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Literature summary extracted from

  • Ji, L.; Becana, M.; Klucas, R.V.
    Involvement of molecular oxygen in the enzyme-catalyzed NADH oxidation and ferric leghemoglobin reduction (1992), Plant Physiol., 100, 33-39.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.6.2.6 NAD(P)H + ferrileghemoglobin Glycine max
-
 NAD(P)+ + ferroleghemoglobin
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.6.2.6 Glycine max
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.6.2.6 root nodule
-
 Glycine max
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.6.2.6 0.388
-
 reduction of ferrileghemoglobin in the presence of O2 Glycine max
1.6.2.6 1.85
-
 oxidation of NADH in the presence of O2, 30fold higher than in the absence of O2 Glycine max
1.6.2.6 4.5
-
 reduction of 2,6-dichloroindophenol in the presence of O2 Glycine max

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.6.2.6 2,6-dichloroindophenol + NADH no activity in the absence of Glycine max reduced 2,6-dichloroindophenol + NAD+
-
 ?
1.6.2.6 NAD(P)H + ferrileghemoglobin
-
 Glycine max NAD(P)+ + ferroleghemoglobin
-
 ?
1.6.2.6 NAD(P)H + ferrileghemoglobin no activity in the absence of O2, formation of H2O2 or peroxide intermediates during NADH oxidation Glycine max NAD(P)+ + ferroleghemoglobin
-
 ?