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Literature summary extracted from

  • McConkey, S.; Saunders, J.; Speare, D.J.
    Comparison of NADH-dependent cytochrome b5 reductase activity and in vitro methemoglobin induction by sodium nitrite in Oncorhynchus mykiss, Salmo salar, and Salvelinus fontinalis (2013), Fish Physiol. Biochem., 39, 713-719.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.6.2.2 additional information species-specific sensitivity to methemoglobin induction, in vitro induction of methemoglobin by 1 mM NaNO2, overview Oncorhynchus mykiss
1.6.2.2 additional information species-specific sensitivity to methemoglobin induction, in vitro induction of methemoglobin by 1 mM NaNO2, overview Salmo salar
1.6.2.2 additional information species-specific sensitivity to methemoglobin induction, in vitro induction of methemoglobin by 1 mM NaNO2, overview Salvelinus fontinalis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.6.2.2 membrane
-
 Oncorhynchus mykiss 16020
-
1.6.2.2 membrane
-
 Salmo salar 16020
-
1.6.2.2 membrane
-
 Salvelinus fontinalis 16020
-

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 Oncorhynchus mykiss
-
 2 ferrocytochrome b5 + NAD+ + H+
-
 ?
1.6.2.2 2 ferricytochrome b5 + NADH Salmo salar
-
 2 ferrocytochrome b5 + NAD+ + H+
-
 ?
1.6.2.2 2 ferricytochrome b5 + NADH Salvelinus fontinalis
-
 2 ferrocytochrome b5 + NAD+ + H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.6.2.2 Oncorhynchus mykiss
-
-
-
1.6.2.2 Salmo salar
-
-
-
1.6.2.2 Salvelinus fontinalis
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.6.2.2 erythrocyte
-
 Oncorhynchus mykiss
-
1.6.2.2 erythrocyte
-
 Salmo salar
-
1.6.2.2 erythrocyte
-
 Salvelinus fontinalis
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.6.2.2 2 ferricytochrome b5 + NADH
-
 Oncorhynchus mykiss 2 ferrocytochrome b5 + NAD+ + H+
-
 ?
1.6.2.2 2 ferricytochrome b5 + NADH
-
 Salmo salar 2 ferrocytochrome b5 + NAD+ + H+
-
 ?
1.6.2.2 2 ferricytochrome b5 + NADH
-
 Salvelinus fontinalis 2 ferrocytochrome b5 + NAD+ + H+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.6.2.2 cb5r
-
 Oncorhynchus mykiss
1.6.2.2 cb5r
-
 Salmo salar
1.6.2.2 cb5r
-
 Salvelinus fontinalis
1.6.2.2 NADH-dependent cytochrome b5 reductase
-
 Oncorhynchus mykiss
1.6.2.2 NADH-dependent cytochrome b5 reductase
-
 Salmo salar
1.6.2.2 NADH-dependent cytochrome b5 reductase
-
 Salvelinus fontinalis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.6.2.2 30
-
 assay at Oncorhynchus mykiss
1.6.2.2 30
-
 assay at Salmo salar
1.6.2.2 30
-
 assay at Salvelinus fontinalis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.6.2.2 8
-
 assay at Oncorhynchus mykiss
1.6.2.2 8
-
 assay at Salmo salar
1.6.2.2 8
-
 assay at Salvelinus fontinalis

Cofactor

EC Number Cofactor Comment Organism Structure
1.6.2.2 NADH dependent on Oncorhynchus mykiss
1.6.2.2 NADH dependent on Salmo salar
1.6.2.2 NADH dependent on Salvelinus fontinalis