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Literature summary 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

Cloned(Commentary)

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

Crystallization (Commentary)

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

Localization

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

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.6.2.2 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+
-
 ?
1.6.2.2 methemoglobin + NADH Homo sapiens provides functional hemoglobin hemoglobin + NAD+
-
 ?

Organism

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

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.6.2.2 erythrocyte
-
 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+
-
 ?
1.6.2.2 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+
-
 ?
1.6.2.2 methemoglobin + NADH provides functional hemoglobin Homo sapiens hemoglobin + NAD+
-
 ?

Cofactor

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