information
suppression of shikimate dehydrogenase activity by RNAi. Transgenic lines with less than 40% of wild-type activity display severe growth retardation and reduced content of aromatic amino acids and downstream products such as cholorogenic acid and lignin. Dehydroquinate, the substrate of the enzyme, accumulates, and due to a second, cytosolic enzyme, the product, shikimate accumulates
additional information
the shikimate C1-carboxyl is formed by the phenol hydroxyl of a tyrosine. Substitution of this residue in Staphyococcus epidermidis SDH causes a substantial reduction in turnover rate
additional information
-
the shikimate C1-carboxyl is formed by the phenol hydroxyl of a tyrosine. Substitution of this residue in Staphyococcus epidermidis SDH causes a substantial reduction in turnover rate
-
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Jacobson, J.W.; Hart, B.A.; Doy, C.H.; Giles, N.H.
Purification and stability of the multienzyme complex encoded in the arom gene cluster of Neurospora crassa
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Neurospora crassa
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Purification and characterization of 3-dehydroquinate hydrolase and shikmate oxidoreductase. Evidence for a bifunctional enzyme
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Physcomitrium patens
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The purification of shikimate dehydrogenase from Escherichia coli
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Escherichia coli
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Partial purification and some properties of shikimate dehydrogenase from tomatoes
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Solanum lycopersicum
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Koshiba, T.
Purification of two forms of the associated 3-dehydroquinate hydro-lyase and shikimate:NADP+ oxidoreductase in Phaseolus mungo seedlings
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Vigna mungo
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5-Dehydroshikimate reductase in the tea plant (Camellia sinensis L.). Properties and distribution
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Camellia sinensis
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Pisum sativum
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-
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Aromatic biosynthesis. XIV. 5-dehydroshikimic reductase
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787-795
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Escherichia coli
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Purification and properties of shikimate dehydrogenase from cucumber (Cucumis sativus L.).
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Capsicum annuum
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A thermostable shikimate 5-dehydrogenase from the archaeon Archaeoglobus fulgidus
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Archaeoglobus fulgidus
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Haemophilus influenzae, Haemophilus influenzae (P43876)
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Cloning and expression of functional shikimate dehydrogenase (EC 1.1.1.25) from Mycobacterium tuberculosis H37Rv
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Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
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Crystal structure of shikimate 5-dehydrogenase (SDH) bound to NADP: insights into function and evolution
Structure
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Methanocaldococcus jannaschii (Q58484), Methanocaldococcus jannaschii
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Cloning, expression, purification and preliminary crystallographic characterization of a shikimate dehydrogenase from Corynebacterium glutamicum
Acta Crystallogr. Sect. F
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Corynebacterium glutamicum
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Structure of Arabidopsis dehydroquinate dehydratase-shikimate dehydrogenase and implications for metabolic channeling in the shikimate pathway
Biochemistry
45
10406
2006
Arabidopsis thaliana
brenda
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Purification and properties of NADP-dependent shikimate dehydrogenase from Gluconobacter oxydans IFO 3244 and its application to enzymatic shikimate production
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Gluconobacter oxydans, Gluconobacter oxydans IFO 3244
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Biochemical characterization and inhibitor discovery of shikimate dehydrogenase from Helicobacter pylori
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Helicobacter pylori (Q56S04), Helicobacter pylori, Helicobacter pylori SS1 (Q56S04)
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Mycobacterium tuberculosis
brenda
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Crystal structure of a novel shikimate dehydrogenase from Haemophilus influenzae
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Haemophilus influenzae
brenda
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Functional shikimate dehydrogenase from Mycobacterium tuberculosis H37Rv: purification and characterization
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Mycobacterium tuberculosis (A5U5Q2), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (A5U5Q2), Mycobacterium tuberculosis H37Rv
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Vogan, E.
Shikimate dehydrogenase structure reveals novel fold
Structure
11
902-903
2003
Methanocaldococcus jannaschii
brenda
Ding, L.; Hofius, D.; Hajirezaei, M.R.; Fernie, A.R.; Boernke, F.; Sonnewald, U.
