Cytochrome b5, type A

Cytochrome b5 type A (microsomal)
PDB rendering based on 1cyo.
Available structures PDB 1cyo, 1do9, 1ehb, 1es1, 1f03, 1f04, 1i5u, 1j0q, 1lqx, 1lr6, 1m20, 1m2i, 1m2m, 1m59, 1nx7, 1sh4, 1u9m, 1u9u
Identifiers
Symbols	CYB5A; CYB5; MCB5
External IDs	OMIM: 613218 MGI: 1926952 HomoloGene: 41475 GeneCards: CYB5A Gene
Gene Ontology Molecular function • aldo-keto reductase (NADP) activity • cytochrome-c oxidase activity • enzyme binding • heme binding • metal ion binding Cellular component • cytoplasm • mitochondrion • mitochondrial outer membrane • mitochondrial outer membrane • endoplasmic reticulum • endoplasmic reticulum membrane • microsome • membrane • integral to membrane Biological process • vitamin metabolic process • water-soluble vitamin metabolic process • transport • electron transport chain Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	1528	109672
Ensembl	ENSG00000166347	ENSMUSG00000024646
UniProt	P00167	Q544Z9
RefSeq (mRNA)	NM_001190807.2	NM_025797.3
RefSeq (protein)	NP_001177736.1	NP_080073.1
Location (UCSC)	Chr 18: 71.92 – 71.96 Mb	Chr 18: 85.02 – 85.05 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

1. ^ "Entrez Gene: CYB5A Cytochrome b5, form A". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1528. 

Further reading

• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=556930. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=433928. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1219480. 

This membrane protein-related article is a stub. You can help Wikipedia by expanding it.v · Categories: Human proteins Membrane protein stubs Transmembrane proteins Wikimedia Foundation. 2010. Игры ⚽ Нужно решить контрольную? 1910 in Argentine football USS Arthur (1855) Look at other dictionaries: Cytochrome b5 — Rat cytochrome b5 bound to heme Identifiers Symbol CYB5A Alt. symbols CYB5 …   Wikipedia cytochrome P450 — (= cytochrome m; CYP) Large group of mixed function oxidases of the cytochrome b type, involved, among other things, in steroid hydroxylation reactions in the adrenal cortex. In liver they are found in the microsomal fraction and can be induced… …   Dictionary of molecular biology Cytochrome b — Mitochondrial cytochrome bc1 complex Identifiers Symbol Cytochrom B N Pfam …   Wikipedia Cytochrome P450 — Oxidase (CYP2C9) Identifiers Symbol p450 Pfam …   Wikipedia Cytochrome b6f complex — Crystal structure of the cytochrome b6f complex from C. reinhardtii (1q90). Hydrocarbon boundaries of the lipid bilayer are shown by red and blue dots …   Wikipedia Cytochrome — c with heme c. Cytochromes are, in general, membrane bound hemoproteins that contain heme groups and carry out electron transport. They are found either as monomeric proteins (e.g., cytochrome c) or as subunits of bigger enzymatic complexes that… …   Wikipedia Cytochrome c — Cytochrome c, somatic Three dimensional structure of cytochrome c (green) with a heme molecule coordinating a central Iron atom (orange) …   Wikipedia Cytochrome c assembly protein family — Cytochrome C assembly protein Identifiers Symbol Cytochrom C asm Pfam PF01578 Pfam clan C …   Wikipedia Cytochrome p450 — Le cytochrome p450 (CYP) a une importance particulière en médecine et en pharmacie. En effet, cette enzyme est très impliquée dans la dégradation des molécules exogènes (xénobiotiques), en particulier des médicaments. Plus le cytochrome p450 est… …   Wikipédia en Français Cytochrome p450 c17 — Cytochrome p450 Le cytochrome p450 (CYP) a une importance particulière en médecine et en pharmacie. En effet, cette enzyme est très impliquée dans la dégradation des molécules exogènes (xénobiotiques), en particulier des médicaments. Plus le… …   Wikipédia en Français 18+ © Academic, 2000-2024 Contact us: Technical Support, Advertising Dictionaries export, created on PHP, Joomla, Drupal, WordPress, MODx. Mark and share Search through all dictionaries Translate… Search Internet Share the article and excerpts Direct link … Do a right-click on the link above and select “Copy Link”