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show all sequences of 1.1.1.B61

Molecular characterization of quinate and shikimate metabolism in Populus trichocarpa

Guo, J.; Carrington, Y.; Alber, A.; Ehlting, J.; J. Biol. Chem. 289, 23846-23858 (2014)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
recombinant His6-tagged DQD/SDH isozyme 5 overexpression in Escherichia coli strain M15
Populus trichocarpa
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
Michaelis-Menten kinetics
Populus trichocarpa
0.321
-
shikimate
with NADP+, pH 8.5, 22C, recombinant His-tagged Poptr1
Populus trichocarpa
0.346
-
shikimate
with NAD+, pH 8.5, 22C, recombinant His-tagged Poptr1
Populus trichocarpa
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
3-dehydroquinate
Populus trichocarpa
-
3-dehydroshikimate + H2O
-
-
r
3-dehydroshikimate + NADPH
Populus trichocarpa
-
shikimate + NADP+
-
-
r
additional information
Populus trichocarpa
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
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Populus trichocarpa
-
trees grown in a field at the University of Victoria, Victoria, British Columbia, Canada
-
Populus trichocarpa Nisqually-1
-
trees grown in a field at the University of Victoria, Victoria, British Columbia, Canada
-
Purification (Commentary)
Commentary
Organism
recombinant His6-tagged DQD/SDH isozyme 5 from Escherichia coli strain M15 by nickel affinity chromatography
Populus trichocarpa
Source Tissue
Source Tissue
Commentary
Organism
Textmining
bark
-
Populus trichocarpa
-
leaf
-
Populus trichocarpa
-
additional information
poplar DQD/SDHs have distinct expression profiles, organ-specific expression of poplar DQD/SDHs, overview
Populus trichocarpa
-
phloem
-
Populus trichocarpa
-
xylem
-
Populus trichocarpa
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3-dehydroquinate
-
740724
Populus trichocarpa
3-dehydroshikimate + H2O
-
-
-
r
3-dehydroshikimate + NADPH
-
740724
Populus trichocarpa
shikimate + NADP+
-
-
-
r
3-dehydroshikimate + NADPH
SDH reaction
740724
Populus trichocarpa
shikimate + NADP+
-
-
-
r
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
740724
Populus trichocarpa
?
-
-
-
-
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
740724
Populus trichocarpa
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
More
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
Populus trichocarpa
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
22
-
assay at room temperature
Populus trichocarpa
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.5
-
assay at
Populus trichocarpa
Cofactor
Cofactor
Commentary
Organism
Structure
additional information
for Poptr5, no activity with shikimate is detectable in the presence of NAD+ even with elevated enzyme concentrations
Populus trichocarpa
NADP+
-
Populus trichocarpa
NADPH
-
Populus trichocarpa
Cloned(Commentary) (protein specific)
Commentary
Organism
recombinant His6-tagged DQD/SDH isozyme 5 overexpression in Escherichia coli strain M15
Populus trichocarpa
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
additional information
for Poptr5, no activity with shikimate is detectable in the presence of NAD+ even with elevated enzyme concentrations
Populus trichocarpa
NADP+
-
Populus trichocarpa
NADPH
-
Populus trichocarpa
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
Michaelis-Menten kinetics
Populus trichocarpa
0.321
-
shikimate
with NADP+, pH 8.5, 22C, recombinant His-tagged Poptr1
Populus trichocarpa
0.346
-
shikimate
with NAD+, pH 8.5, 22C, recombinant His-tagged Poptr1
Populus trichocarpa
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
3-dehydroquinate
Populus trichocarpa
-
3-dehydroshikimate + H2O
-
-
r
3-dehydroshikimate + NADPH
Populus trichocarpa
-
shikimate + NADP+
-
-
r
additional information
Populus trichocarpa
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
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His6-tagged DQD/SDH isozyme 5 from Escherichia coli strain M15 by nickel affinity chromatography
Populus trichocarpa
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
bark
-
Populus trichocarpa
-
leaf
-
Populus trichocarpa
-
additional information
poplar DQD/SDHs have distinct expression profiles, organ-specific expression of poplar DQD/SDHs, overview
Populus trichocarpa
-
phloem
-
Populus trichocarpa
-
xylem
-
Populus trichocarpa
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3-dehydroquinate
-
740724
Populus trichocarpa
3-dehydroshikimate + H2O
-
-
-
r
3-dehydroshikimate + NADPH
-
740724
Populus trichocarpa
shikimate + NADP+
-
-
-
r
3-dehydroshikimate + NADPH
SDH reaction
740724
Populus trichocarpa
shikimate + NADP+
-
-
-
r
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
740724
Populus trichocarpa
?
-
-
-
-
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
740724
Populus trichocarpa
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
More
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
Populus trichocarpa
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
22
-
assay at room temperature
Populus trichocarpa
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.5
-
assay at
Populus trichocarpa
General Information
General Information
Commentary
Organism
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
Populus trichocarpa
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
Populus trichocarpa
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
Populus trichocarpa
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
Populus trichocarpa
General Information (protein specific)
General Information
Commentary
Organism
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
Populus trichocarpa
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
Populus trichocarpa
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
Populus trichocarpa
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
Populus trichocarpa
Other publictions for EC 1.1.1.B61
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
739956
Peek
The shikimate dehydrogenase fa ...
Arabidopsis thaliana, Populus trichocarpa
Arch. Biochem. Biophys.
566
85-99
2015
-
-
-
1
-
-
-
4
-
-
-
2
-
2
-
-
-
-
-
-
-
-
4
2
2
-
-
2
2
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
4
-
-
-
2
-
-
-
-
-
-
-
-
4
2
2
-
-
2
2
-
-
-
-
5
5
-
-
-
740724
Guo
Molecular characterization of ...
Populus trichocarpa, Populus trichocarpa Nisqually-1
J. Biol. Chem.
289
23846-23858
2014
-
-
1
-
-
-
-
3
-
-
-
3
-
2
-
-
1
-
-
5
-
-
5
1
1
-
-
-
1
-
-
3
-
-
-
-
-
1
3
-
-
-
-
-
-
3
-
-
-
3
-
-
-
1
-
5
-
-
5
1
1
-
-
-
1
-
-
-
-
4
4
-
-
-
740771
Peek
Identification of novel polyph ...
Arabidopsis thaliana
J. Biomol. Screen.
19
1090-1098
2014
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-
1
1
-
-
3
-
-
-
-
1
-
5
-
-
1
-
-
-
-
-
2
-
1
-
-
-
1
-
-
2
-
-
2
-
-
1
2
1
-
-
2
3
-
-
-
-
-
1
-
-
-
1
-
-
-
-
2
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-