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Human Metabolome Database Version 2.5

 

Showing metabocard for Sulfite (HMDB00240)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-07-27 12:14:09
Accession Number HMDB00240
Secondary Accession Numbers Not Available
Common Name Sulfite
Description Endogenous sulfite is generated as a consequence of the body's normal processing of sulfur-containing amino acids. Sulfites occur as a consequence of fermentation and also occur naturally in a number of foods and beverages. As food additives, sulfiting agents were first used in 1664 and approved in the United States as long ago as the 1800s. Sulfite sensitivity occurs most often in asthmatic adults--predominantly women; it is uncommonly reported in preschool children. Adverse reactions to sulfites in nonasthmatics are extremely rare. Asthmatics who are steroid-dependent or who have a higher degree of airway hyperreactivity may be at greater risk of experiencing a reaction to sulfite-containing foods. Sulfite sensitivity reactions vary widely, ranging from no reaction to severe. The majority of reactions are mild. These manifestations may include dermatologic, respiratory, or gastrointestinal signs and symptoms. The precise mechanisms of the sensitivity responses have not been completely elucidated. Inhalation of sulfur dioxide (SO2) generated in the stomach following ingestion of sulfite-containing foods or beverages, a deficiency in a mitochondrial enzyme, and an IgE-mediated immune response have all been implicated. Exogenously supplied sulfite is detoxified by the enzyme sulfite oxidase. Sulfite oxidase (EC 1.8.3.1) is 1 of 3 enzymes in humans that requires molybdenum as a cofactor. Sulfite oxidase deficiency is a rare autosomal inherited disease with severe neurological symptoms such as untreatable seizures, attenuated growth of the brain and mental retardation. It results from defects in the enzyme sulfite oxidase, which is responsible for the oxidation of sulfite to sulfate. This reaction is the final step in the degradation of sulfur containing metabolites including the amino acids cysteine and methionine. is a neurometabolic disease that results in severe developmental delay and premature death. The term isolated sulfite oxidase deficiency is used to define the deficiency caused by mutations in the sulfite oxidase gene. This differentiates it from another version of sulfite oxidase deficiency that is due to defects in the Moco biosynthetic pathway. Isolated sulfite oxidase deficiency is a rare but devastating neurologic disease that usually presents in early infancy with seizures and alterations in muscle tone. (PMID: 16234925, 16140720, 8586770)
Synonyms
  1. Sulfite ion
  2. Sulphite
  3. Sulfite ions
  4. Bisulfite
  5. Sulfonate
  6. trioxosulfate(2-)
  7. Sulfite dianion
  8. Sulfuric anhydride
  9. trioxosulfate(IV)
  10. Sulfur trioxide
Chemical IUPAC Name sulfite
Chemical Formula [SO3]2-
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Inorganic
Super Class
  • Inorganic compounds
Class
  • Inorganic Ions and Gases
Sub Class
  • Anions
Family
  • Mammalian Metabolite
Species
  • anion
Biofunction
  • Component of Sulfur metabolism
Application
—
Source
  • Endogenous
Average Molecular Weight 80.063
Monoisotopic Molecular Weight 79.956818
Isomeric SMILES [O-]S([O-])=O
Canonical SMILES [O-]S([O-])=O
KEGG Compound ID C00094 Link Image
BioCyc ID SO3 Link Image
BiGG ID 33833 Link Image
Wikipedia Link Sulfite Link Image
NuGOwiki Link HMDB00240 Link Image
Metagene Link HMDB00240 Link Image
METLIN ID 3223 Link Image
PubChem Compound 1099 Link Image
PubChem Substance 15218641 Link Image
ChEBI ID 17359 Link Image
CAS Registry Number 14265-45-3
InChI Identifier InChI=1/H2O3S/c1-4(2)3/h(H2,1,2,3)/p-2
Synthesis Reference Dorain, P. B.; Von Raben, K. U.; Chang, R. K.; Laube, B. L. Catalytic formation of sulfite and sulfate ions from sulfur dioxide on silver observed by surface-enhanced Raman scattering. Chemical Physics Letters (1981), 84(2), 405-9.
