Sulfit oxidasa

Recerca
PMC	articles
PubMed	articles
NCBI	proteins

Sulfit oxidasa
Identificadors
Número EC	1.8.3.1
Bases de dades
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
Estructures PDB	RCSB PDB; PDBj; PDBe; PDBsum
PMC
Recerca
PMC	articles
PubMed	articles
NCBI	proteins

sulfit oxidasa
Estructures disponibles
PDB	Cerca ortòloga: PDBe RCSB
Llista de codis id de PDB
	1MJ4
Identificadors
Àlies	SUOX (HUGO), entrez:6821, sulfite oxidase
Identif. externs	OMIM: 606887 MGI: 2446117 HomoloGene: 394 GeneCards: SUOX OMA: SUOX - orthologs
Número EC	1.8.3.1
Malalties relacionades genèticament
	isolated sulfite oxidase deficiency
Localització del gen (humà)
	Cromosoma: 12 (humà)
Fi	56.006.641 bp
Localització del gen (ratolí)
	Cromosoma: 10 (ratolí)
Fi	128.509.942 bp
Patró d'expressió d'ARN
	Més explicacions
	right lobe of liver ; ; right adrenal gland ; ; right adrenal cortex ; ; human kidney ; ; left adrenal gland ; ; left adrenal cortex ; ; mucosa of transverse colon ; ; muscle of thigh ; ; apex of heart ; ; medul·la renal;
	Més explicacions
	vesícula seminal; ; gastrula ; ; pyloric antrum ; ; mucous cell of stomach ; ; left lobe of liver ; ; epithelium of stomach ; ; right kidney ; ; decidu; ; human kidney ; ; tríceps braquial;
	Més referències a dades d'expressió
Ontologia genètica
Funció molecular	molybdopterin cofactor binding ; molybdenum ion binding ; oxidoreductase activity ; sulfite oxidase activity ; heme binding ; metal ion binding ; unió proteica ;
Component cel·lular	matriu mitocondrial ; mitochondrial intermembrane space ; mitocondri ;
Procés biològic	sulfur compound metabolic process ; sulfide oxidation, using sulfide:quinone oxidoreductase ; nitrate assimilation ;
	Fonts: Amigo / QuickGO
Ortòlegs
	6821
	211389
	ENSG00000139531
	ENSMUSG00000049858
	P51687
	Q8R086
	NM_000456; NM_001032386; NM_001032387
	NM_173733
	NP_000447; NP_001027558; NP_001027559
	NP_776094
	Wikidata
Veure/Editar gen humà	Veure/Editar gen del ratolí

La sulfit oxidasa catalitza la reacció de sulfit i aigua donant sulfat

La sulfit oxidasa (EC 1.8.3.1) és un enzim dins el mitocondri de tots els eucariotes. Oxida el sulfit a sulfat i, via citocrom c, transfereix elselectrons produïts en la cadena de transport d'electrons, permetent la generació d'ATP en fosforilació oxidativa.^[6]^[7]^[8] Aquest és el darrer pas en el metabolisme dels compostoa que contenen sofre i el sulfat s'excreta.

La sulfit oxidasa és un metal·loenzim que utilitza un cofactor molibdopterina i un grup heme. pertany a la superfamília de lesmolibdè oxotransferases la qual també incloi DMSO reductasa, xantina oxidasa i nitrit reductasa.

En els mamífers, l'expressió de nivells de sulfit oxidasa és alta en el fetge, el ronyó i el cor i molt baixa en la melsa, el cervell, el múscul esquelètic i la sang.

Referències

↑ «Malalties que s'associen genèticament amb sulfit oxidasa, vegeu/editeu les referències a wikidata».
1 2 3 GRCh38: Ensembl release 89: ENSG00000139531 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000049858 – 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.
↑ D'Errico G, Di Salle A, La Cara F, Rossi M, Cannio R «Identification and characterization of a novel bacterial sulfite oxidase with no heme binding domain from Deinococcus radiodurans». J. Bacteriol., 188, 2, 1-2006, p. 694–701. DOI: 10.1128/JB.188.2.694-701.2006. PMC: 1347283. PMID: 16385059.
↑ Tan WH, Eichler FS, Hoda S, Lee MS, Baris H, Hanley CA, Grant PE, Krishnamoorthy KS, Shih VE «Isolated sulfite oxidase deficiency: a case report with a novel mutation and review of the literature». Pediatrics, 116, 3, 9-2005, p. 757–66. DOI: 10.1542/peds.2004-1897. PMID: 16140720.
↑ Cohen HJ, Betcher-Lange S, Kessler DL, Rajagopalan KV «Hepatic sulfite oxidase. Congruency in mitochondria of prosthetic groups and activity». J. Biol. Chem., 247, 23, 12-1972, p. 7759–66. PMID: 4344230.

