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Literature summary for 1.6.2.2 extracted from

  • Yamada, M.; Tamada, T.; Takeda, K.; Matsumoto, F.; Ohno, H.; Kosugi, M.; Takaba, K.; Shoyama, Y.; Kimura, S.; Kuroki, R.; Miki, K.
    Elucidations of the catalytic cycle of NADH-cytochrome b5 reductase by X-ray crystallography: new insights into regulation of efficient electron transfer (2013), J. Mol. Biol., 425, 4295-4306.
    View publication on PubMed
Search for more literature for 1.6.2.2

Crystallization (Commentary)

Crystallization (Comment) Organism
fully reduced form and the oxidized form of the purified liver enzyme, X-ray diffraction structure determination and analysis at 1.68 A resolution Sus scrofa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 ferricytochrome b5 + NADH Sus scrofa
-
 2 ferrocytochrome b5 + NAD+ + H+
-
 ?

Organism

Organism UniProt Comment Textmining
Sus scrofa P83686
-
-

Source Tissue

Source Tissue Comment Organism Textmining
erythrocyte
-
 Sus scrofa
-
liver
-
 Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 ferricytochrome b5 + NADH
-
 Sus scrofa 2 ferrocytochrome b5 + NAD+ + H+
-
 ?

Synonyms

Synonyms Comment Organism
B5R
-
 Sus scrofa
NADH-cytochrome b5 reductase
-
 Sus scrofa

Cofactor

Cofactor Comment Organism Structure
FAD redox state of FAD during the b5R catalytic cycle and crystal structures comparion of the fully reduced form and the oxidized form, overview Sus scrofa
NADH
-
 Sus scrofa

General Information

General Information Comment Organism
additional information the NADH-cytochrome b5 reductase is a flavoprotein consisting of NADH and FAD binding domains, that catalyzes electron transfer from the two-electron carrier NADH to the one-electron carrier cytochrome b5 Sus scrofa
physiological function the enzyme catalyzes the electron transfer from NADH to cytochrome b5 and participates in fatty acid synthesis, cholesterol synthesis, and xenobiotic oxidation as a member of the electron transport chain on the endoplasmic reticulum. In erythrocytes, the enzyme also participates in the reduction of methemoglobin Sus scrofa