BRENDA - Enzyme Database show
show all sequences of 4.2.1.51

Regulatory properties of prephenate dehydrogenase and prephenate dehydratase from Corynebacterium glutamicum

Hagino, H.; Nakayama, K.; Agric. Biol. Chem. 38, 2367-2376 (1974)
No PubMed abstract available

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
3-Aminotyrosine
activation
Corynebacterium glutamicum
D-tyrosine
activation
Corynebacterium glutamicum
L-isoleucine
activation
Corynebacterium glutamicum
L-leucine
activation
Corynebacterium glutamicum
L-methionine
activation
Corynebacterium glutamicum
L-tyrosine
1 mM, 6fold activation; activation
Corynebacterium glutamicum
p-aminophenylalanine
activation
Corynebacterium glutamicum
Inhibitors
Inhibitors
Commentary
Organism
Structure
4-methyltryptophan
-
Corynebacterium glutamicum
5-Methyltryptophan
-
Corynebacterium glutamicum
6-Fluorotryptophan
-
Corynebacterium glutamicum
L-phenylalanine
0.05 mM, 50% inhibition
Corynebacterium glutamicum
L-tryptophan
0.1 mM, 100% inhibition
Corynebacterium glutamicum
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.1
-
prephenate
-
Corynebacterium glutamicum
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
prephenate
Corynebacterium glutamicum
-
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Corynebacterium glutamicum
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
prephenate
-
33885
Corynebacterium glutamicum
phenylpyruvate + H2O + CO2
-
33885
Corynebacterium glutamicum
?
prephenate
-
33885
Corynebacterium glutamicum
?
-
-
-
-
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
33
-
Corynebacterium glutamicum
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.8
-
potassium phosphate buffer
Corynebacterium glutamicum
7
-
,Tris-maleate buffer
Corynebacterium glutamicum
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.05
-
L-phenylalanine
-
Corynebacterium glutamicum
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
3-Aminotyrosine
activation
Corynebacterium glutamicum
D-tyrosine
activation
Corynebacterium glutamicum
L-isoleucine
activation
Corynebacterium glutamicum
L-leucine
activation
Corynebacterium glutamicum
L-methionine
activation
Corynebacterium glutamicum
L-tyrosine
1 mM, 6fold activation; activation
Corynebacterium glutamicum
p-aminophenylalanine
activation
Corynebacterium glutamicum
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
4-methyltryptophan
-
Corynebacterium glutamicum
5-Methyltryptophan
-
Corynebacterium glutamicum
6-Fluorotryptophan
-
Corynebacterium glutamicum
L-phenylalanine
0.05 mM, 50% inhibition
Corynebacterium glutamicum
L-tryptophan
0.1 mM, 100% inhibition
Corynebacterium glutamicum
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.05
-
L-phenylalanine
-
Corynebacterium glutamicum
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.1
-
prephenate
-
Corynebacterium glutamicum
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
prephenate
Corynebacterium glutamicum
-
?
-
-
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
prephenate
-
33885
Corynebacterium glutamicum
phenylpyruvate + H2O + CO2
-
33885
Corynebacterium glutamicum
?
prephenate
-
33885
Corynebacterium glutamicum
?
-
-
-
-
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
33
-
Corynebacterium glutamicum
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.8
-
potassium phosphate buffer
Corynebacterium glutamicum
7
-
,Tris-maleate buffer
Corynebacterium glutamicum
Other publictions for EC 4.2.1.51
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)
747338
Wu
Enhancement of L-phenylalanin ...
Escherichia coli
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2018
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El-Azaz
Identification of a small pro ...
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4
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6
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2
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X-ray structure of prephenate ...
Streptococcus mutans
J. Microbiol.
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730847
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-
Production of L-phenylalanine ...
Escherichia coli, Escherichia coli W3110 / ATCC 27325
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Sharma
-
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Camellia sinensis
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2011
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2
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716582
Bross
Complementation of the pha2 ye ...
Arabidopsis thaliana
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7
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702472
Van Vleet
13C isotope effect on the reac ...
Methanocaldococcus jannaschii
Biochim. Biophys. Acta
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2010
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1
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702720
Zhou
Enhanced l-phenylalanine biosy ...
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101
4151-4156
2010
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1
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1
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4
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1
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3
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2
1
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1
1
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692260
Lim
Characterization of a key trif ...
Archaeoglobus fulgidus, Nanoarchaeum equitans
Extremophiles
13
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2009
2
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1
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2
2
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4
1
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7
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1
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1
1
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1
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1
1
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1
1
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1
1
706236
Tzin
Expression of a bacterial bi-f ...
Escherichia coli
Plant J.
60
156-167
2009
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1
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1
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1
1
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706809
Battilana
The 1-deoxy-D: -xylulose 5-pho ...
Vitis vinifera x Vitis riparia, Vitis vinifera x Vitis vinifera
