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show all sequences of 1.16.1.9

Biological activity of Fe(III) aquo-complexes towards ferric chelate reductase (FCR)

Escudero, R.; Gomez-Gallego, M.; Romano, S.; Fernandez, I.; Gutierrez-Alonso, A.; Sierra, M.A.; Lopez-Rayo, S.; Nadal, P.; Lucena, J.J.; Org. Biomol. Chem. 10, 2272-2281 (2012)

Data extracted from this reference:

Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
-
Cucumis sativus
16020
-
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2 Fe(II)-siderophore + NADP+ + H+
Cucumis sativus
-
2 Fe(III)-siderophore + NADPH
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Cucumis sativus
-
cv. Ashley
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
root
-
Cucumis sativus
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2 Fe(II)-siderophore + NADP+ + H+
-
728418
Cucumis sativus
2 Fe(III)-siderophore + NADPH
-
-
-
r
Fe(III)-o,o-EDDHA I + NADPH
i.e. ethylenediaminebis(o-hydroxyphenyl)acetic acid
728418
Cucumis sativus
Fe(II)-o,o-EDDHA I + NADP+ + H+
-
-
-
?
additional information
the enzyme is able to effectively reduce synthetic ferric chelates, which are octahedral Fe(III) complexes derived from polyaminocarboxylic acids, the process requires the generation of a coordination vacancy in the Fe(III)L6 complex I and the incorporation of a water molecule, photometric titration, overview
728418
Cucumis sativus
?
-
-
-
-
Cofactor
Cofactor
Commentary
Organism
Structure
NADP+
dependent on
Cucumis sativus
NADPH
dependent on
Cucumis sativus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADP+
dependent on
Cucumis sativus
NADPH
dependent on
Cucumis sativus
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
-
Cucumis sativus
16020
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2 Fe(II)-siderophore + NADP+ + H+
Cucumis sativus
-
2 Fe(III)-siderophore + NADPH
-
-
r
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
root
-
Cucumis sativus
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2 Fe(II)-siderophore + NADP+ + H+
-
728418
Cucumis sativus
2 Fe(III)-siderophore + NADPH
-
-
-
r
Fe(III)-o,o-EDDHA I + NADPH
i.e. ethylenediaminebis(o-hydroxyphenyl)acetic acid
728418
Cucumis sativus
Fe(II)-o,o-EDDHA I + NADP+ + H+
-
-
-
?
additional information
the enzyme is able to effectively reduce synthetic ferric chelates, which are octahedral Fe(III) complexes derived from polyaminocarboxylic acids, the process requires the generation of a coordination vacancy in the Fe(III)L6 complex I and the incorporation of a water molecule, photometric titration, overview
728418
Cucumis sativus
?
-
-
-
-
General Information
General Information
Commentary
Organism
physiological function
the process known as Strategy I, occurs in the rhizosphere and is mediated by the FRO2, a ferric chelate reductase enzyme. Once reduced, the Fe(II) is taken up into the cells by the IRT1, a specific transport system
Cucumis sativus
General Information (protein specific)
General Information
Commentary
Organism
physiological function
the process known as Strategy I, occurs in the rhizosphere and is mediated by the FRO2, a ferric chelate reductase enzyme. Once reduced, the Fe(II) is taken up into the cells by the IRT1, a specific transport system
Cucumis sativus
Other publictions for EC 1.16.1.9
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)
743901
Chandel
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3
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1
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1
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3
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2
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2
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1
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1
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1
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12
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1
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20
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4
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2
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1
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1
2
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4
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2
2
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1
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2
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20
1
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1
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4
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27
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1
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6
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2
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1
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1
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2
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6
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2
2
2
2
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721185
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64
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2008
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1
1
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3
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2
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4
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1
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1
1
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2
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1
2
1
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3
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2
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1
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1
1
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676551
Schagerloef
Transmembrane topology of FRO2 ...
Arabidopsis thaliana
Plant Mol. Biol.
62
215-221
2006
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-
-
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-
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1
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1
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2
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2
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1
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723453
Waters
Characterization of FRO1, a pe ...
Pisum sativum
Plant Physiol.
129
85-94
2002
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1
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1
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1
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3
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1
1
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1
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1
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3
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1
1
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1
1
1
1
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723258
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A ferric-chelate reductase for ...
Arabidopsis thaliana
Nature
397
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1999
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1
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1
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1
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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
2
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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
1
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1
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