Functional analysis of the essential bifunctional tobacco enzyme 3-dehydroquinate dehydratase/shikimate dehydrogenase in transgenic tobacco plants
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Nicotiana tabacum, Nicotiana tabacum (Q6PUF9), Nicotiana tabacum (Q6PUG0)
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1.6 A structure of an NAD(+)-dependent quinate dehydrogenase from Corynebacterium glutamicum
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Corynebacterium glutamicum (Q9X5C9)
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Kinetic and chemical mechanisms of shikimate dehydrogenase from Mycobacterium tuberculosis
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Mycobacterium tuberculosis (A5U5Q2), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (A5U5Q2)
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Structural and biochemical analyses of shikimate dehydrogenase AroE from Aquifex aeolicus: implications for the catalytic mechanism
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Aquifex aeolicus (O67049), Aquifex aeolicus
brenda
Singh, S.A.; Christendat, D.
The DHQ-dehydroshikimate-SDH-shikimate-NADP(H) complex: insights into metabolite transfer in the shikimate pathway
Cryst. Growth Des.
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Arabidopsis thaliana
-
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Bagautdinov, B.; Kunishima, N.
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Thermus thermophilus (Q5SJF8), Thermus thermophilus HB8 / ATCC 27634 / DSM 579 (Q5SJF8)
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Structural studies of shikimate 5-dehydrogenase from Mycobacterium tuberculosis
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Mycobacterium tuberculosis
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Singh, S.; Stavrinides, J.; Christendat, D.; Guttman, D.S.
A phylogenomic analysis of the shikimate dehydrogenases reveals broadscale functional diversification and identifies one functionally distinct subclass
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25
2221-2232
2008
Pseudomonas putida (Q88GF6), Pseudomonas putida (Q88IJ7), Pseudomonas putida (Q88JP1), Pseudomonas putida (Q88K85), Pseudomonas putida (Q88RQ5), Pseudomonas putida KT2440 (Q88IJ7), Pseudomonas putida KT2440 (Q88RQ5), Pseudomonas putida KT 2240 (Q88GF6), Pseudomonas putida KT 2240 (Q88IJ7), Pseudomonas putida KT 2240 (Q88JP1), Pseudomonas putida KT 2240 (Q88K85), Pseudomonas putida KT 2240 (Q88RQ5)
brenda
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X-ray crystallographic and enzymatic analyses of shikimate dehydrogenase from Staphylococcus epidermidis
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Staphylococcus epidermidis RP62A (Q5HNV1)
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45
200-205
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Mycobacterium tuberculosis
brenda
Barcellos, G.B.; Caceres, R.A.; de Azevedo, W.F.
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15
147-155
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Bacillus anthracis
brenda
Cao, S.; Hu, Z.; Zheng, Y.; Lu, B.
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58
5801-5805
2010
Fragaria x ananassa
brenda
Rodrigues, V.S.; Breda, A.; Santos, D.S.; Basso, L.A.
The conserved Lysine69 residue plays a catalytic role in Mycobacterium tuberculosis shikimate dehydrogenase
BMC Res. Notes
2
227
2009
no activity in Homo sapiens, Mycobacterium tuberculosis (P95001), Mycobacterium tuberculosis
brenda
Lee, H.H.
Overexpression, crystallization and preliminary X-ray crystallographic analysis of shikimate dehydrogenase from Archaeoglobus fulgidus
Acta Crystallogr. Sect. F
67
1556-1558
2011
Archaeoglobus fulgidus (O27957), Archaeoglobus fulgidus, Archaeoglobus fulgidus ATCC 49558 (O27957)
brenda
Lee, H.H.
Overexpression, crystallization, and preliminary X-ray crystallographic analysis of shikimate dehydrogenase from Thermotoga maritima
Acta Crystallogr. Sect. F
67
824-826
2011
Thermotoga maritima (Q9WYI1), Thermotoga maritima, Thermotoga maritima ATCC 43589 (Q9WYI1)
brenda
Kubota, T.; Tanaka, Y.; Hiraga, K.; Inui, M.; Yukawa, H.
Characterization of shikimate dehydrogenase homologues of Corynebacterium glutamicum
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97
8139-8149
2013
Corynebacterium glutamicum (A4QB65), Corynebacterium glutamicum (A4QEK4), Corynebacterium glutamicum, Corynebacterium glutamicum JCM 18229 (A4QB65), Corynebacterium glutamicum JCM 18229 (A4QEK4)
brenda
Lee, H.H.
High-resolution structure of shikimate dehydrogenase from Thermotoga maritima reveals a tightly closed conformation
Mol. Cells
33
229-233
2012
Thermotoga maritima (Q9WYI1), Thermotoga maritima, Thermotoga maritima ATCC 43589 (Q9WYI1)
brenda
Peek, J.; Christendat, D.