Melting Point (Experimental) Not Available
Experimental Water Solubility 558.5 mg/mL [sodium salt, HMP experimental] Source: PhysProp
Predicted Water Solubility Not Available Calculated using ALOGPS
Physiological Charge -2
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -2.7 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Not Available
Not Available
Predicted 13C NMR Spectrum Not Available
Not Available
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm (Predicted from LogP)
  • mitochondria
Biofluid Location Not Available
Tissue Location
Tissue References
Brain —
Neutrophil —
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Sulfate/Sulfite Metabolism SMP00041 Link Image map00920 Link Image
General References
  1. Graf WD, Oleinik OE, Jack RM, Weiss AH, Johnson JL: Ahomocysteinemia in molybdenum cofactor deficiency. Neurology. 1998 Sep;51(3):860-2. [PubMed Link Image]
  2. Jeppesen C: Media for Aeromonas spp., Plesiomonas shigelloides and Pseudomonas spp. from food and environment. Int J Food Microbiol. 1995 Jun;26(1):25-41. [PubMed Link Image]
  3. Mitsuhashi H, Nojima Y, Tanaka T, Ueki K, Maezawa A, Yano S, Naruse T: Sulfite is released by human neutrophils in response to stimulation with lipopolysaccharide. J Leukoc Biol. 1998 Nov;64(5):595-9. [PubMed Link Image]
  4. von Graevenitz A, Bucher C: Evaluation of differential and selective media for isolation of Aeromonas and Plesiomonas spp. from human feces. J Clin Microbiol. 1983 Jan;17(1):16-21. [PubMed Link Image]
  5. Tsariuk LA, Rybachuk VN, Shevchenko LI, Tolstykh VM: [Determination of fibrinogen concentration in blood plasma by the sulfite precipitation method] Vopr Med Khim. 1979 Jan-Feb;25(1):97-101. [PubMed Link Image]
  6. Shea M, Howell S: High-performance liquid chromatographic measurement of exogenous thiosulfate in urine and plasma. Anal Biochem. 1984 Aug 1;140(2):589-94. [PubMed Link Image]
  7. Bor-Kucukatay M, Kucukatay V, Agar A, Baskurt OK: Effect of sulfite on red blood cell deformability ex vivo and in normal and sulfite oxidase-deficient rats in vivo. Arch Toxicol. 2005 Sep;79(9):542-6. Epub 2005 Apr 13. [PubMed Link Image]
  8. Gubash SM, Ingham L: Comparison of a new, bismuth-iron-sulfite-cycloserine agar for isolation of Clostridium perfringens with the tryptose-sulfite-cycloserine and blood agars. Zentralbl Bakteriol. 1997 Feb;285(3):397-402. [PubMed Link Image]
  9. Kim E, Driscoll CF, Minah GE: The effect of a denture adhesive on the colonization of Candida species in vivo. J Prosthodont. 2003 Sep;12(3):187-91. [PubMed Link Image]
  10. Willis CL, Cummings JH, Neale G, Gibson GR: Nutritional aspects of dissimilatory sulfate reduction in the human large intestine. Curr Microbiol. 1997 Nov;35(5):294-8. [PubMed Link Image]
