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Literature summary for 1.6.2.2 extracted from

  • Bando, S.; Takano, T.; Yubisui, T.; Shirabe, K.; Takeshita, M.; Nakagawa, A.
    Structure of human erythrocyte NADH-cytochrome b5 reductase (2004), Acta Crystallogr. Sect. D, 60, 1929-1934.
    View publication on PubMed
Search for more literature for 1.6.2.2

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli as alpha-thrombin-cleavable fusion protein Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting-drop vapor diffusion method Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
soluble formed by alternative splicing Homo sapiens
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 ferricytochrome b5 + NADH Homo sapiens involved in the synthesis of fatty acids and cholesterol, and in the oxidation of xenobiotics 2 ferrocytochrome b5 + NAD+ + H+
-
 ?
methemoglobin + NADH Homo sapiens provides functional hemoglobin hemoglobin + NAD+
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
erythrocyte
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 ferricytochrome b5 + NADH
-
 Homo sapiens 2 ferrocytochrome b5 + NAD+ + H+
-
 ?
2 ferricytochrome b5 + NADH involved in the synthesis of fatty acids and cholesterol, and in the oxidation of xenobiotics Homo sapiens 2 ferrocytochrome b5 + NAD+ + H+
-
 ?
methemoglobin + NADH provides functional hemoglobin Homo sapiens hemoglobin + NAD+
-
 ?

Cofactor

Cofactor Comment Organism Structure
FAD non-covalently bound in a large cleft between the two major domains Homo sapiens
NADH
-
 Homo sapiens