Theor. Appl. Genet.
118
653-669
2009
-
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2
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2
2
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684578
Chavez-Bejar
Metabolic engineering of Esche ...
Zymomonas mobilis, Zymomonas mobilis ATCC 31821
Appl. Environ. Microbiol.
74
3284-3290
2008
-
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1
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4
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694629
Yamada
Mutation of a rice gene encodi ...
Oryza sativa
Plant Cell
20
1316-1329
2008
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1
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1
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1
6
1
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2
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4
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2
2
6
2
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1
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1
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2
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1
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1
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-
695038
Vivan
Structural studies of prephena ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Proteins
72
1352-1362
2008
-
-
1
1
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2
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6
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681657
Tan
Structures of open (R) and clo ...
Chlorobaculum tepidum, Staphylococcus aureus
J. Struct. Biol.
162
94-107
2007
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2
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2
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677342
Vivan
Crystallization and preliminar ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Acta Crystallogr. Sect. F
62
357-360
2006
-
-
1
1
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-
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162
-
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2
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678167
Kleeb
A monofunctional and thermosta ...
Methanocaldococcus jannaschii
Biochemistry
45
14101-14110
2006
-
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1
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1
1
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3
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4
-
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1
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1
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1
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1
1
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1
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682402
Warpeha
G-protein-coupled receptor 1, ...
Arabidopsis thaliana
Plant Physiol.
140
844-855
2006
-
-
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1
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1
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6
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663605
Liberles
Allosteric mechanisms in ACT d ...
Escherichia coli
Amino Acids
28
1-12
2005
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1
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3
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-
665625
Prakash
pheA (Rv3838c) of Mycobacteriu ...
Mycobacterium tuberculosis
J. Biol. Chem.
280
20666-20671
2005
3
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1
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4
1
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1
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4
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1
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2
1
1
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1
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3
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1
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4
-
1
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1
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1
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2
1
1
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1
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-
649516
Hsu
Mutational analysis of feedbac ...
Corynebacterium glutamicum, Corynebacterium glutamicum CCRC 11384
Arch. Microbiol.
181
237-244
2004
-
-
1
-
15
-
1
9
-
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1
2
-
3
-
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1
1
-
-
9
-
4
1
1
-
-
7
1
-
-
-
-
-
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-
-
1
-
-
15
-
-
1
-
9
-
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1
2
-
-
-
1
-
-
9
-
4
1
1
-
-
7
1
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Prephenate dehydratase of the ...
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Phenylalanine production by me ...
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Purification of prephenate deh ...
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Cloning, sequencing, and expre ...
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Prephenate dehydratase (monofu ...
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Molecular cloning and nucleoti ...
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Cloning of the genes concerend ...
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Baldwin
Kinetic studies on the mechani ...
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[A prephenate dehydratase from ...
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Purification of Prephenate deh ...
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Purification and properties of ...
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Chorismate mutase/prephenate d ...
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33887
Davidson
Chorismate mutase-prephenate d ...
Escherichia coli
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1972
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33888
Schmit
Chorismate mutase-prephenate d ...
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33889
Schmit
Chorismate mutase-prephenate d ...
Salmonella enterica subsp. enterica serovar Typhimurium
Biochemistry
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1969
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33890
Cerutti
Enzymatic formation of phenylp ...
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