  11. Sardesai VM: Molybdenum: an essential trace element. Nutr Clin Pract. 1993 Dec;8(6):277-81. [PubMed Link Image]
  12. Togawa T, Ogawa M, Nawata M, Ogasawara Y, Kawanabe K, Tanabe S: High performance liquid chromatographic determination of bound sulfide and sulfite and thiosulfate at their low levels in human serum by pre-column fluorescence derivatization with monobromobimane. Chem Pharm Bull (Tokyo). 1992 Nov;40(11):3000-4. [PubMed Link Image]
  13. Pearson SJ, Czudek C, Mercer K, Reynolds GP: Electrochemical detection of human brain transmitter amino acids by high-performance liquid chromatography of stable o-phthalaldehyde-sulphite derivatives. J Neural Transm Gen Sect. 1991;86(2):151-7. [PubMed Link Image]
  14. Mishra A, Dayal N, Beck-Speier I: Effect of sulphite on the oxidative metabolism of human neutrophils: studies with lucigenin- and luminol-dependent chemiluminescence. J Biolumin Chemilumin. 1995 Jan-Feb;10(1):9-19. [PubMed Link Image]
  15. Beck-Speier I, Lenz AG, Godleski JJ: Responses of human neutrophils to sulfite. J Toxicol Environ Health. 1994 Mar;41(3):285-97. [PubMed Link Image]
  16. Beck-Speier I, Liese JG, Belohradsky BH, Godleski JJ: Sulfite stimulates NADPH oxidase of human neutrophils to produce active oxygen radicals via protein kinase C and Ca2+/calmodulin pathways. Free Radic Biol Med. 1993 Jun;14(6):661-8. [PubMed Link Image]
  17. Zhang X, Vincent AS, Halliwell B, Wong KP: A mechanism of sulfite neurotoxicity: direct inhibition of glutamate dehydrogenase. J Biol Chem. 2004 Oct 8;279(41):43035-45. Epub 2004 Jul 23. [PubMed Link Image]
  18. Wikipedia Link Image
Metabolic Enzymes
  1. 3-mercaptopyruvate sulfurtransferase
  2. Thiosulfate sulfurtransferase
  3. Sulfite oxidase, mitochondrial precursor
  4. Putative thiosulfate sulfurtransferase KAT
  5. cDNA FLJ34555 fis, clone KIDNE2000833, highly similar to THIOSULFATE SULFURTRANSFERASE (EC 2.8.1.1)
Enzyme 1 [top]
Enzyme 1 ID 6061
Enzyme 1 Name 3-mercaptopyruvate sulfurtransferase
Enzyme 1 Synonyms
  1. MST
Enzyme 1 Gene Name MPST
Enzyme 1 Protein Sequence >3-mercaptopyruvate sulfurtransferase 
MASPQLCRALVSAQWVAEALRAPRAGQPLQLLDASWYLPKLGRDARREFEERHIPGAAFF
DIDQCSDRTSPYDHMLPGAEHFAEYAGRLGVGAATHVVIYDASDQGLYSAPRVWWMFRAF
GHHAVSLLDGGLRHWLRQNLPLSSGKSQPAPAEFRAQLDPAFIKTYEDIKENLESRRFQV
VDSRATGRFRGTEPEPRDGIEPGHIPGTVNIPFTDFLSQEGLEKSPEEIRHLFQEKKVDL
SKPLVATCGSGVTACHVALGAYLCGKPDVPIYDGSWVEWYMRARPEDVISEGRGKTH
Enzyme 1 Number of Residues 297
Enzyme 1 Molecular Weight 33179
Enzyme 1 Theoretical pI 6.58
Enzyme 1 GO Classification
Function
  • catalytic activity
