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KEGG pathways | MAP code | Pathways |
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MAP00530 | Aminosugars metabolism |
UniProtKB:Accession Number | P83686 | P20070 | P00387 |
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Entry name | NB5R3_PIG | NB5R3_RAT | NB5R3_HUMAN |
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Activity | NADH + 2 ferricytochrome b5 = NAD(+) + H(+) + 2 ferrocytochrome b5. | NADH + 2 ferricytochrome b5 = NAD(+) + H(+) + 2 ferrocytochrome b5. | NADH + 2 ferricytochrome b5 = NAD(+) + H(+) + 2 ferrocytochrome b5. |
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Subunit | Component of a complex composed of cytochrome b5, NADH- cytochrome b5 reductase (CYB5R3) and MOSC2. | Component of a complex composed of cytochrome b5, NADH- cytochrome b5 reductase (CYB5R3) and MOSC2 (By similarity). | Component of a complex composed of cytochrome b5, NADH- cytochrome b5 reductase (CYB5R3) and MOSC2 (By similarity). |
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Subcellular location | Endoplasmic reticulum membrane, Lipid- anchor, Cytoplasmic side (By similarity). Mitochondrion outer membrane, Lipid-anchor, Cytoplasmic side (By similarity). Cytoplasm (By similarity). Note=The enzyme exists in two forms, a membrane-bound form on the cytoplasmic side of the endoplasmic reticulum and also on the mitochondrial outer membrane and in soluble form in erythrocytes (By similarity). NADH-cytochrome b5 reductase 3 membrane-bound form: Endoplasmic reticulum membrane, Lipid-anchor, Cytoplasmic side (By similarity). Mitochondrion outer membrane, Lipid-anchor, Cytoplasmic side (By similarity). NADH-cytochrome b5 reductase 3 soluble form: Cytoplasm (By similarity). | Isoform 1: Endoplasmic reticulum membrane, Lipid-anchor, Cytoplasmic side. Mitochondrion outer membrane, Lipid-anchor, Cytoplasmic side.,Isoform 3: Cytoplasm. Note=Produces the soluble form found in erythrocytes. | Isoform 1: Endoplasmic reticulum membrane, Lipid-anchor, Cytoplasmic side. Mitochondrion outer membrane, Lipid-anchor, Cytoplasmic side.,Isoform 2: Cytoplasm. Note=Produces the soluble form found in erythrocytes. |
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Cofactor | FAD. | FAD. | FAD. |
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Compound table: links to PDB-related databases & PoSSuM |
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| Cofactors | Substrates | Products |
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KEGG-id | C00016 | C00004 | C00996 | C00080 | C00003 | C00999 |
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Compound | FAD | NADH | Ferricytochrome b5 | H+ | NAD+ | Ferrocytochrome b5 |
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Type | amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,nucleotide | amide group,amine group,nucleotide | aromatic ring (with nitrogen atoms),carbohydrate,heavy metal | others | amide group,amine group,nucleotide | aromatic ring (with nitrogen atoms),carbohydrate,heavy metal |
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ChEBI | 16238
| 16908
|
| 15378
| 15846
|
|
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PubChem | 643975
| 439153
|
| 1038
| 5893
|
|
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| | | | | | | | | | | | | |
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1ndhA01 |  |  |  |  |  |  |  | Bound:FAD | Unbound | Unbound | | Unbound | Unbound |
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1i7pA01 |  |  |  |  |  |  |  | Bound:FAD | Unbound | Unbound | | Unbound | Unbound |
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1ib0A01 |  |  |  |  |  |  |  | Bound:FAD | Unbound | Unbound | | Bound:NAD | Unbound |
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1qx4A01 |  |  |  |  |  |  |  | Bound:FAD | Unbound | Unbound | | Unbound | Unbound |
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1qx4B01 |  |  |  |  |  |  |  | Bound:FAD | Unbound | Unbound | | Unbound | Unbound |
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1umkA01 |  |  |  |  |  |  |  | Bound:FAD | Unbound | Unbound | | Unbound | Unbound |
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1ndhA02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound |
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1i7pA02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound |
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1ib0A02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound |
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1qx4A02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound |
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1qx4B02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound |
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1umkA02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | | Unbound | Unbound |
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References for Catalytic Mechanism | References | Sections | No. of steps in catalysis |
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[12] | p.39-40 |
| [14] | p.299-300 |
| [17] |
|
| [19] | Scheme II, p.3587-3588 |
|
references | [1] |
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PubMed ID | 3624234 |
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Journal | J Biol Chem |
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Year | 1987 |
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Volume | 262 |
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Pages | 11801-2 |
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Authors | Miki K, Kaida S, Kasai N, Iyanagi T, Kobayashi K, Hayashi K |
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Title | Crystallization and preliminary x-ray crystallographic study of NADH-cytochrome b5 reductase from pig liver microsomes. |
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[2] |
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PubMed ID | 3656431 |
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Journal | J Mol Biol |
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Year | 1987 |
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Volume | 195 |
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Pages | 749-50 |
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Authors | Takano T, Ogawa K, Sato M, Bando S, Yubisui T |
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Title | Preliminary X-ray data of NADH-cytochrome b5 reductase from human erythrocytes. |
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[3] |
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PubMed ID | 2831990 |
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Journal | Biochim Biophys Acta |
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Year | 1988 |
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Volume | 953 |
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Pages | 164-78 |
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Authors | Utecht RE, Kurtz DM Jr |
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Title | Cytochrome b5 and NADH-cytochrome-b5 reductase from sipunculan erythrocytes; a methemerythrin reduction system from Phascolopsis gouldii. |
