Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.6.2.2 extracted from

  • Iyanagi, T.; Watanabe, S.; Anan, K.F.
    One-electron oxidation-reduction properties of hepatic NADH-cytochrome b5 reductase (1984), Biochemistry, 23, 1418-1425.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0004 0.0005 NADH lysosome- and detergent-solubilized enzyme Sus scrofa
0.03 0.04 cytochrome b5 lysosome- and detergent-solubilized enzyme Sus scrofa

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum
-
Sus scrofa 5783
-

Metals/Ions

Metals/Ions Comment Organism Structure
additional information rate of reduction depends on ionic strength Sus scrofa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
30000
-
x * 30000, lysosome-solubilized enzyme, SDS-PAGE Sus scrofa
35000
-
x * 35000, detergent-solubilized enzyme, SDS-PAGE Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
lysosome- and detergent-solubilization Sus scrofa

Reaction

Reaction Comment Organism Reaction ID
NADH + 2 ferricytochrome b5 = NAD+ + H+ + 2 ferrocytochrome b5 electron-transport chain from NADH to a terminal oxidase desaturase, proposed electron transfer mechanism Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
NADH + ferricytochrome b5
-
Sus scrofa NAD+ + H+ + ferrocytochrome b5
-
r

Subunits

Subunits Comment Organism
? x * 30000, lysosome-solubilized enzyme, SDS-PAGE Sus scrofa
? x * 35000, detergent-solubilized enzyme, SDS-PAGE Sus scrofa

Cofactor

Cofactor Comment Organism Structure
NADH
-
Sus scrofa