  • sulfurtransferase activity
  • thiosulfate sulfurtransferase activity
  • transferase activity
  • transferase activity, transferring sulfur-containing groups
Process
  • anion transport
  • cellular physiological process
  • inorganic anion transport
  • ion transport
  • physiological process
  • sulfate transport
  • transport
Component
—
Enzyme 1 General Function Inorganic ion transport and metabolism
Enzyme 1 Specific Function Transfer of a sulfur ion to cyanide or to other thiol compounds. Also has weak rhodanese activity. May have a role in cyanide degradation or in thiosulfate biosynthesis
Enzyme 1 Pathways
Enzyme 1 Reactions
  • 3-mercaptopyruvate + cyanide = pyruvate + thiocyanate
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 432376 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P25325 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name THTM_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >891 bp 
ATGGCTTCGCCGCAGCTCTGCCGCGCGCTGGTGTCGGCGCAATGGGTGGCGGAGGCGCTG
CGGGCCCCGCGCGCTGGGCAGCCTCTGCAGCTGCTGGACGCCTCCTGGTACCTGCCGAAG
CTGGGGCGCGACGCGACGCAGTTCGAGGAGCGCCACATCCCGGGCGCCGCTTTCTTCGAC
ATCGACCAGTGCAGCGACCGCACCTCGCCCTACGACCACATGCTGCCCGGGGCCGAGCAT
TTCGCGGAGTACGCAGGCCGCCTGGGCGTGGGCGCGGCCACCCACGTCGTGATCTACGAC
GCCAGCGACCAGGGCCTCTACTCCGCCCCGCGCGTCTGGTGGATGTTCCGCGCCTTCGGC
CACCACGCCGTGTCACTGCTTGATGGCGGCCTCCGCCACTGGCTGCGCCAGAACCTCCCG
CTCAGCTCCGGCAAGAGCCAACCTGCTCCCGCCGAGTTCCGCGCTCAGCTCGACCCCGCC
TTCATCAAGACCTACGAGGACATCAAGGAGAACCTGGAATCCCGGCGCTTCCAGGTGGTG
GACTCCCGAGCCACTGGCAGGTTCCGCGGCACCGAGCCCGAGCCCCGAGACGGCATTGAA
CCTGGCCACATCCCAGGTACCGTGAACATCCCCTTCACAGACTTCCTGAGCCAGGAGGGG
CTGGAGAAGAGCCCTGAGGAGATCCGCCATCTGTTCCAGGAGAAGAAAGTGGACCTGTCT
AAGCCACTGGTGGCCACGTGTGGCTCTGGCGTCACAGCCTGCCACGTGGCACTAGGGGCC
TACCTCTGCGGCAAGCCAGACGTGCCCATCTACGATGGCTCCTGGGTGGAGTGGTACATG
CGCGCCCGGCCCGAGGATGTCATCTCAGAGGGCCGGGGGAAGACCCACTGA
Enzyme 1 GenBank Gene ID X59434 Link Image
Enzyme 1 GeneCard ID MPST Link Image
Enzyme 1 GenAtlas ID MPST Link Image
Enzyme 1 HGNC ID HGNC:7223 Link Image
Enzyme 1 Chromosome Location 22
Enzyme 1 Locus 22q13.1
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Pallini R, Guazzi GC, Cannella C, Cacace MG: Cloning and sequence analysis of the human liver rhodanese: comparison with the bovine and chicken enzymes. Biochem Biophys Res Commun. 1991 Oct 31;180(2):887-93. [PubMed Link Image]
  2. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 6345
Enzyme 2 Name Thiosulfate sulfurtransferase
Enzyme 2 Synonyms
  1. Rhodanese
Enzyme 2 Gene Name TST
Enzyme 2 Protein Sequence >Thiosulfate sulfurtransferase 
MVHQVLYRALVSTKWLAESIRTGKLGPGLRVLDASWYSPGTREARKEYLERHVPGASFFD
IEECRDTASPYEMMLPSEAGFAEYVGRLGISNHTHVVVYDGEHLGSFYAPRVWWMFRVFG