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[4] |
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PubMed ID | 2494940 |
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Journal | Arch Biochem Biophys |
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Year | 1989 |
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Volume | 270 |
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Pages | 137-43 |
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Authors | Reif DW, Coulombe RA Jr, Aust SD |
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Title | Vanadate-dependent NAD(P)H oxidation by microsomal enzymes. |
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[5] |
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PubMed ID | 2189408 |
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Journal | Biochem Biophys Res Commun |
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Year | 1990 |
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Volume | 168 |
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Pages | 1285-91 |
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Authors | Hyde GE, Campbell WH |
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Title | High-level expression in Escherichia coli of the catalytically active flavin domain of corn leaf NADH:nitrate reductase and its comparison to human NADH:cytochrome B5 reductase. |
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[6] |
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PubMed ID | 2123873 |
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Journal | J Biol Chem |
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Year | 1990 |
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Volume | 265 |
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Pages | 21709-13 |
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Authors | Strittmatter P, Hackett CS, Korza G, Ozols J |
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Title | Characterization of the covalent cross-links of the active sites of amidinated cytochrome b5 and NADH:cytochrome b5 reductase. |
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[7] |
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PubMed ID | 2019583 |
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Journal | J Biol Chem |
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Year | 1991 |
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Volume | 266 |
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Pages | 7531-6 |
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Authors | Shirabe K, Yubisui T, Nishino T, Takeshita M |
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Title | Role of cysteine residues in human NADH-cytochrome b5 reductase studied by site-directed mutagenesis. Cys-273 and Cys-283 are located close to the NADH-binding site but are not catalytically essential. |
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[8] |
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PubMed ID | 1898726 |
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Journal | J Biol Chem |
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Year | 1991 |
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Volume | 266 |
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Pages | 66-70 |
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Authors | Yubisui T, Shirabe K, Takeshita M, Kobayashi Y, Fukumaki Y, Sakaki Y, Takano T |
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Title | Structural role of serine 127 in the NADH-binding site of human NADH-cytochrome b5 reductase. |
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[9] |
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PubMed ID | 1370824 |
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Journal | J Biol Chem |
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Year | 1992 |
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Volume | 267 |
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Pages | 2519-23 |
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Authors | Strittmatter P, Kittler JM, Coghill JE, Ozols J |
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Title | Characterization of lysyl residues of NADH-cytochrome b5 reductase implicated in charge-pairing with active-site carboxyl residues of cytochrome b5 by site-directed mutagenesis of an expression vector for the flavoprotein. |
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[10] |
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Comments | X-ray crystallography |
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PubMed ID | 7893687 |
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Journal | Biochemistry |
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Year | 1995 |
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Volume | 34 |
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Pages | 2763-7 |
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Authors | Nishida H, Inaka K, Yamanaka M, Kaida S, Kobayashi K, Miki K |
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Title | Crystal structure of NADH-cytochrome b5 reductase from pig liver at 2.4 A resolution. |
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Related PDB | 1ndh |
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[11] |
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PubMed ID | 7890048 |
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Journal | FEBS Lett |
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Year | 1995 |
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Volume | 361 |
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Pages | 97-100 |
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Authors | Nishida H, Inaka K, Miki K |
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Title | Specific arrangement of three amino acid residues for flavin-binding barrel structures in NADH-cytochrome b5 reductase and the other flavin-dependent reductases. |
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[12] |
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PubMed ID | 8880927 |
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Journal | Proteins |
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Year | 1996 |
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Volume | 26 |
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Pages | 32-41 |
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Authors | Nishida H, Miki K |
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Title | Electrostatic properties deduced from refined structures of NADH-cytochrome b5 reductase and the other flavin-dependent reductases: pyridine nucleotide-binding and interaction with an electron-transfer partner. |
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[13] |
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PubMed ID | 9602031 |
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Journal | Biochim Biophys Acta |
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Year | 1998 |
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Volume | 1384 |
