Cytochrome b5, type A

From Wikipedia, the free encyclopedia
  (Redirected from CYB5A)
Jump to: navigation, search
Cytochrome b5 type A (microsomal)
Protein CYB5A PDB 1cyo.png
PDB rendering based on 1cyo.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols CYB5A ; CYB5; MCB5
External IDs OMIM613218 MGI1926952 HomoloGene41475 ChEMBL: 6170 GeneCards: CYB5A Gene
RNA expression pattern
PBB GE CYB5A 215726 s at tn.png
PBB GE CYB5A 207843 x at tn.png
PBB GE CYB5A 209366 x at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 1528 109672
Ensembl ENSG00000166347 ENSMUSG00000024646
UniProt P00167 P56395
RefSeq (mRNA) NM_001190807 NM_025797
RefSeq (protein) NP_001177736 NP_080073
Location (UCSC) Chr 18:
71.92 – 71.96 Mb
Chr 18:
84.85 – 84.88 Mb
PubMed search [1] [2]

Cytochrome b5, form A (gene name CYB5A), is a human microsomal cytochrome b5.[1]

Cytochrome b5 is a membrane bound hemoprotein which function 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): 4975–8. 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. 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. 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. 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. 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. 
  • 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. 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. 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. 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. 
  • 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. 
  • 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): 293–6. PMC 1219480. PMID 9601054.