HRTVSVLNGGFRNWLKEGHPVTSEPSRPEPAVFKATLDRSLLKTYEQVLENLESKRFQLV
DSRSQGRFLGTEPEPDAVGLDSGHIRGAVNMPFMDFLTEDGFEKGPEELRALFQTKKVDL
SQPLIATCRKGVTACHVALAAYLCGKPDVAVYDGSWSEWFRRAPPESRVSQGKSEKA
Enzyme 2 Number of Residues 297
Enzyme 2 Molecular Weight 33429
Enzyme 2 Theoretical pI 7.28
Enzyme 2 GO Classification
Function
  • catalytic activity
  • sulfurtransferase activity
  • thiosulfate sulfurtransferase activity
  • transferase activity
  • transferase activity, transferring sulfur-containing groups
Process
  • anion transport
  • cellular physiological process
  • inorganic anion transport
  • ion transport
  • physiological process
  • sulfate transport
  • transport
Component
—
Enzyme 2 General Function Inorganic ion transport and metabolism
Enzyme 2 Specific Function Formation of iron-sulfur complexes, cyanide detoxification or modification of sulfur-containing enzymes. Other thiol compounds, besides cyanide, can act as sulfur ion acceptors. Also has weak mercaptopyruvate sulfurtransferase (MST) activity
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions
  • thiosulfate + cyanide = sulfite + thiocyanate
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 1877031 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q16762 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name THTR_HUMAN Link Image
Enzyme 2 PDB ID 1ORB Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >894 bp 
ATGGTTCATCAGGTGCTCTACCGGGCGCTGGTCTCCACCAAGTGGCTGGCGGAGTCCATC
AGGACTGGCAAGCTGGGGCCCGGCCTGCGGGTGCTGGACGCGTCCTGGTACTCACCAGGC
ACCCGAGAGGCCCGCAAGGAGTACCTCGAGCGCCACGTACCCGGCGCCTCTTTCTTTGAC
ATAGAAGAGTGCCGGGACACGGCGTCGCCCTACGAGATGATGCTGCCCAGCGAGGCTGGC
TTCGCCGAGTATGTGGGCCGCCTGGGCATCAGCAACCACACGCACGTGGTGGTGTATGAT
GGTGAACACCTGGGCAGCTTCTATGCTCCCCGGGTCTGGTGGATGTTCCGTGTGTTTGGC
CACCGCACCGTATCAGTGCTCAATGGTGGCTTCCGGAACTGGCTGAAGGAGGGCCACCCG
GTGACATCCGAGCCCTCACGCCCAGAACCGGCCGTCTTCAAAGCCACACTGGACCGCTCC
CTGCTCAAGACCTACGAGCAGGTGCTGGAGAACCTTGAATCTAAGAGGTTCCAGCTGGTG
GATTCAAGGTCTCAAGGGCGGTTCCTGGGCACCGAGCCGGAGCCGGATGCAGTAGGACTG
GACTCGGGCCATATCCGTGGTGCCGTCAACATGCCTTTCATGGACTTCCTGACTGAGGAT
GGCTTCGAGAAGGGCCCAGAAGAGCTCCGTGCTCTGTTCCAGACCAAGAAGGTGGATCTC
TCGCAGCCTCTCATTGCCACGTGCCGCAAGGGAGTCACCGCCTGCCACGTGGCCTTGGCT
GCCTACCTCTGCGGCAAGCCTGATGTGGCCGTGTACGATGGCTCCTGGTCCGAGTGGTTT
CGCCGGGCCCCCCCAGAGAGCCGTGTGTCCCAGGGAAAGTCTGAGAAGGCCTGA
Enzyme 2 GenBank Gene ID D87292 Link Image
Enzyme 2 GeneCard ID TST Link Image
Enzyme 2 GenAtlas ID TST Link Image
Enzyme 2 HGNC ID HGNC:12388 Link Image
Enzyme 2 Chromosome Location 22
Enzyme 2 Locus 22q13.1
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Aita N, Ishii K, Akamatsu Y, Ogasawara Y, Tanabe S: Cloning and expression of human liver rhodanese cDNA. Biochem Biophys Res Commun. 1997 Feb 3;231(1):56-60. [PubMed Link Image]
