[{"@context":"http:\/\/schema.org\/","@type":"BlogPosting","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/cytochrome-b5-type-a-wikipedia\/#BlogPosting","mainEntityOfPage":"https:\/\/wiki.edu.vn\/en\/wiki24\/cytochrome-b5-type-a-wikipedia\/","headline":"Cytochrome b5, type A – Wikipedia","name":"Cytochrome b5, type A – Wikipedia","description":"From Wikipedia, the free encyclopedia Protein-coding gene in the species Homo sapiens Cytochrome b5, form A (gene name CYB5A), is","datePublished":"2018-05-11","dateModified":"2018-05-11","author":{"@type":"Person","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/#Person","name":"lordneo","url":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/","image":{"@type":"ImageObject","@id":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","url":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","height":96,"width":96}},"publisher":{"@type":"Organization","name":"Enzyklop\u00e4die","logo":{"@type":"ImageObject","@id":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","url":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","width":600,"height":60}},"image":{"@type":"ImageObject","@id":"https:\/\/upload.wikimedia.org\/wikipedia\/commons\/thumb\/c\/cb\/PDB_1cyo_EBI.jpg\/180px-PDB_1cyo_EBI.jpg","url":"https:\/\/upload.wikimedia.org\/wikipedia\/commons\/thumb\/c\/cb\/PDB_1cyo_EBI.jpg\/180px-PDB_1cyo_EBI.jpg","height":"135","width":"180"},"url":"https:\/\/wiki.edu.vn\/en\/wiki24\/cytochrome-b5-type-a-wikipedia\/","wordCount":6506,"articleBody":"From Wikipedia, the free encyclopediaProtein-coding gene in the species Homo sapiensCytochrome b5, form A (gene name CYB5A), is a human microsomal cytochrome b5.[5]Cytochrome b5 is a membrane bound hemoprotein which functions as an electron carrier for several membrane bound oxygenases. It has two isoforms produced by alternative splicing. Isoform 1 is bound to the cytoplasmic side of the endoplasmic reticulum. It has a C-terminal transmembrane alpha-helix. Isoform 2 was found in cytoplasm. Defects in CYB5A are the cause of type IV hereditary methemoglobinemia.References[edit]Further reading[edit]Ng S, Smith MB, Smith HT, Millett F (1977). “Effect of modification of individual cytochrome c lysines on the reaction with cytochrome b5”. Biochemistry. 16 (23): 4975\u20138. doi:10.1021\/bi00642a006. PMID\u00a0199233.Dailey HA, Strittmatter P (1979). “Modification and identification of cytochrome b5 carboxyl groups involved in protein-protein interaction with cytochrome b5 reductase”. J. Biol. Chem. 254 (12): 5388\u201396. doi:10.1016\/S0021-9258(18)50608-6. PMID\u00a0221468.Mitoma J, Ito A (1992). “The carboxy-terminal 10 amino acid residues of cytochrome b5 are necessary for its targeting to the endoplasmic reticulum”. EMBO J. 11 (11): 4197\u2013203. doi:10.1002\/j.1460-2075.1992.tb05513.x. PMC\u00a0556930. PMID\u00a01396600.Giordano SJ, Steggles AW (1991). “The human liver and reticulocyte cytochrome b5 mRNAs are products from a single gene”. Biochem. Biophys. Res. Commun. 178 (1): 38\u201344. doi:10.1016\/0006-291X(91)91776-9. PMID\u00a01712589.Shephard EA, Povey S, Spurr NK, Phillips IR (1992). “Chromosomal localization of a cytochrome b5 gene to human chromosome 18 and a cytochrome b5 pseudogene to the X chromosome”. Genomics. 11 (2): 302\u20138. doi:10.1016\/0888-7543(91)90136-3. PMID\u00a01840560.Strittmatter P, Hackett CS, Korza G, Ozols J (1991). “Characterization of the covalent cross-links of the active sites of amidinated cytochrome b5 and NADH:cytochrome b5 reductase”. J. Biol. Chem. 265 (35): 21709\u201313. doi:10.1016\/S0021-9258(18)45798-5. PMID\u00a02123873.Ozols J (1989). “Structure of cytochrome b5 and its topology in the microsomal membrane”. Biochim. Biophys. Acta. 997 (1\u20132): 121\u201330. doi:10.1016\/0167-4838(89)90143-X. PMID\u00a02752049.Yoo M, Steggles AW (1988). “The complete nucleotide sequence of human liver cytochrome b5 mRNA”. Biochem. Biophys. Res. Commun. 156 (1): 576\u201380. doi:10.1016\/S0006-291X(88)80881-7. PMID\u00a03178851.Hegesh E, Hegesh J, Kaftory A (1986). “Congenital methemoglobinemia with a deficiency of cytochrome b5”. N. Engl. J. Med. 314 (12): 757\u201361. doi:10.1056\/NEJM198603203141206. PMID\u00a03951505.Abe K, Kimura S, Kizawa R,  et\u00a0al. (1985). “Amino acid sequences of cytochrome b5 from human, porcine, and bovine erythrocytes and comparison with liver microsomal cytochrome b5”. J. Biochem. 