Bibliografia

Kisker, C. “Sulfite oxidase”, Messerschimdt, A.; Huber, R.; Poulos, T.; Wieghardt, K.; eds. Handbook of Metalloproteins, vol 2; John Wiley and Sons, Ltd: New York, 2002
Feng C, Wilson HL, Hurley JK, et al. «Essential role of conserved arginine 160 in intramolecular electron transfer in human sulfite oxidase.». Biochemistry, 42, 42, 2003, p. 12235–42. DOI: 10.1021/bi0350194. PMID: 14567685.
Lee HF, Mak BS, Chi CS, et al. «A novel mutation in neonatal isolated sulphite oxidase deficiency.». Neuropediatrics, 33, 4, 2002, p. 174–9. DOI: 10.1055/s-2002-34491. PMID: 12368985.
Steinberg KK, Relling MV, Gallagher ML, et al. «Genetic studies of a cluster of acute lymphoblastic leukemia cases in Churchill County, Nevada.». Environ. Health Perspect., 115, 1, 2007, p. 158–64. DOI: 10.1289/ehp.9025. PMC: 1817665. PMID: 17366837.
Kimura K, Wakamatsu A, Suzuki Y, et al. «Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes.». Genome Res., 16, 1, 2006, p. 55–65. DOI: 10.1101/gr.4039406. PMC: 1356129. PMID: 16344560.
Wilson HL, Wilkinson SR, Rajagopalan KV «The G473D mutation impairs dimerization and catalysis in human sulfite oxidase.». Biochemistry, 45, 7, 2006, p. 2149–60. DOI: 10.1021/bi051609l. PMID: 16475804.
Hoffmann C, Ben-Zeev B, Anikster Y, et al. «Magnetic resonance imaging and magnetic resonance spectroscopy in isolated sulfite oxidase deficiency.». J. Child Neurol., 22, 10, 2007, p. 1214–21. DOI: 10.1177/0883073807306260. PMID: 17940249.
Johnson JL, Coyne KE, Garrett RM, et al. «Isolated sulfite oxidase deficiency: identification of 12 novel SUOX mutations in 10 patients.». Hum. Mutat., 20, 1, 2002, p. 74. DOI: 10.1002/humu.9038. PMID: 12112661.
Woo WH, Yang H, Wong KP, Halliwell B «Sulphite oxidase gene expression in human brain and in other human and rat tissues.». Biochem. Biophys. Res. Commun., 305, 3, 2003, p. 619–23. DOI: 10.1016/S0006-291X(03)00833-7. PMID: 12763039.
Feng C, Wilson HL, Tollin G, et al. «The pathogenic human sulfite oxidase mutants G473D and A208D are defective in intramolecular electron transfer.». Biochemistry, 44, 42, 2005, p. 13734–43. DOI: 10.1021/bi050907f. PMID: 16229463.
Tan WH, Eichler FS, Hoda S, et al. «Isolated sulfite oxidase deficiency: a case report with a novel mutation and review of the literature.». Pediatrics, 116, 3, 2005, p. 757–66. DOI: 10.1542/peds.2004-1897. PMID: 16140720.
Astashkin AV, Johnson-Winters K, Klein EL, et al. «Structural studies of the molybdenum center of the pathogenic R160Q mutant of human sulfite oxidase by pulsed EPR spectroscopy and 17O and 33S labeling.». J. Am. Chem. Soc., 130, 26, 2008, p. 8471–80. DOI: 10.1021/ja801406f. PMC: 2779766. PMID: 18529001.
Dronov R, Kurth DG, Möhwald H, et al. «Layer-by-layer arrangement by protein-protein interaction of sulfite oxidase and cytochrome c catalyzing oxidation of sulfite.». J. Am. Chem. Soc., 130, 4, 2008, p. 1122–3. DOI: 10.1021/ja0768690. PMID: 18177044.
Edwards MC, Johnson JL, Marriage B, et al. «Isolated sulfite oxidase deficiency: review of two cases in one family.». Ophthalmology, 106, 10, 1999, p. 1957–61. DOI: 10.1016/S0161-6420(99)90408-6. PMID: 10519592.
Gerhard DS, Wagner L, Feingold EA, et al. «The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).». Genome Res., 14, 10B, 2004, p. 2121–7. DOI: 10.1101/gr.2596504. PMC: 528928. PMID: 15489334.
Rudolph MJ, Johnson JL, Rajagopalan KV, Kisker C «The 1.2 A structure of the human sulfite oxidase cytochrome b(5) domain.». Acta Crystallogr. D Biol. Crystallogr., 59, Pt 7, 2003, p. 1183–91. DOI: 10.1107/S0907444903009934. PMID: 12832761.
Feng C, Wilson HL, Hurley JK, et al. «Role of conserved tyrosine 343 in intramolecular electron transfer in human sulfite oxidase.». J. Biol. Chem., 278, 5, 2003, p. 2913–20. DOI: 10.1074/jbc.M210374200. PMID: 12424234.
Neumann M, Leimkühler S «Heavy metal ions inhibit molybdoenzyme activity by binding to the dithiolene moiety of molybdopterin in Escherichia coli.». FEBS J., 275, 22, 2008, p. 5678–89. DOI: 10.1111/j.1742-4658.2008.06694.x. PMID: 18959753.
Strausberg RL, Feingold EA, Grouse LH, et al. «Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.». Proc. Natl. Acad. Sci. U.S.A., 99, 26, 2002, p. 16899–903. DOI: 10.1073/pnas.242603899. PMC: 139241. PMID: 12477932.
Wilson HL, Rajagopalan KV «The role of tyrosine 343 in substrate binding and catalysis by human sulfite oxidase.». J. Biol. Chem., 279, 15, 2004, p. 15105–13. DOI: 10.1074/jbc.M314288200. PMID: 14729666.
Hakonarson H, Qu HQ, Bradfield JP, et al. «A novel susceptibility locus for type 1 diabetes on Chr12q13 identified by a genome-wide association study.». Diabetes, 57, 4, 2008, p. 1143–6. DOI: 10.2337/db07-1305. PMID: 18198356.

