1.16.1.10: ferric-chelate reductase [NAD(P)H]

This is an abbreviated version!
For detailed information about ferric-chelate reductase [NAD(P)H], go to the full flat file.

Reaction

2 Fe(II)-siderophore +

Synonyms

AF0830, cFRO, chloroplast ferric chelate oxidoreductase, FCR, ferric chelate oxidoreductase, ferric chelate reductase, Ferric chelate reductase 1 like protein, ferric reductase, ferric-chelate reductase (NAD(P)H), FRO protein, FRO2, FRO3, FRO5, FRRS1L

ECTree

     1 Oxidoreductases

         1.16 Oxidizing metal ions

             1.16.1 With NAD⁺ or NADP⁺ as acceptor

                1.16.1.10 ferric-chelate reductase [NAD(P)H]

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Results	in table
1	Activating Compound
8	AA Sequence
4	Cloned(Commentary)
10	Cofactor
1	Crystallization (Commentary)
2	Expression
13	General Information
4	KM Value [mM]
11	Localization
1	Metals/Ions
3	Molecular Weight [Da]
3	Natural Substrates/ Products (Substrates)
13	Organism
4	pH Optimum
2	pH Range
1	pI Value
2	Protein Variants
2	Purification (Commentary)
1	Reaction
9	Reference
13	Source Tissue
1	Specific Activity [micromol/min/mg]
14	Substrates and Products (Substrate)
2	Subunits
35	Synonyms
1	Systematic Name
3	Temperature Optimum [°C]
1	Temperature Range [°C]

KM Value

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KM Value on EC 1.16.1.10 - ferric-chelate reductase [NAD(P)H]

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KM VALUE [mM]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.066

Fe(III)-EDTA

Archaeoglobus fulgidus

O29428

pH 7.0, 85°C, cosubstrate: NADPH

722612

0.061

NADH

Archaeoglobus fulgidus

O29428

pH 7.0, 85°C

722612

0.08

NADPH

Archaeoglobus fulgidus

O29428

pH 7.0, 85°C

722612

additional information

additional information

Beta vulgaris

-

FCR activity of inner envelope of chloroplast vesicles isolated from Fe-deficient plants shows clear biphasic kinetics. Using NADPH, biphasic saturation kinetics are measured with the first saturation found at KM = 0.0046 mM Fe(III)-EDTA, and the second saturation found at KM = 0.0557 mM Fe(III)-EDTA. In the presence of NADH, the saturation kinetics is monophasic, the sole saturation reaction rate is significantly lower, and the KM value of the reaction is significantly higher with 0.0834 mM Fe(III)-EDTA compared to the second saturation measured with NADPH. In vesicles isolated from Fe-sufficient plants, the affinity of the enzyme does not change with KM = 0.0042mM Fe(III)-EDTA. The second, low-affinity saturation point, KM = 0.155 mM Fe(III)-EDTA is significantly higher than that in Fe-sufficient plants, with a reaction rate that is also somewhat higher than in the envelope of chloroplast membranes of Fe-sufficient plants

745899

-