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Literature summary extracted from

  • Van den Broek, H.W.J.; Santema, J.S.; Wassink, J.H.; Veeger, C.
    Pyridine-nucleotide transhydrogenase. 1. Isolation, purification and characterisation of the transhydrogenase from Azotobacter vinelandii (1971), Eur. J. Biochem., 24, 31-45.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.6.1.1 2'-AMP almost no effect Azotobacter vinelandii

General Stability

EC Number General Stability Organism
1.6.1.1 bovine serum albumin, 0.2%, stabilization of diluted solutions Azotobacter vinelandii
1.6.1.1 urea, 5 min, 50% inactivation Azotobacter vinelandii

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.6.1.1 deoxycholate
-
 Azotobacter vinelandii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.6.1.1 0.0003
-
 FAD at 25°C Azotobacter vinelandii
1.6.1.1 0.0025
-
 FAD at 0°C Azotobacter vinelandii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.6.1.1 EDTA slight activating at low buffer concentrations Azotobacter vinelandii

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.6.1.1 30000000 50000000 rod-like structure, light scattering Azotobacter vinelandii

Organism

EC Number Organism UniProt Comment Textmining
1.6.1.1 Azotobacter vinelandii
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.6.1.1
-
 Azotobacter vinelandii

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.6.1.1 220 260
-
 Azotobacter vinelandii

Storage Stability

EC Number Storage Stability Organism
1.6.1.1 4°C, 0.1 M phosphate buffer, pH 7.5, 1 mM EDTA, several months, no loss of activity, storage at -20°C yields a partly insoluble enzyme Azotobacter vinelandii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.6.1.1 NAD(P)H + 2,6-dichlorophenolindophenol
-
 Azotobacter vinelandii NAD(P)+ + reduced 2,6-dichlorophenolindophenol
-
 ?
1.6.1.1 NAD(P)H + K4Fe(CN)6
-
 Azotobacter vinelandii NAD(P)+ + K3Fe(CN)6
-
 ?
1.6.1.1 NADH + thio-NAD+
-
 Azotobacter vinelandii NAD+ + thio-NADH
-
 ?
1.6.1.1 NADH + thio-NADP+
-
 Azotobacter vinelandii NAD+ + thio-NADPH
-
 ?
1.6.1.1 NADP+ + NADH diaphorase-type reactions with NAD(P)H, K3Fe(CN)6 and 2,6-dichlorophenol indophenol Azotobacter vinelandii NADPH + NAD+
-
 ?
1.6.1.1 NADPH + thio-NAD+ + H+[side 1]
-
 Azotobacter vinelandii NADP+ + thio-NADH + H+[side 2]
-
 ?
1.6.1.1 NADPH + thio-NADP+ + H+[side 1]
-
 Azotobacter vinelandii NADP+ + thio-NADPH + H+[side 2]
-
 ?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.6.1.1 50
-
 1 h stable, inactivation is dramatically accelerated by NADH and NADPH, partial protection by NADP+ and FMN, almost full protection by FAD Azotobacter vinelandii
1.6.1.1 65
-
 15 min, complete inactivation, protection by FAD Azotobacter vinelandii

Cofactor

EC Number Cofactor Comment Organism Structure
1.6.1.1 FAD FAD dissociates from the enzyme by heat treatment at 100°C or by treatment with 5% trichloroacetic acid at 0°C Azotobacter vinelandii