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Literature summary extracted from

  • Mihara, K.; Sato, R.
    Purification and properties of the intact form of NADH-cytochrome b5 reductase from rabbit liver microsomes (1975), J. Biochem., 78, 1057-1073.
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.6.2.2 endoplasmic reticulum
-
 Oryctolagus cuniculus 5783
-
1.6.2.2 membrane
-
 Oryctolagus cuniculus 16020
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.6.2.2 365000
-
 oligomeric aggregates of detergent solubilized enzyme, sedimentation equilibrium Oryctolagus cuniculus

Organism

EC Number Organism UniProt Comment Textmining
1.6.2.2 Oryctolagus cuniculus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.6.2.2
-
 Oryctolagus cuniculus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.6.2.2 liver
-
 Oryctolagus cuniculus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.6.2.2 1200 1300 ferricyanide reduction Oryctolagus cuniculus

Storage Stability

EC Number Storage Stability Organism
1.6.2.2 -70°C, several months, no loss of activity Oryctolagus cuniculus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.6.2.2 2 ferricytochrome b5 + NADH specific for NADH as electron donor, artificial acceptors: ferricyanide, 2,6-dichlorphenolindophenol Oryctolagus cuniculus 2 ferrocytochrome b5 + NAD+ + H+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.6.2.2 ?
-
 Oryctolagus cuniculus

Cofactor

EC Number Cofactor Comment Organism Structure
1.6.2.2 NADH
-
 Oryctolagus cuniculus