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Pages | 16-22 |
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Authors | Shirabe K, Nagai T, Yubisui T, Takeshita M |
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Title | Electrostatic interaction between NADH-cytochrome b5 reductase and cytochrome b5 studied by site-directed mutagenesis. |
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[14] |
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PubMed ID | 10082957 |
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Journal | Biochim Biophys Acta |
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Year | 1999 |
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Volume | 1430 |
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Pages | 290-301 |
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Authors | Kimura S, Emi Y, Ikushiro S, Iyanagi T |
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Title | Systematic mutations of highly conserved His49 and carboxyl-terminal of recombinant porcine liver NADH-cytochrome b5 reductase solubilized domain. |
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[15] |
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PubMed ID | 10622712 |
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Journal | FEBS Lett |
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Year | 1999 |
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Volume | 462 |
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Pages | 283-8 |
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Authors | Lamb DC, Kelly DE, Manning NJ, Kaderbhai MA, Kelly SL |
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Title | Biodiversity of the P450 catalytic cycle: yeast cytochrome b5/NADH cytochrome b5 reductase complex efficiently drives the entire sterol 14-demethylation (CYP51) reaction. |
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[16] |
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PubMed ID | 11695905 |
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Journal | Biochemistry |
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Year | 2001 |
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Volume | 40 |
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Pages | 13574-82 |
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Authors | Bewley MC, Marohnic CC, Barber MJ |
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Title | The structure and biochemistry of NADH-dependent cytochrome b5 reductase are now consistent. |
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Related PDB | 1i7p,1ib0 |
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[17] |
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PubMed ID | 11574067 |
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Journal | J Biochem (Tokyo) |
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Year | 2001 |
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Volume | 130 |
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Pages | 481-90 |
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Authors | Kimura S, Nishida H, Iyanagi T |
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Title | Effects of flavin-binding motif amino acid mutations in the NADH-cytochrome b5 reductase catalytic domain on protein stability and catalysis. |
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[18] |
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PubMed ID | 14503867 |
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Journal | Biochemistry |
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Year | 2003 |
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Volume | 42 |
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Pages | 11170-82 |
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Authors | Marohnic CC, Bewley MC, Barber MJ |
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Title | Engineering and characterization of a NADPH-utilizing cytochrome b5 reductase. |
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[19] |
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PubMed ID | 12459552 |
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Journal | J Biol Chem |
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Year | 2003 |
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Volume | 278 |
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Pages | 3580-9 |
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Authors | Kimura S, Kawamura M, Iyanagi T |
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Title | Role of Thr(66) in porcine NADH-cytochrome b5 reductase in catalysis and control of the rate-limiting step in electron transfer. |
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[20] |
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PubMed ID | 14609324 |
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Journal | Biochemistry |
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Year | 2003 |
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Volume | 42 |
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Pages | 13145-51 |
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Authors | Bewley MC, Davis CA, Marohnic CC, Taormina D, Barber MJ |
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Title | The structure of the S127P mutant of cytochrome b5 reductase that causes methemoglobinemia shows the AMP moiety of the flavin occupying the substrate binding site. |
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Related PDB | 1qx4 |
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[21] |
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PubMed ID | 15488472 |
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Journal | Arch Biochem Biophys |
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Year | 2004 |
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Volume | 431 |
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Pages | 233-44 |
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Authors | Davis CA, Crowley LJ, Barber MJ |
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Title | Cytochrome b5 reductase: the roles of the recessive congenital methemoglobinemia mutants P144L, L148P, and R159*. |
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[22] |
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PubMed ID | 15502298 |
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Journal | Acta Crystallogr D Biol Crystallogr |
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Year | 2004 |
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Volume | 60 |
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Pages | 1929-34 |
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Authors | Bando S, Takano T, Yubisui T, Shirabe K, Takeshita M, Nakagawa A |
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Title | Structure of human erythrocyte NADH-cytochrome b5 reductase. |
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Related PDB | 1umk |
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created | updated |
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2004-12-20 | 2009-02-26 |
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