| 释义 |
- References
- Further reading
{{Infobox_gene}}Cytochrome b5, form A (gene name CYB5A), is a human microsomal cytochrome b5.[1]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. References1. ^{{cite web | title = Entrez Gene: CYB5A Cytochrome b5, form A| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1528| accessdate = }}
Further reading{{refbegin | 2}}- {{cite journal | vauthors=Ng S, Smith MB, Smith HT, Millett F |title=Effect of modification of individual cytochrome c lysines on the reaction with cytochrome b5. |journal=Biochemistry |volume=16 |issue= 23 |pages= 4975–8 |year= 1977 |pmid= 199233 |doi=10.1021/bi00642a006 }}
- {{cite journal | vauthors=Dailey HA, Strittmatter P |title=Modification and identification of cytochrome b5 carboxyl groups involved in protein-protein interaction with cytochrome b5 reductase. |journal=J. Biol. Chem. |volume=254 |issue= 12 |pages= 5388–96 |year= 1979 |pmid= 221468 |doi= }}
- {{cite journal | vauthors=Mitoma J, Ito A |title=The carboxy-terminal 10 amino acid residues of cytochrome b5 are necessary for its targeting to the endoplasmic reticulum. |journal=EMBO J. |volume=11 |issue= 11 |pages= 4197–203 |year= 1992 |pmid= 1396600 |doi= | pmc=556930 }}
- {{cite journal | vauthors=Giordano SJ, Steggles AW |title=The human liver and reticulocyte cytochrome b5 mRNAs are products from a single gene. |journal=Biochem. Biophys. Res. Commun. |volume=178 |issue= 1 |pages= 38–44 |year= 1991 |pmid= 1712589 |doi=10.1016/0006-291X(91)91776-9 }}
- {{cite journal | vauthors=Shephard EA, Povey S, Spurr NK, Phillips IR |title=Chromosomal localization of a cytochrome b5 gene to human chromosome 18 and a cytochrome b5 pseudogene to the X chromosome. |journal=Genomics |volume=11 |issue= 2 |pages= 302–8 |year= 1992 |pmid= 1840560 |doi=10.1016/0888-7543(91)90136-3 }}
- {{cite journal | vauthors=Strittmatter P, Hackett CS, Korza G, Ozols J |title=Characterization of the covalent cross-links of the active sites of amidinated cytochrome b5 and NADH:cytochrome b5 reductase. |journal=J. Biol. Chem. |volume=265 |issue= 35 |pages= 21709–13 |year= 1991 |pmid= 2123873 |doi= }}
- {{cite journal | author=Ozols J |title=Structure of cytochrome b5 and its topology in the microsomal membrane. |journal=Biochim. Biophys. Acta |volume=997 |issue= 1-2 |pages= 121–30 |year= 1989 |pmid= 2752049 |doi=10.1016/0167-4838(89)90143-X }}
- {{cite journal | vauthors=Yoo M, Steggles AW |title=The complete nucleotide sequence of human liver cytochrome b5 mRNA. |journal=Biochem. Biophys. Res. Commun. |volume=156 |issue= 1 |pages= 576–80 |year= 1988 |pmid= 3178851 |doi=10.1016/S0006-291X(88)80881-7 }}
- {{cite journal | vauthors=Hegesh E, Hegesh J, Kaftory A |title=Congenital methemoglobinemia with a deficiency of cytochrome b5. |journal=N. Engl. J. Med. |volume=314 |issue= 12 |pages= 757–61 |year= 1986 |pmid= 3951505 |doi=10.1056/NEJM198603203141206 }}
- {{cite journal | vauthors=Abe K, Kimura S, Kizawa R |title=Amino acid sequences of cytochrome b5 from human, porcine, and bovine erythrocytes and comparison with liver microsomal cytochrome b5. |journal=J. Biochem. |volume=97 |issue= 6 |pages= 1659–68 |year= 1985 |pmid= 4030743 |doi= |display-authors=etal}}
