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Literature summary extracted from

  • Elahian, F.; Sepehrizadeh, Z.; Moghimi, B.; Mirzaei, S.A.
    Human cytochrome b5 reductase: structure, function, and potential applications (2012), Crit. Rev. Biotechnol., 2012, 1-11.
    View publication on PubMed

Application

EC Number Application Comment Organism
1.6.2.2 analysis potential use of the enzyme as biosensor Homo sapiens
1.6.2.2 diagnostics potential use of the enzyme in diagnostic areas Homo sapiens
1.6.2.2 industry potential use of the enzyme in the food industry Homo sapiens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.6.2.2 heterologous expression in Escherichia coli or in yeast cells via different expression vectors, in Aspergillus oryzae using pNGA142, Salmonella typhimurium using pIN, in Spodoptera frugiperda Sf9 insect cells using pFASTBAC baculovirus vectors, in cell-free systems, in plant cells using pRT, in lymphoid cells using Epstein-Barr virus, and in CHO cells using SV40 transfection method Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
1.6.2.2 A179T naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations Homo sapiens
1.6.2.2 A179V naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations Homo sapiens
1.6.2.2 C204R naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations Homo sapiens
1.6.2.2 C204Y naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations Homo sapiens
1.6.2.2 D239T the mutation changes the enzme preference for NADH to one for NADPH. Diseases related to CyB5R dysfunctions due to mutations in the gene encoding the enzyme, detailed overview Homo sapiens
1.6.2.2 D240G naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations Homo sapiens
1.6.2.2 E213K naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations Homo sapiens
1.6.2.2 F157C naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations Homo sapiens
1.6.2.2 G144D naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations Homo sapiens
1.6.2.2 G292D naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations Homo sapiens
1.6.2.2 G72A naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations Homo sapiens
1.6.2.2 G76S naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations Homo sapiens
1.6.2.2 I216T naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations Homo sapiens
1.6.2.2 I85S naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations Homo sapiens
1.6.2.2 L149P naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations Homo sapiens
1.6.2.2 L217P naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations Homo sapiens
1.6.2.2 L239R naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations Homo sapiens
1.6.2.2 L73P naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations Homo sapiens
1.6.2.2 M127V naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations Homo sapiens
1.6.2.2 P145L naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations Homo sapiens
1.6.2.2 P145S naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations Homo sapiens
1.6.2.2 P276L naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations Homo sapiens
1.6.2.2 P65L naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations Homo sapiens
1.6.2.2 P96H naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations Homo sapiens
1.6.2.2 R241G naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations Homo sapiens
1.6.2.2 R259W naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations Homo sapiens
1.6.2.2 R46W naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations Homo sapiens
1.6.2.2 R50Q naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations Homo sapiens
1.6.2.2 R58Q naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations Homo sapiens
1.6.2.2 S128P naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations Homo sapiens
1.6.2.2 S54R naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations Homo sapiens
1.6.2.2 V106M naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations Homo sapiens
1.6.2.2 V253M naturally occuring mutation causing the RCM phenotype depending on homozygosity/heterozygosity or other additional mutations Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.6.2.2 cytoplasm soluble isozyme Homo sapiens 5737
-
1.6.2.2 lysosome
-
 Homo sapiens 5764
-
1.6.2.2 membrane
-
 Homo sapiens 16020
-
1.6.2.2 microsome the microsomal isozyme consists of one hydrophobic membrane-anchoring domain and a larger hydrophilic flavin catalytic domain Homo sapiens
-
-
1.6.2.2 mitochondrion
-
 Homo sapiens 5739
-

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 the electrostatic interactions between the lysyl residues (K42, K126, K163, and K164) in the enzyme and the carboxyl groups (E47, E48, E52, E60, and D64) of cytochrome b5 keep the proteins tightly complexed and are suitable for electron transfer, reaction mechanism, overview 2 ferrocytochrome b5 + NAD+ + H+
-
 ?

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
1.6.2.2 native membrane-bound isozyme by solubiization from membranes, anion exchange chromatography, and affinity chromatography Homo sapiens

Reaction

EC Number Reaction Comment Organism Reaction ID
1.6.2.2 NADH + 2 ferricytochrome b5 = NAD+ + H+ + 2 ferrocytochrome b5 reaction mechanism, overview Homo sapiens
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.6.2.2 erythrocyte contains the soluble isozyme but no microsomal isozyme 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 the electrostatic interactions between the lysyl residues (K42, K126, K163, and K164) in the enzyme and the carboxyl groups (E47, E48, E52, E60, and D64) of cytochrome b5 keep the proteins tightly complexed and are suitable for electron transfer, reaction mechanism, overview Homo sapiens 2 ferrocytochrome b5 + NAD+ + H+
-
 ?
1.6.2.2 2 ferricytochrome b5 + NADH potassium ferricyanide, cytochrome b5, or NADH-2,6-dichlorophenol-indophenol can act as electron acceptors Homo sapiens 2 ferrocytochrome b5 + NAD+ + H+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.6.2.2 CyB5R
-
 Homo sapiens
1.6.2.2 cytochrome b5 reductase
-
 Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.6.2.2 7.2 8.4 assay at, dependent on assay method Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.6.2.2 FAD flavoprotein, the FAD domain has a large cleft in which the FAD prosthetic group is located. The N-terminus of the NADH domain plays a hinge-connecting role between the two domains, the FAD and the NADH domains Homo sapiens
1.6.2.2 NADH preferred electron donor for CyB5R, a D239T mutation will change this preference to one for NADPH. The NADH domain provides a suitable position for the NADH coenzyme. The N-terminus of the NADH domain plays a hinge-connecting role between the two domains, the FAD and the NADH domains Homo sapiens

General Information

EC Number General Information Comment Organism
1.6.2.2 evolution CyB5R is a member of the NAD(P)H-ferredoxin reductase (FNR) enzyme superfamily, phylogenetic analysis Homo sapiens
1.6.2.2 malfunction autosomal cytochrome b5 reductase gene deficiency manifests with the accumulation of oxidized Fe+3 and recessive congenital methemoglobinemia in humans. Diseases related to CyB5R dysfunctions, overviews Homo sapiens
1.6.2.2 metabolism 2e- transfer from NADH to the enzyme CyB5R, to FAD, followed by reduction of 2 CyB5 and electron transfer to desaturase, CyP450 or methemoglobin Homo sapiens
1.6.2.2 additional information the soluble CyB5R diffraction map reveals two distinct domains: the N-terminal FAD binding domain (from I34 to R143), which contains a binding site for the FAD prosthetic group, and the NADH domain (residues K173 to F301). These domains are separated by a large interdomain cleft (G144-V172) known as a hinge region. The three anti-parallel beta-sheets in the hinge region keep the two lobes in close proximity with the correct conformational orientation. This orientation appears to be critical for electron transfer from NADH to FAD. The FAD domain consists of six anti-parallel beta-sheets and one alpha-helix with the order 5beta/1alpha/1beta. The NADH domain forms a alpha/beta/aalpha structure consisting of five beta-strands and four alpha-helices Homo sapiens
1.6.2.2 physiological function cytochrome b5 reductase is involved in the transfer of reducing equivalents from the physiological electron donor, NADH, via an FAD domain to the small molecules of cytochrome b5. It takes part in many oxidation and reduction reactions, such as the reduction of methemoglobin to hemoglobin Homo sapiens