97 (6): 1659\u201368. doi:10.1093\/oxfordjournals.jbchem.a135224. PMID\u00a04030743.Strittmatter P, Spatz L, Corcoran D,  et\u00a0al. (1975). “Purification and properties of rat liver microsomal stearyl coenzyme A desaturase”. Proc. Natl. Acad. Sci. U.S.A. 71 (11): 4565\u20139. doi:10.1073\/pnas.71.11.4565. PMC\u00a0433928. PMID\u00a04373719.Rashid MA, Hagihara B, Kobayashi M,  et\u00a0al. (1974). “Structural studies of cytochrome b5. 3. Sequential studies on human liver cytochrome b5”. J. Biochem. 74 (5): 985\u20131002. PMID\u00a04770377.N\u00f3brega FG, Ozols J (1971). “Amino acid sequences of tryptic peptides of cytochromes b5 from microsomes of human, monkey, porcine, and chicken liver”. J. Biol. Chem. 246 (6): 1706\u201317. doi:10.1016\/S0021-9258(18)62368-3. PMID\u00a04993957.Ozols J (1972). “Cytochrome b 5 from a normal human liver. Isolation and the partial amino acid sequence”. J. Biol. Chem. 247 (7): 2242\u20135. doi:10.1016\/S0021-9258(19)45520-8. PMID\u00a05062820.Dailey HA, Strittmatter P (1980). “Characterization of the interaction of amphipathic cytochrome b5 with stearyl coenzyme A desaturase and NADPH:cytochrome P-450 reductase”. J. Biol. Chem. 255 (11): 5184\u20139. doi:10.1016\/S0021-9258(19)70768-6. PMID\u00a06102994.De Silvestris M, D’Arrigo A, Borgese N (1995). “The targeting information of the mitochondrial outer membrane isoform of cytochrome b5 is contained within the carboxyl-terminal region”. FEBS Lett. 370 (1\u20132): 69\u201374. doi:10.1016\/0014-5793(95)00797-D. PMID\u00a07649306. S2CID\u00a026031756.Li XR, Giordano SJ, Yoo M, Steggles AW (1995). “The isolation and characterization of the human cytochrome b5 gene”. Biochem. Biophys. Res. Commun. 209 (3): 894\u2013900. doi:10.1006\/bbrc.1995.1582. PMID\u00a07733981.Giordano SJ, Yoo M, Ward DC,  et\u00a0al. (1994). “The human cytochrome b5 gene and two of its pseudogenes are located on chromosomes 18q23, 14q31-32.1 and 20p11.2, respectively”. Hum. Genet. 92 (6): 615\u20138. doi:10.1007\/BF00420948. PMID\u00a08262522. S2CID\u00a028828499.Guengerich FP, Johnson WW (1998). “Kinetics of ferric cytochrome P450 reduction by NADPH-cytochrome P450 reductase: rapid reduction in the absence of substrate and variations among cytochrome P450 systems”. Biochemistry. 36 (48): 14741\u201350. doi:10.1021\/bi9719399. PMID\u00a09398194.Lee-Robichaud P, Akhtar ME, Akhtar M (1998). “Control of androgen biosynthesis in the human through the interaction of Arg347 and Arg358 of CYP17 with cytochrome b5”. Biochem. J. 332. ( Pt 2) (2): 293\u20136. doi:10.1042\/bj3320293. PMC\u00a01219480. PMID\u00a09601054.PDB gallery1cyo: BOVINE CYTOCHROME B(5)1do9: SOLUTION STRUCTURE OF OXIDIZED MICROSOMAL RABBIT CYTOCHROME B5. FACTORS DETERMINING THE HETEROGENEOUS BINDING OF THE HEME.1ehb: CRYSTAL STRUCTURE OF RECOMBINANT TRYPSIN-SOLUBILIZED FRAGMENT OF CYTOCHROME B51es1: CRYSTAL STRUCTURE OF VAL61HIS MUTANT OF TRYPSIN-SOLUBILIZED FRAGMENT OF CYTOCHROME B51f03: SOLUTION STRUCTURE OF OXIDIZED BOVINE MICROSOMAL CYTOCHROME B5 MUTANT (E44A, E48A, E56A, D60A) AND ITS INTERACTION WITH CYTOCHROME C1f04: SOLUTION STRUCTURE OF OXIDIZED BOVINE MICROSOMAL CYTOCHROME B5 MUTANT (E44A, E48A, E56A, D60A) AND ITS INTERACTION WITH CYTOCHROME C1i5u: SOLUTION STRUCTURE OF CYTOCHROME B5 TRIPLE MUTANT (E48A\/E56A\/D60A)1j0q: Solution Structure of Oxidized Bovine Microsomal Cytochrome b5 mutant V61H1lqx: Crystal structure of V45E mutant of cytochrome b51lr6: Crystal structure of V45Y mutant of cytochrome b51m20: Crystal Structure of F35Y Mutant of Trypsin-solubilized Fragment of Cytochrome b51m2i: Crystal structure of E44A\/E56A mutant of cytochrome b51m2m: Crystal structure of E44A\/E48A\/E56A\/D60A mutant of cytochrome b51m59: Crystal Structure of P40V Mutant of Trypsin-solubilized Fragment of Cytochrome b51nx7: Solution Structure of Oxidized Bovine Microsomal Cytochrome B51sh4: Solution structure of oxidized bovine microsomal cytochrome B5 Mutant V45H1u9m: Crystal structure of F58W mutant of cytochrome b51u9u: Crystal structure of F58Y mutant of cytochrome b5  "},{"@context":"http:\/\/schema.org\/","@type":"BreadcrumbList","itemListElement":[{"@type":"ListItem","position":1,"item":{"@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/#breadcrumbitem","name":"Enzyklop\u00e4die"}},{"@type":"ListItem","position":2,"item":{"@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/cytochrome-b5-type-a-wikipedia\/#breadcrumbitem","name":"Cytochrome b5, type A – Wikipedia"}}]}]