BRENDA - Enzyme Database show
show all sequences of 1.3.1.78

Non-plastidic, tyrosine-insensitive prephenate dehydrogenases from legumes

Schenck, C.A.; Chen, S.; Siehl, D.L.; Maeda, H.A.; Nat. Chem. Biol. 11, 52-57 (2015)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene ADH1, phylogenetic analysis; gene ADH2, phylogenetic analysis
Arabidopsis thaliana
Inhibitors
Inhibitors
Commentary
Organism
Structure
L-tyrosine
strong inhibition; strong inhibition
Arabidopsis thaliana
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
chloroplast
;
Arabidopsis thaliana
9507
-
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-arogenate + NADP+
Arabidopsis thaliana
-
L-tyrosine + NADPH + CO2
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Arabidopsis thaliana
Q944B6
-
-
Arabidopsis thaliana
Q9LMR3
-
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
leaf
;
Arabidopsis thaliana
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-arogenate + NADP+
-
745837
Arabidopsis thaliana
L-tyrosine + NADPH + CO2
-
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
NADP+
;
Arabidopsis thaliana
Cloned(Commentary) (protein specific)
Commentary
Organism
gene ADH1, phylogenetic analysis
Arabidopsis thaliana
gene ADH2, phylogenetic analysis
Arabidopsis thaliana
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADP+
-
Arabidopsis thaliana
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
L-tyrosine
strong inhibition
Arabidopsis thaliana
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
chloroplast
-
Arabidopsis thaliana
9507
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-arogenate + NADP+
Arabidopsis thaliana
-
L-tyrosine + NADPH + CO2
-
-
?
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
leaf
-
Arabidopsis thaliana
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-arogenate + NADP+
-
745837
Arabidopsis thaliana
L-tyrosine + NADPH + CO2
-
-
-
?
General Information
General Information
Commentary
Organism
evolution
prephenate dehydrogenases (TyrAps, also known as PDHs) from two legumes, Glycine max (soybean) and Medicago truncatula, are phylogenetically distinct from canonical plant ADH enzymes, prefer prephenate to arogenate substrate, localize outside of the plastids and are not inhibited by L-Tyr. Diversification of primary metabolic Tyr pathway via an alternative cytosolic PDH pathway in plants, phylogenetic and biochemical differentiation of ADHs and PDHs; prephenate dehydrogenases (TyrAps, also known as PDHs) from two legumes, Glycine max (soybean) and Medicago truncatula, are phylogenetically distinct from canonical plant ADH enzymes, prefer prephenate to arogenate substrate, localize outside of the plastids and are not inhibited by L-Tyr. Diversification of primary metabolic Tyr pathway via an alternative cytosolic PDH pathway in plants, phylogenetic and biochemical differentiation of ADHs and PDHs
Arabidopsis thaliana
metabolism
in plants, L-Tyr is synthe­sized in the plastids via the arogenate dehydrogenase pathway, in which prephenate is first converted to arogenate by prephenate aminotransferase, EC 2.6.1.7, and then to L-Tyr by enzyme ADH; in plants, L-Tyr is synthe­sized in the plastids via the arogenate dehydrogenase pathway, in which prephenate is first converted to arogenate by prephenate aminotransferase, EC 2.6.1.7, and then to L-Tyr by enzyme ADH
Arabidopsis thaliana
General Information (protein specific)
General Information
Commentary
Organism
evolution
prephenate dehydrogenases (TyrAps, also known as PDHs) from two legumes, Glycine max (soybean) and Medicago truncatula, are phylogenetically distinct from canonical plant ADH enzymes, prefer prephenate to arogenate substrate, localize outside of the plastids and are not inhibited by L-Tyr. Diversification of primary metabolic Tyr pathway via an alternative cytosolic PDH pathway in plants, phylogenetic and biochemical differentiation of ADHs and PDHs
Arabidopsis thaliana
metabolism
in plants, L-Tyr is synthe­sized in the plastids via the arogenate dehydrogenase pathway, in which prephenate is first converted to arogenate by prephenate aminotransferase, EC 2.6.1.7, and then to L-Tyr by enzyme ADH
Arabidopsis thaliana
Other publictions for EC 1.3.1.78
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)
745837
Schenck
Non-plastidic, tyrosine-insen ...
Arabidopsis thaliana
Nat. Chem. Biol.
11
52-57
2015
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700819
Rippert
Tyrosine and phenylalanine are ...
Arabidopsis thaliana
Plant Physiol.
149
1251-1260
2009
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677163
Legrand
Biochemical characterization a ...
Synechocystis sp.
Structure
14
767-776
2006
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654548
Bonner
A core catalytic domain of the ...
Anabaena sp., Chlorella sorokiniana, Fischerella sp., Porphyridium purpureum, Prochlorothrix hollandica, Synechococcus elongatus PCC 6301, Synechocystis sp., Synechocystis sp. PCC 6803, Synechocystis sp. PCC 6902
Biochem. J.
382
279-291
2004
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2
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27
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1
27
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390801
Rippert
Molecular and biochemical char ...
Arabidopsis thaliana
Plant Mol. Biol.
48
361-368
2002
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655440
Rippert
Purification and kinetic analy ...
Arabidopsis thaliana
Eur. J. Biochem.
269
4753-4761
2002
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5
5
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2
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18
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18
5
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2
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3
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390805
Bonner
-
Distinctive enzymes of aromati ...
Chlorella sorokiniana, Nicotiana sylvestris
Plant Cell Physiol.
36
1013-1022
1995
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2
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390781
Bonner
Arogenate dehydrogenase ...
Brevibacterium flavum, Corynebacterium glutamicum, Euglena gracilis, Nicotiana sylvestris, Phenylobacterium immobile, Sorghum bicolor, Streptomyces phaeochromogenes, Vigna radiata, Zea mays
Methods Enzymol.
142
488-494
1987
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20
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390788
Connelly
Tyrosine biosynthesis in Sorgh ...
Sorghum bicolor
Z. Naturforsch. C
41
69-78
1986
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390560
Byng
Evolutionary implications of f ...
Acinetobacter calcoaceticus, Acinetobacter lwoffii, Acinetobacter sp., Acinetobacter sp. C1W
Arch. Microbiol.
143
122-129
1985
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390793
Keller
Aromatic amino acid biosynthes ...
Pseudomonas sp., Pseudomonas sp. CBS3
Syst. Appl. Microbiol.
4
27-33
1983
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390794
Gaines
L-tyrosine regulation and bios ...
Nicotiana sylvestris
Planta
156
233-240
1982
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390796
Keller
-
Arogenate (pretyrosine) as an ...
Sphingomonas paucimobilis
FEMS Microbiol. Lett.
13
3-4
1982
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390531
Fazel
Obligatory biosynthesis of L-t ...
Brevibacterium flavum, Corynebacterium ammoniagenes, Corynebacterium glutamicum
J. Bacteriol.
138
805-815
1979
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1
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6
3
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6
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3
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6
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3
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6
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3
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3
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390557
Rubin
Enzymology of L-tyrosine biosy ...
Vigna radiata
Plant Physiol.
64
727-734
1979
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