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Literature summary for 1.6.2.6 extracted from

  • Moran, J.F.; Sun, Z.; Sarath, G.; Arredondo-Peter, R.; James, E.K.; Becana, M.; Klucas, R.V.
    Molecular cloning, functional characterization, and subcellular localization of soybean nodule dihydrolipoamide reductase (2002), Plant Physiol., 128, 300-313.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli BL21 Glycine max

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.029
-
ferrileghemoglobin recombinant FLbR-2 Glycine max
0.058
-
NADH recombinant FLbR-2 Glycine max
3.381
-
Lipoamide recombinant FLbR-2 Glycine max

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Glycine max 5739
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50030
-
electrospray mass spectrometry Glycine max

Organism

Organism UniProt Comment Textmining
Glycine max O81413
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Glycine max

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
Glycine max
-
root
-
Glycine max
-
root nodule
-
Glycine max
-
stem
-
Glycine max
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
NADH + ferrileghemoglobin
-
Glycine max NAD+ + ferroleghemoglobin
-
?
NADH + lipoamide
-
Glycine max NAD+ + ?
-
?

Synonyms

Synonyms Comment Organism
FLbR-2
-
Glycine max

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.6
-
ferrileghemoglobin recombinant FLbR-2 Glycine max
137
-
NADH recombinant FLbR-2 Glycine max
392
-
Lipoamide recombinant FLbR-2 Glycine max

Cofactor

Cofactor Comment Organism Structure
FAD not covalently bound to the protein Glycine max

pI Value

Organism Comment pI Value Maximum pI Value
Glycine max isoelectric focusing, pH-range 4.0-6.5
-
5.8