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Literature summary for 1.8.1.4 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
Search for more literature for 1.8.1.4

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli Glycine max

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.029
-
 ferrileghemoglobin
-
 Glycine max
0.058
-
 NADH
-
 Glycine max
3.38
-
 Lipoamide
-
 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
50027
-
 x * 50027, MW only of protein, flavin is reduced during analysis, electrospray MS analysis Glycine max

Organism

Organism UniProt Comment Textmining
Glycine max O81413
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Glycine max

Source Tissue

Source Tissue Comment Organism Textmining
nodule enzyme form FlbR-2 Glycine max
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
83.06
-
 lipoamide reduction Glycine max

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
dimer x * 50027, MW only of protein, flavin is reduced during analysis, electrospray MS analysis Glycine max

Cofactor

Cofactor Comment Organism Structure
FAD covalently bound to the protein Glycine max
NAD+
-
 Glycine max
NADH
-
 Glycine max