Enllaços externs

«Sulfit oxidasa» (en anglès). Medical Subject Headings.
Research Activity of Sarkar Group Arxivat 2009-02-22 a Wayback Machine.

[1] «Malalties que s'associen genèticament amb sulfit oxidasa, vegeu/editeu les referències a wikidata».

[refGRCh38Ensembl-2] 1 2 3 GRCh38: Ensembl release 89: ENSG00000139531 - Ensembl, May 2017

[refGRCm38Ensembl-3] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000049858 – Ensembl, May 2017

[4] «Human PubMed Reference:». National Center for Biotechnology Information, U.S. National Library of Medicine.

[5] «Mouse PubMed Reference:». National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid16385059-6] D'Errico G, Di Salle A, La Cara F, Rossi M, Cannio R «Identification and characterization of a novel bacterial sulfite oxidase with no heme binding domain from Deinococcus radiodurans». J. Bacteriol., 188, 2, 1-2006, p. 694–701. DOI: 10.1128/JB.188.2.694-701.2006. PMC: 1347283. PMID: 16385059.

[pmid16140720-7] Tan WH, Eichler FS, Hoda S, Lee MS, Baris H, Hanley CA, Grant PE, Krishnamoorthy KS, Shih VE «Isolated sulfite oxidase deficiency: a case report with a novel mutation and review of the literature». Pediatrics, 116, 3, 9-2005, p. 757–66. DOI: 10.1542/peds.2004-1897. PMID: 16140720.

[pmid4344230-8] Cohen HJ, Betcher-Lange S, Kessler DL, Rajagopalan KV «Hepatic sulfite oxidase. Congruency in mitochondria of prosthetic groups and activity». J. Biol. Chem., 247, 23, 12-1972, p. 7759–66. PMID: 4344230.

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