Sulfite oxidase

sulfite oxidase
Sulfite oxidase catalyses the oxidation-reduction reaction of sulfite and water, yielding sulfate.
Identifiers
EC no.1.8.3.1
CAS no.9029-38-3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
SUOX
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesSUOX, entrez:6821, sulfite oxidase
External IDsOMIM: 606887; MGI: 2446117; HomoloGene: 394; GeneCards: SUOX; OMA:SUOX - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_000456
NM_001032386
NM_001032387

NM_173733

RefSeq (protein)

NP_000447
NP_001027558
NP_001027559

NP_776094

Location (UCSC)Chr 12: 56 – 56.01 MbChr 10: 128.51 – 128.51 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Sulfite oxidase (EC 1.8.3.1) is an enzyme in the mitochondria of all eukaryotes, with exception of the yeasts.[citation needed] It oxidizes sulfite to sulfate and, via cytochrome c, transfers the electrons produced to the electron transport chain, allowing generation of ATP in oxidative phosphorylation.[5][6][7] This is the last step in the metabolism of sulfur-containing compounds and the sulfate is excreted.

Sulfite oxidase is a metallo-enzyme that utilizes a molybdopterin cofactor and a heme group (in the case of animals). It is one of the cytochromes b5 and belongs to the enzyme super-family of molybdenum oxotransferases that also includes DMSO reductase, xanthine oxidase, and nitrite reductase.

In mammals, the expression levels of sulfite oxidase is high in the liver, kidney, and heart, and very low in spleen, brain, skeletal muscle, and blood.

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000139531Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000049858Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ D'Errico G, Di Salle A, La Cara F, Rossi M, Cannio R (January 2006). "Identification and characterization of a novel bacterial sulfite oxidase with no heme binding domain from Deinococcus radiodurans". J. Bacteriol. 188 (2): 694–701. doi:10.1128/JB.188.2.694-701.2006. PMC 1347283. PMID 16385059.
  6. ^ Tan WH, Eichler FS, Hoda S, Lee MS, Baris H, Hanley CA, Grant PE, Krishnamoorthy KS, Shih VE (September 2005). "Isolated sulfite oxidase deficiency: a case report with a novel mutation and review of the literature". Pediatrics. 116 (3): 757–66. doi:10.1542/peds.2004-1897. PMID 16140720. S2CID 6506338.
  7. ^ Cohen HJ, Betcher-Lange S, Kessler DL, Rajagopalan KV (December 1972). "Hepatic sulfite oxidase. Congruency in mitochondria of prosthetic groups and activity". J. Biol. Chem. 247 (23): 7759–66. doi:10.1016/S0021-9258(19)44588-2. PMID 4344230.