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.
Referencesedit
^ abcGRCh38: Ensembl release 89: ENSG00000166347 – Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000024646 – Ensembl, May 2017
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
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): 4975–8. doi:10.1021/bi00642a006. PMID 199233.
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): 5388–96. doi:10.1016/S0021-9258(18)50608-6. PMID 221468.
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): 4197–203. doi:10.1002/j.1460-2075.1992.tb05513.x. PMC556930. PMID 1396600.
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): 38–44. doi:10.1016/0006-291X(91)91776-9. PMID 1712589.
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): 302–8. doi:10.1016/0888-7543(91)90136-3. PMID 1840560.
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): 21709–13. doi:10.1016/S0021-9258(18)45798-5. PMID 2123873.
Ozols J (1989). "Structure of cytochrome b5 and its topology in the microsomal membrane". Biochim. Biophys. Acta. 997 (1–2): 121–30. doi:10.1016/0167-4838(89)90143-X. PMID 2752049.
Yoo M, Steggles AW (1988). "The complete nucleotide sequence of human liver cytochrome b5 mRNA". Biochem. Biophys. Res. Commun. 156 (1): 576–80. doi:10.1016/S0006-291X(88)80881-7. PMID 3178851.
Hegesh E, Hegesh J, Kaftory A (1986). "Congenital methemoglobinemia with a deficiency of cytochrome b5". N. Engl. J. Med. 314 (12): 757–61. doi:10.1056/NEJM198603203141206. PMID 3951505.
Abe K, Kimura S, Kizawa R, et al. (1985). "Amino acid sequences of cytochrome b5 from human, porcine, and bovine erythrocytes and comparison with liver microsomal cytochrome b5". J. Biochem. 97 (6): 1659–68. doi:10.1093/oxfordjournals.jbchem.a135224. PMID 4030743.
Strittmatter P, Spatz L, Corcoran D, et al. (1975). "Purification and properties of rat liver microsomal stearyl coenzyme A desaturase". Proc. Natl. Acad. Sci. U.S.A. 71 (11): 4565–9. doi:10.1073/pnas.71.11.4565. PMC433928. PMID 4373719.
Rashid MA, Hagihara B, Kobayashi M, et al. (1974). "Structural studies of cytochrome b5. 3. Sequential studies on human liver cytochrome b5". J. Biochem. 74 (5): 985–1002. PMID 4770377.
Nóbrega 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): 1706–17. doi:10.1016/S0021-9258(18)62368-3. PMID 4993957.
Ozols J (1972). "Cytochrome b 5 from a normal human liver. Isolation and the partial amino acid sequence". J. Biol. Chem. 247 (7): 2242–5. doi:10.1016/S0021-9258(19)45520-8. PMID 5062820.
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): 5184–9. doi:10.1016/S0021-9258(19)70768-6. PMID 6102994.
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 (1–2): 69–74. doi:10.1016/0014-5793(95)00797-D. PMID 7649306. S2CID 26031756.
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): 894–900. doi:10.1006/bbrc.1995.1582. PMID 7733981.
Giordano SJ, Yoo M, Ward DC, et al. (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): 615–8. doi:10.1007/BF00420948. PMID 8262522. S2CID 28828499.
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): 14741–50. doi:10.1021/bi9719399. PMID 9398194.
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): 293–6. doi:10.1042/bj3320293. PMC1219480. PMID 9601054.
