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Literature summary extracted from

  • Davis, C.A.; Crowley, L.J.; Barber, M.J.
    Cytochrome b5 reductase: the roles of the recessive congenital methemoglobinemia mutants P144L, L148P, and R159* (2004), Arch. Biochem. Biophys., 431, 233-244.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.6.2.2 expressed in Escherichia coli BL21(DE3)-RIL Rattus norvegicus

Protein Variants

EC Number Protein Variants Comment Organism
1.6.2.2 L148P 31% of wild type activity, reduced temperature stability and resistance against limited proteolysis with trypsin, increased affinity for NAD+ Rattus norvegicus
1.6.2.2 P144L 28% of wild type activity, reduced temperature stability and resistance against limited proteolysis with trypsin, increased affinity for NAD+ Rattus norvegicus
1.6.2.2 P144L/L148P 8% of wild type activity, reduced temperature stability and resistance against limited proteolysis with trypsin, increased affinity for NAD+ Rattus norvegicus
1.6.2.2 R159 deletion mutant, could not be successfully expressed Rattus norvegicus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.6.2.2 NAD+ competitive, stronger inhibition of mutant enzymes compared to wild type enzyme Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.6.2.2 0.008
-
 ferricyanide L148P mutant enzyme, pH 7.0, 25°C Rattus norvegicus
1.6.2.2 0.008
-
 ferricyanide P144L mutant enzyme, pH 7.0, 25°C Rattus norvegicus
1.6.2.2 0.008
-
 ferricyanide P144L/L148P mutant enzyme, pH 7.0, 25°C Rattus norvegicus
1.6.2.2 0.008
-
 ferricyanide wild type enzyme, pH 7.0, 25°C Rattus norvegicus
1.6.2.2 0.01
-
 ferricytochome b5 L148P mutant enzyme, pH 7.0, 25°C Rattus norvegicus
1.6.2.2 0.012
-
 ferricytochome b5 P144L mutant enzyme, pH 7.0, 25°C Rattus norvegicus
1.6.2.2 0.013
-
 ferricytochome b5 P144L/L148P mutant enzyme, pH 7.0, 25°C Rattus norvegicus
1.6.2.2 0.013
-
 ferricytochome b5 wild type enzyme, pH 7.0, 25°C Rattus norvegicus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.6.2.2 membrane full length form contains a 3 kDa membrane anchoring domain Rattus norvegicus 16020
-
1.6.2.2 soluble truncated form lacking the membrane anchoring domain, present in erythrocytes Rattus norvegicus
-
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.6.2.2 30000
-
 SDS-PAGE Rattus norvegicus

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 Rattus norvegicus involved in the synthesis of fatty acids and cholesterol, and in the oxidation of xenobiotics, enzyme defects causes methemoglobinemia type I or type II 2 ferrocytochrome b5 + NAD+ + H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.6.2.2 Rattus norvegicus P20070
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.6.2.2 recombinant enzymes Rattus norvegicus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.6.2.2 2 ferricyanide + NADH
-
 Rattus norvegicus 2 ferrocyanide + NAD+ + H+
-
 ?
1.6.2.2 2 ferricytochrome b5 + NADH
-
 Rattus norvegicus 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, enzyme defects causes methemoglobinemia type I or type II Rattus norvegicus 2 ferrocytochrome b5 + NAD+ + H+
-
 ?
1.6.2.2 NADH + ferricytochrome b5
-
 Rattus norvegicus NAD+ + H+ + ferrocytochrome b5
-
 r
1.6.2.2 NADH + ferricytochrome b5
-
 Rattus norvegicus NAD+ + H+ + 2 ferrocytochrome b5
-
 r

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.6.2.2 33
-
 ferricytochome b5 P144L/L148P mutant enzyme, pH 7.0, 25°C Rattus norvegicus
1.6.2.2 100
-
 ferricyanide P144L/L148P mutant enzyme, pH 7.0, 25°C Rattus norvegicus
1.6.2.2 117
-
 ferricytochome b5 P144L mutant enzyme, pH 7.0, 25°C Rattus norvegicus
1.6.2.2 130
-
 ferricytochome b5 L148P mutant enzyme, pH 7.0, 25°C Rattus norvegicus
1.6.2.2 283
-
 ferricyanide P144L mutant enzyme, pH 7.0, 25°C Rattus norvegicus
1.6.2.2 300
-
 ferricyanide L148P mutant enzyme, pH 7.0, 25°C Rattus norvegicus
1.6.2.2 417
-
 ferricytochome b5 wild type enzyme, pH 7.0, 25°C Rattus norvegicus
1.6.2.2 800
-
 ferricyanide wild type enzyme, pH 7.0, 25°C Rattus norvegicus

Cofactor

EC Number Cofactor Comment Organism Structure
1.6.2.2 FAD non-covalentely bound prosthetic group Rattus norvegicus
1.6.2.2 NADH
-
 Rattus norvegicus