Cytochrome b5, type A

Cytochrome b5 type A (microsomal)

PDB rendering based on 1cyo.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
2I96

Identifiers

Symbols

CYB5A ; CYB5; MCB5

External IDs

OMIM: 613218 MGI: 1926952 HomoloGene: 41475 ChEMBL: 6170 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	• mitochondrial outer membrane • endoplasmic reticulum membrane • membrane • integral component of membrane • extracellular exosome
Biological process	• vitamin metabolic process • water-soluble vitamin metabolic process • L-ascorbic acid metabolic process • small molecule metabolic process • response to cadmium ion • oxidation-reduction process • hydrogen ion transmembrane transport
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 18:
74.25 – 74.29 Mb

Chr 18:
84.85 – 84.88 Mb

PubMed search

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

↑ "Entrez Gene: CYB5A Cytochrome b5, form A".

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.

PDB gallery

1cyo: 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 B5

1es1: CRYSTAL STRUCTURE OF VAL61HIS MUTANT OF TRYPSIN-SOLUBILIZED FRAGMENT OF CYTOCHROME B5

1f03: SOLUTION STRUCTURE OF OXIDIZED BOVINE MICROSOMAL CYTOCHROME B5 MUTANT (E44A, E48A, E56A, D60A) AND ITS INTERACTION WITH CYTOCHROME C

1f04: SOLUTION STRUCTURE OF OXIDIZED BOVINE MICROSOMAL CYTOCHROME B5 MUTANT (E44A, E48A, E56A, D60A) AND ITS INTERACTION WITH CYTOCHROME C

1i5u: SOLUTION STRUCTURE OF CYTOCHROME B5 TRIPLE MUTANT (E48A/E56A/D60A)

1j0q: Solution Structure of Oxidized Bovine Microsomal Cytochrome b5 mutant V61H

1lqx: Crystal structure of V45E mutant of cytochrome b5

1lr6: Crystal structure of V45Y mutant of cytochrome b5

1m20: Crystal Structure of F35Y Mutant of Trypsin-solubilized Fragment of Cytochrome b5

1m2i: Crystal structure of E44A/E56A mutant of cytochrome b5

1m2m: Crystal structure of E44A/E48A/E56A/D60A mutant of cytochrome b5

1m59: Crystal Structure of P40V Mutant of Trypsin-solubilized Fragment of Cytochrome b5

1nx7: Solution Structure of Oxidized Bovine Microsomal Cytochrome B5

1sh4: Solution structure of oxidized bovine microsomal cytochrome B5 Mutant V45H

1u9m: Crystal structure of F58W mutant of cytochrome b5

1u9u: Crystal structure of F58Y mutant of cytochrome b5

This article is issued from Wikipedia - version of the Tuesday, May 05, 2015. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.

Cytochrome b5, type A

References

Further reading