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cytochrome, type, cytochrome, form, gene, name, cyb5a, human, microsomal, cytochrome, cyb5aavailable, structurespdbortholog, search, pdbe, rcsblist, codes2i96identifiersaliasescyb5a, cyb5, mcb5, cytochrome, type, metagexternal, idsomim, 613218, 1926952, homolo. Cytochrome b5 form A gene name CYB5A is a human microsomal cytochrome b5 5 CYB5AAvailable structuresPDBOrtholog search PDBe RCSBList of PDB id codes2I96IdentifiersAliasesCYB5A CYB5 MCB5 Cytochrome b5 type A cytochrome b5 type A METAGExternal IDsOMIM 613218 MGI 1926952 HomoloGene 41475 GeneCards CYB5AGene location Human Chr Chromosome 18 human 1 Band18q22 3Start74 250 846 bp 1 End74 291 973 bp 1 Gene location Mouse Chr Chromosome 18 mouse 2 Band18 E4 18 57 53 cMStart84 856 829 bp 2 End84 897 996 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed inkidney tubuleright lobe of liverkidneyrenal medullaglomeruluspancreatic ductal celljejunal mucosametanephric glomerulusbody of pancreasgallbladderTop expressed inolfactory epitheliumproximal tubulegallbladderkidneyirisleft lobe of liverwhite adipose tissuelacrimal glandcarotid bodysubcutaneous adipose tissueMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functioncytochrome c oxidase activity aldo keto reductase NADP activity metal ion binding heme binding enzyme bindingCellular componentorganelle membrane integral component of membrane endoplasmic reticulum membrane membrane intracellular membrane bounded organelle mitochondrial outer membrane endoplasmic reticulum mitochondrion extracellular exosome cytoplasm cytosolBiological processresponse to cadmium ion L ascorbic acid metabolic process proton transmembrane transport electron transport chainSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez1528109672EnsemblENSG00000166347ENSMUSG00000024646UniProtP00167P56395RefSeq mRNA NM 001190807NM 001914NM 148923NM 025797NM 001348159RefSeq protein NP 001177736NP 001905NP 683725NP 080073NP 001335088Location UCSC Chr 18 74 25 74 29 MbChr 18 84 86 84 9 MbPubMed search 3 4 WikidataView Edit HumanView Edit Mouse 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 a b c GRCh38 Ensembl release 89 ENSG00000166347 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000024646 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Mouse PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Entrez Gene CYB5A Cytochrome b5 form A Further reading editNg 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 8 doi 10 1021 bi00642a006 PMID 199233 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 96 doi 10 1016 S0021 9258 18 50608 6 PMID 221468 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 203 doi 10 1002 j 1460 2075 1992 tb05513 x PMC 556930 PMID 1396600 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 44 doi 10 1016 0006 291X 91 91776 9 PMID 1712589 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 8 doi 10 1016 0888 7543 91 90136 3 PMID 1840560 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 13 doi 10 1016 S0021 9258 18 45798 5 PMID 2123873 Ozols J 1989 Structure of cytochrome b5 and its topology in the microsomal membrane Biochim Biophys Acta 997 1 2 121 30 doi 10 1016 0167 4838 89 90143 X PMID 2752049 Yoo M Steggles AW 1988 The complete nucleotide sequence of human liver cytochrome b5 mRNA Biochem Biophys Res Commun 156 1 576 80 doi 10 1016 S0006 291X 88 80881 7 PMID 3178851 Hegesh E Hegesh J Kaftory A 1986 Congenital methemoglobinemia with a deficiency of cytochrome b5 N Engl J Med 314 12 757 61 doi 10 1056 NEJM198603203141206 PMID 3951505 Abe K Kimura S Kizawa R et al 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 68 doi 10 1093 oxfordjournals jbchem a135224 PMID 4030743 Strittmatter P Spatz L Corcoran D et al 1975 Purification and properties of rat liver microsomal stearyl coenzyme A desaturase Proc Natl Acad Sci U S A 71 11 4565 9 doi 10 1073 pnas 71 11 4565 PMC 433928 PMID 4373719 Rashid MA Hagihara B Kobayashi M et al 1974 Structural studies of cytochrome b5 3 Sequential studies on human liver cytochrome b5 J Biochem 74 5 985 1002 PMID 4770377 Nobrega 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 17 doi 10 1016 S0021 9258 18 62368 3 PMID 4993957 Ozols J 1972 Cytochrome b 5 from a normal human liver Isolation and the partial amino acid sequence J Biol Chem 247 7 2242 5 doi 10 1016 S0021 9258 19 45520 8 PMID 5062820 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 9 doi 10 1016 S0021 9258 19 70768 6 PMID 6102994 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 2 69 74 doi 10 1016 0014 5793 95 00797 D PMID 7649306 S2CID 26031756 Li XR Giordano SJ Yoo M Steggles AW 1995 The isolation and characterization of the human cytochrome b5 gene Biochem Biophys Res Commun 209 3 894 900 doi 10 1006 bbrc 1995 1582 PMID 7733981 Giordano SJ Yoo M Ward DC et al 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 8 doi 10 1007 BF00420948 PMID 8262522 S2CID 28828499 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 50 doi 10 1021 bi9719399 PMID 9398194 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 6 doi 10 1042 bj3320293 PMC 1219480 PMID 9601054 nbsp This membrane protein related article is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title Cytochrome b5 type A amp oldid 1170148562, wikipedia, wiki, book, books, library,