  2. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
  3. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 6346
Enzyme 3 Name Sulfite oxidase, mitochondrial precursor
Enzyme 3 Synonyms Not Available
Enzyme 3 Gene Name SUOX
Enzyme 3 Protein Sequence >Sulfite oxidase, mitochondrial precursor 
MGTLLGLGAVLAYQDHRCRAAQESTHIYTKEEVSSHTSPETGIWVTLGSEVFDVTEFVDL
HPGGPSKLMLAAGGPLEPFWALYAVHNQSHVRELLAQYKIGELNPEDKVAPTVETSDPYA
DDPVRHPALKVNSQRPFNAEPPPELLTENYITPNPIFFTRNHLPVPNLDPDTYRLHVVGA
PGGQSLSLSLDDLHNFPRYEITVTLQCAGNRRSEMTQVKEVKGLEWRTGAISTARWAGAR
LCDVLAQAGHQLCETEAHVCFEGLDSDPTGTAYGASIPLARAMDPEAEVLLAYEMNGQPL
PRDHGFPVRVVVPGVVGARHVKWLGRVSVQPEESYSHWQRRDYKGFSPSVDWETVDFDSA
PSIQELPVQSAITEPRDGETVESGEVTIKGYAWSGGGRAVIRVDVSLDGGLTWQVAKLDG
EEQRPRKAWAWRLWQLKAPVPAGQKELNIVCKAVDDGYNVQPDTVAPIWNLRGVLSNAWH
RVHVYVSP
Enzyme 3 Number of Residues 488
Enzyme 3 Molecular Weight 53885
Enzyme 3 Theoretical pI 5.31
Enzyme 3 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
—
Enzyme 3 General Function Not Available
Enzyme 3 Specific Function Sulfite + O(2) + H(2)O = sulfate + H(2)O(2)
Enzyme 3 Pathways
Enzyme 3 Reactions
  • sulfite + O2 + H2O = sulfate + H2O2
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 508502 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P51687 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name SUOX_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1467 bp 
ATGGGGACCCTATTAGGTCTCGGTGCAGTGTTGGCCTATCAGGACCATCGGTGTAGGGCT
GCTCAGGAGTCAACACACATATACACTAAGGAGGAAGTGAGTTCCCACACCAGCCCTGAG
ACTGGGATCTGGGTGACTCTGGGCTCTGAGGTCTTTGATGTCACAGAATTTGTGGACCTA
CATCCAGGGGGGCCTTCAAAGCTGATGCTAGCAGCTGGGGGTCCCCTAGAGCCCTTCTGG
GCCCTCTATGCTGTTCACAACCAGTCCCATGTGCGTGAGTTACTGGCTCAGTACAAGATT
GGGGAGCTGAATCCTGAAGACAAGGTAGCCCCCACCGTGGAGACCTCTGACCCTTATGCT
GATGATCCTGTACGTCACCCAGCCCTGAAGGTCAACAGCCAGCGGCCCTTTAATGCAGAG
CCTCCCCCTGAGCTGCTGACAGAAAACTACATCACACCCAACCCTATCTTCTTCACCCGG
AACCATCTGCCTGTACCTAACCTGGATCCAGACACCTATCGCTTACACGTAGTAGGAGCA
CCTGGGGGTCAGTCACTGTCTCTTTCCCTGGATGACTTGCACAACTTTCCCAGGTACGAG
ATCACAGTCACTCTGCAGTGTGCCGGCAACCGACGCTCTGAGATGACTCAGGTCAAAGAA
GTAAAAGGTCTGGAGTGGAGAACAGGAGCCATCAGCACTGCACGCTGGGCTGGGGCACGG
CTCTGTGATGTGTTAGCCCAGGCTGGCCACCAACTCTGTGAAACTGAGGCCCACGTCTGC
TTTGAGGGACTGGACTCAGACCCTACTGGGACTGCCTATGGAGCATCCATCCCTCTGGCT
CGGGCCATGGACCCTGAAGCTGAGGTCCTGCTGGCATATGAGATGAATGGGCAGCCTCTG
CCACGTGACCACGGCTTCCCTGTGCGTGTGGTGGTTCCTGGAGTGGTGGGTGCCCGCCAT
GTCAAATGGCTGGGCAGAGTGAGTGTGCAGCCAGAGGAAAGTTACAGCCACTGGCAACGG
CGGGATTACAAAGGCTTCTCTCCATCTGTGGACTGGGAGACTGTAGATTTTGACTCTGCT
CCATCCATTCAGGAACTTCCTGTCCAGTCCGCCATCACAGAGCCCCGGGATGGAGAGACT
GTAGAATCAGGGGAGGTGACCATCAAGGGCTATGCATGGAGTGGTGGTGGCAGGGCTGTG