The shikimate dehydrogenase family: functional diversity within a conserved structural and mechanistic framework
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566
85-99
2015
Escherichia coli, Helicobacter pylori, Staphylococcus aureus, Mycobacterium tuberculosis, Populus trichocarpa, Corynebacterium glutamicum (A4QB65), Archaeoglobus fulgidus (O27957), Aquifex aeolicus (O67049), Aspergillus nidulans (P07547), Staphylococcus epidermidis (Q5HNV1), Toxoplasma gondii (Q6W3D0), Pseudomonas putida (Q88IJ7), Arabidopsis thaliana (Q9SQT8), Archaeoglobus fulgidus ATCC 49558 (O27957), Aspergillus nidulans FGSC A4 (P07547), Staphylococcus epidermidis ATCC 35984 (Q5HNV1), Pseudomonas putida KT 2240 (Q88IJ7)
brenda
Prus-Glowacki, W.; Sukovata, L.; Lewandowska-Wosik, A.; Nowak-Bzowy, R.
Shikimate dehydrogenase (E.C. 1.1.1.25 ShDH) alleles as potential markers for flowering phenology in Pinus sylvestris
Dendrobiology
73
153-162
2015
Pinus sylvestris
-
brenda
Guo, J.; Carrington, Y.; Alber, A.; Ehlting, J.
Molecular characterization of quinate and shikimate metabolism in Populus trichocarpa
J. Biol. Chem.
289
23846-23858
2014
Populus trichocarpa, Populus trichocarpa Nisqually-1
brenda
Peek, J.; Shi, T.; Christendat, D.
Identification of novel polyphenolic inhibitors of shikimate dehydrogenase (AroE)
J. Biomol. Screen.
19
1090-1098
2014
Pseudomonas putida (Q88RQ5), Pseudomonas putida, Arabidopsis thaliana (Q9SQT8), Arabidopsis thaliana, Pseudomonas putida KT 2240 (Q88RQ5)
brenda
Bontpart, T.; Marlin, T.; Vialet, S.; Guiraud, J.L.; Pinasseau, L.; Meudec, E.; Sommerer, N.; Cheynier, V.; Terrier, N.
Two shikimate dehydrogenases, VvSDH3 and VvSDH4, are involved in gallic acid biosynthesis in grapevine
J. Exp. Bot.
67
3537-3550
2016
Vitis vinifera (A0A168S2B8), Vitis vinifera (A0A168S2G5), Vitis vinifera (A0A168S2H6), Vitis vinifera (D7TUX1)
brenda
Peek, J.; Castiglione, G.; Shi, T.; Christendat, D.
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Mol. Biochem. Parasitol.
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Toxoplasma gondii
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Avitia-Dominguez, C.; Sierra-Campos, E.; Salas-Pacheco, J.M.; Najera, H.; Rojo-Dominguez, A.; Cisneros-Martinez, J.; Tellez-Valencia, A.
Inhibition and biochemical characterization of methicillin-resistant Staphylococcus aureus shikimate dehydrogenase: an in silico and kinetic study
Molecules
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Staphylococcus aureus, Staphylococcus aureus ATCC MRSA252
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Li, Z.; Liu, Y.; Bai, X.; Deng, Q.; Wang, J.; Zhang, G.; Xiao, C.; Mei, Y.; Wang, Y.
SAR studies on 1,2,4-triazolo[3,4-b][1,3,4]thiadiazoles as inhibitors of Mtb shikimate dehydrogenase for the development of novel antitubercular agents
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Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
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Zhang, J.; ten Pierick, A.; van Rossum, H.M.; Seifar, R.M.; Ras, C.; Daran, J.M.; Heijnen, J.J.; Wahl, S.A.
Determination of the cytosolic NADPH/NADP ratio in Saccharomyces cerevisiae using shikimate dehydrogenase as sensor reaction
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Escherichia coli (P15770)
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Habashi, R.; Hacham, Y.; Dhakarey, R.; Matityahu, I.; Holland, D.; Tian, L.; Amir, R.
Elucidating the role of shikimate dehydrogenase in controlling the production of anthocyanins and hydrolysable tannins in the outer peels of pomegranate
BMC Plant Biol.
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Punica granatum (A0A6P8EJ47), Punica granatum
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Enriquez-Mendiola, D.; Tellez-Valencia, A.; Sierra-Campos, E.; Campos-Almazan, M.; Valdez-Solana, M.; Gomez Palacio-Gastelum, M.; Avitia-Dominguez, C.
Kinetic and molecular dynamic studies of inhibitors of shikimate dehydrogenase from methicillin-resistant Staphylococcus aureus
Chem. Biol. Drug Des.