- {{cite journal | vauthors=Strittmatter P, Spatz L, Corcoran D |title=Purification and properties of rat liver microsomal stearyl coenzyme A desaturase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=71 |issue= 11 |pages= 4565–9 |year= 1975 |pmid= 4373719 |doi=10.1073/pnas.71.11.4565 | pmc=433928 |display-authors=etal}}
- {{cite journal | vauthors=Rashid MA, Hagihara B, Kobayashi M |title=Structural studies of cytochrome b5. 3. Sequential studies on human liver cytochrome b5. |journal=J. Biochem. |volume=74 |issue= 5 |pages= 985–1002 |year= 1974 |pmid= 4770377 |doi= |display-authors=etal}}
- {{cite journal | vauthors=Nóbrega FG, Ozols J |title=Amino acid sequences of tryptic peptides of cytochromes b5 from microsomes of human, monkey, porcine, and chicken liver. |journal=J. Biol. Chem. |volume=246 |issue= 6 |pages= 1706–17 |year= 1971 |pmid= 4993957 |doi= }}
- {{cite journal | author=Ozols J |title=Cytochrome b 5 from a normal human liver. Isolation and the partial amino acid sequence. |journal=J. Biol. Chem. |volume=247 |issue= 7 |pages= 2242–5 |year= 1972 |pmid= 5062820 |doi= }}
- {{cite journal | vauthors=Dailey HA, Strittmatter P |title=Characterization of the interaction of amphipathic cytochrome b5 with stearyl coenzyme A desaturase and NADPH:cytochrome P-450 reductase. |journal=J. Biol. Chem. |volume=255 |issue= 11 |pages= 5184–9 |year= 1980 |pmid= 6102994 |doi= }}
- {{cite journal | vauthors=De Silvestris M, D'Arrigo A, Borgese N |title=The targeting information of the mitochondrial outer membrane isoform of cytochrome b5 is contained within the carboxyl-terminal region. |journal=FEBS Lett. |volume=370 |issue= 1-2 |pages= 69–74 |year= 1995 |pmid= 7649306 |doi=10.1016/0014-5793(95)00797-D }}
- {{cite journal | vauthors=Li XR, Giordano SJ, Yoo M, Steggles AW |title=The isolation and characterization of the human cytochrome b5 gene. |journal=Biochem. Biophys. Res. Commun. |volume=209 |issue= 3 |pages= 894–900 |year= 1995 |pmid= 7733981 |doi= 10.1006/bbrc.1995.1582 }}
- {{cite journal | vauthors=Giordano SJ, Yoo M, Ward DC |title=The human cytochrome b5 gene and two of its pseudogenes are located on chromosomes 18q23, 14q31-32.1 and 20p11.2, respectively. |journal=Hum. Genet. |volume=92 |issue= 6 |pages= 615–8 |year= 1994 |pmid= 8262522 |doi=10.1007/BF00420948 |display-authors=etal}}
- {{cite journal | vauthors=Guengerich FP, Johnson WW |title=Kinetics of ferric cytochrome P450 reduction by NADPH-cytochrome P450 reductase: rapid reduction in the absence of substrate and variations among cytochrome P450 systems. |journal=Biochemistry |volume=36 |issue= 48 |pages= 14741–50 |year= 1998 |pmid= 9398194 |doi= 10.1021/bi9719399 }}
- {{cite journal | vauthors=Lee-Robichaud P, Akhtar ME, Akhtar M |title=Control of androgen biosynthesis in the human through the interaction of Arg347 and Arg358 of CYP17 with cytochrome b5. | series=332 |journal=Biochem. J. |volume=( Pt 2) |issue= |pages= 293–6 |year= 1998 |pmid= 9601054 |doi= | pmc=1219480 }}
{{refend}}{{PDB Gallery|geneid=1528}}{{membrane-protein-stub}} 1 : Transmembrane proteins |