ATCCGGGTGGATGTGTCTCTGGATGGGGGCCTAACCTGGCAGGTGGCTAAGCTGGATGGA
GAGGAACAGCGCCCCAGGAAGGCCTGGGCATGGCGTCTGTGGCAGTTGAAAGCCCCTGTG
CCAGCTGGACAAAAGGAACTGAACATTGTTTGTAAGGCTGTGGATGATGGTTACAATGTG
CAGCCAGACACCGTGGCCCCAATCTGGAACCTGCGAGGTGTTCTCAGCAATGCCTGGCAT
CGTGTCCATGTCTATGTCTCCCCATGA
Enzyme 3 GenBank Gene ID L31573 Link Image
Enzyme 3 GeneCard ID SUOX Link Image
Enzyme 3 GenAtlas ID SUOX Link Image
Enzyme 3 HGNC ID HGNC:11460 Link Image
Enzyme 3 Chromosome Location 12
Enzyme 3 Locus 12q13.2
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Garrett RM, Bellissimo DB, Rajagopalan KV: Molecular cloning of human liver sulfite oxidase. Biochim Biophys Acta. 1995 Jun 9;1262(2-3):147-9. [PubMed Link Image]
  2. Kisker C, Schindelin H, Pacheco A, Wehbi WA, Garrett RM, Rajagopalan KV, Enemark JH, Rees DC: Molecular basis of sulfite oxidase deficiency from the structure of sulfite oxidase. Cell. 1997 Dec 26;91(7):973-83. [PubMed Link Image]
  3. Garrett RM, Johnson JL, Graf TN, Feigenbaum A, Rajagopalan KV: Human sulfite oxidase R160Q: identification of the mutation in a sulfite oxidase-deficient patient and expression and characterization of the mutant enzyme. Proc Natl Acad Sci U S A. 1998 May 26;95(11):6394-8. [PubMed Link Image]
  4. Edwards MC, Johnson JL, Marriage B, Graf TN, Coyne KE, Rajagopalan KV, MacDonald IM: Isolated sulfite oxidase deficiency: review of two cases in one family. Ophthalmology. 1999 Oct;106(10):1957-61. [PubMed Link Image]
  5. Johnson JL, Coyne KE, Garrett RM, Zabot MT, Dorche C, Kisker C, Rajagopalan KV: Isolated sulfite oxidase deficiency: identification of 12 novel SUOX mutations in 10 patients. Hum Mutat. 2002 Jul;20(1):74. [PubMed Link Image]
  6. Lee HF, Mak BS, Chi CS, Tsai CR, Chen CH, Shu SG: A novel mutation in neonatal isolated sulphite oxidase deficiency. Neuropediatrics. 2002 Aug;33(4):174-9. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 14924
Enzyme 4 Name Putative thiosulfate sulfurtransferase KAT
Enzyme 4 Synonyms Not Available
Enzyme 4 Gene Name KAT
Enzyme 4 Protein Sequence >Putative thiosulfate sulfurtransferase KAT 
MAGAPTVSLPELRSLLASGRARLFDVRSREEAAAGTIPGALNIPVSELESALQMEPAAFQ
ALYSAEKPKLEDEHLVFFCQMGKRGLQATQLARSLGYTGARNYAGAYREWLEKES
Enzyme 4 Number of Residues 115
Enzyme 4 Molecular Weight 12530
Enzyme 4 Theoretical pI 5.91
Enzyme 4 GO Classification Not Available
Enzyme 4 General Function Inorganic ion transport and metabolism
Enzyme 4 Specific Function Possible role in tumorgenesis
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein Not Available
Enzyme 4 UniProtKB/Swiss-Prot ID Q8NFU3 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name KAT_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence Not Available