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2019
Staphylococcus aureus
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Li, J.; Wu, G.; Fu, Q.; Ge, H.; Liu, S.; Li, X.; Cheng, B.
Exploring the influence of conserved lysine69 on the catalytic activity of the Helicobacter pylori shikimate dehydrogenase a combined QM/MM and MD simulations
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Helicobacter pylori
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Huang, K.; Li, M.; Liu, Y.; Zhu, M.; Zhao, G.; Zhou, Y.; Zhang, L.; Wu, Y.; Dai, X.; Xia, T.; Gao, L.
Functional analysis of 3-dehydroquinate dehydratase/shikimate dehydrogenases involved in shikimate pathway in Camellia sinensis
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Camellia sinensis (A0A3G3BK08), Camellia sinensis
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Hyskova, V.; Pliskova, V.; Cerveny, V.; Ryslava, H.
NADP-dependent enzymes are involved in response to salt and hypoosmotic stress in cucumber plants
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Cucumis sativus (A0A0A0LQ48)
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Wang, K.; Zhu, M.; Tang, Y.; Liu, J.; Yan, F.; Yu, Z.; Zhu, J.
Integration of virtual screening and susceptibility test to discover active-site subpocket-specific biogenic inhibitors of Helicobacter pylori shikimate dehydrogenase
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Helicobacter pylori (Q56S04), Helicobacter pylori
brenda
Skariyachan, S.; Manjunath, M.; Bachappanavar, N.
Screening of potential lead molecules against prioritised targets of multi-drug-resistant-Acinetobacter baumannii - insights from molecular docking, molecular dynamic simulations and in vitro assays
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Acinetobacter baumannii
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Punkvang, A.; Kamsri, P.; Mulholland, A.; Spencer, J.; Hannongbua, S.; Pungpo, P.
Simulations of shikimate dehydrogenase from Mycobacterium tuberculosis in complex with 3-dehydroshikimate and NADPH suggest strategies for MtbSDH inhibition
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no activity in Homo sapiens, Mycobacterium tuberculosis (A0A045GU47), Mycobacterium tuberculosis
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Diaz-Quiroz, D.C.; Cardona-Felix, C.S.; Viveros-Ceballos, J.L.; Reyes-Gonzalez, M.A.; Bolivar, F.; Ordonez, M.; Escalante, A.
Synthesis, biological activity and molecular modelling studies of shikimic acid derivatives as inhibitors of the shikimate dehydrogenase enzyme of Escherichia coli
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2018
Escherichia coli (P15770), Escherichia coli
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Garcia, S.; Flores, N.; De Anda, R.; Hernandez, G.; Gosset, G.; Bolivar, F.; Escalante, A.
The role of the ydiB gene, which encodes quinate/shikimate dehydrogenase, in the production of quinic, dehydroshikimic and shikimic acids in a PTS-strain of Escherichia coli
J. Mol. Microbiol. Biotechnol.
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Escherichia coli (P0A6D5), Escherichia coli PB12 (P0A6D5)
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Gritsunov, A.; Peek, J.; Diaz Caballero, J.; Guttman, D.; Christendat, D.
Structural and biochemical approaches uncover multiple evolutionary trajectories of plant quinate dehydrogenases
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Arabidopsis thaliana (Q9SQT8)
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Carrington, Y.; Guo, J.; Le, C.H.; Fillo, A.; Kwon, J.; Tran, L.T.; Ehlting, J.
Evolution of a secondary metabolic pathway from primary metabolism shikimate and quinate biosynthesis in plants
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Chlamydomonas reinhardtii, Physcomitrium patens, Pinus taeda, Populus trichocarpa, Rhodopirellula baltica, Selaginella moellendorffii
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Tahara, K.; Nishiguchi, M.; Funke, E.; Miyazawa, S.I.; Miyama, T.; Milkowski, C.
Dehydroquinate dehydratase/shikimate dehydrogenases involved in gallate biosynthesis of the aluminum-tolerant tree species Eucalyptus camaldulensis
Planta
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Eucalyptus camaldulensis (A0A5H2WVH6), Eucalyptus camaldulensis (A0A5H2WZU5), Eucalyptus camaldulensis (A0A5H2X4C4), Eucalyptus camaldulensis
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Garcia-Guevara, F.; Bravo, I.; Martinez-Anaya, C.; Segovia, L.
Cofactor specificity switch in shikimate dehydrogenase by rational design and consensus engineering
Protein Eng. Des. Sel.
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2017
Escherichia coli (P15770), Escherichia coli
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