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Literature summary extracted from

  • Deng, B.; Parthasarathy, S.; Wang, W.; Gibney, B.R.; Battaile, K.P.; Lovell, S.; Benson, D.R.; Zhu, H.
    Study of the individual cytochrome b5 and cytochrome b5 reductase domains of Ncb5or reveals a unique heme pocket and a possible role of the CS domain (2010), J. Biol. Chem., 285, 30181-30191.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.6.2.2 expressed in Escherichia coli BL21(DE3) cells Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.6.2.2 sitting drop vapor diffusion method, using 2 M (NH4)2SO4, 100 mM sodium/potassium phosphate, pH 6.2, 200 mM Li2SO4, at 4°C Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.6.2.2 microsome Cyb5R3 Homo sapiens
-
-

Organism

EC Number Organism UniProt Comment Textmining
1.6.2.2 Homo sapiens Q7L1T6
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.6.2.2 Ni2+-NTA bead chromatography, HiTrap Q column chromatography, HiTrap phenyl column chromatography, and Superdex 200 gel filtration Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.6.2.2 2 ferricytochrome b5 + NADH
-
 Homo sapiens 2 ferrocytochrome b5 + NAD+ + H+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.6.2.2 b5 plusb5R
-
 Homo sapiens
1.6.2.2 b5/b5R
-
 Homo sapiens
1.6.2.2 B5R cytochrome b5 reductase domain of Ncb5or Homo sapiens
1.6.2.2 CYB5R3
-
 Homo sapiens
1.6.2.2 Cyb5R4
-
 Homo sapiens
1.6.2.2 cytochrome b5 reductase
-
 Homo sapiens
1.6.2.2 NADH cytochrome b5 oxidoreductase
-
 Homo sapiens
1.6.2.2 Ncb5or
-
 Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.6.2.2 FAD
-
 Homo sapiens
1.6.2.2 NADH
-
 Homo sapiens