Enzyme 4 GenBank Gene ID AF439442 Link Image
Enzyme 4 GeneCard ID Q8NFU3 Link Image
Enzyme 4 GenAtlas ID Not Available
Enzyme 4 HGNC ID Not Available
Enzyme 4 Chromosome Location Not Available
Enzyme 4 Locus Not Available
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Wenzel K, Felix SB, Flachmeier C, Heere P, Schulze W, Grunewald I, Pankow H, Hewelt A, Scherneck S, Bauer D, Hoehe MR: Identification and characterization of KAT, a novel gene preferentially expressed in several human cancer cell lines. Biol Chem. 2003 May;384(5):763-75. [PubMed Link Image]
  2. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 16532
Enzyme 5 Name cDNA FLJ34555 fis, clone KIDNE2000833, highly similar to THIOSULFATE SULFURTRANSFERASE (EC 2.8.1.1)
Enzyme 5 Synonyms
  1. SubName: Thiosulfate sulfurtransferase (Rhodanese)
Enzyme 5 Gene Name TST
Enzyme 5 Protein Sequence >cDNA FLJ34555 fis, clone KIDNE2000833, highly similar to THIOSULFATE SULFURTRANSFERASE (EC 2.8.1.1) 
MVHQVLYRALVSTKWLAESIRTGKLGPGLRVLDASWYSPGTREARKEYLERHVPGASFFD
IEECRDTASPYEMMLPSEAGFAEYVGRLGISNHTHVVVYDGEHLGSFYAPRVWWMFRVFG
HRTVSVLNGGFRNWLKEGHPVTSEPSRPEPAVFKATLDRSLLKTYEQVLENLESKRFQLV
DSRSQGRFLGTEPEPDAVGLDSGHIRGAVNMPFMDFLTEDGFEKGPEELRALFQTKKVDL
SQPLIATCRKGVTACHVALAAYLCGKPDVAVYDGSWSEWFRRAPPESRVSQGKSEKA
Enzyme 5 Number of Residues 297
Enzyme 5 Molecular Weight 33429
Enzyme 5 Theoretical pI 7.28
Enzyme 5 GO Classification
Function
  • catalytic activity
  • sulfurtransferase activity
  • thiosulfate sulfurtransferase activity
  • transferase activity
  • transferase activity, transferring sulfur-containing groups
Process
  • anion transport
  • cellular physiological process
  • inorganic anion transport
  • ion transport
  • physiological process
  • sulfate transport
  • transport
Component
—
Enzyme 5 General Function Inorganic ion transport and metabolism
Enzyme 5 Specific Function Not Available
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions
  • thiosulfate + cyanide = sulfite + thiocyanate [RN:R01931] ALL_REAC R01931
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein Not Available
Enzyme 5 UniProtKB/Swiss-Prot ID B3KRM1 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name B3KRM1_HUMAN Link Image
Enzyme 5 PDB ID 1ORB Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence Not Available
Enzyme 5 GenBank Gene ID AK091874 Link Image
Enzyme 5 GeneCard ID B3KRM1 Link Image
Enzyme 5 GenAtlas ID Not Available
Enzyme 5 HGNC ID Not Available
Enzyme 5 Chromosome Location 22
Enzyme 5 Locus 22q13.1
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References Not Available
Enzyme 5 Metabolite References Not Available