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Sulfide (YMDB00121)

Identification
YMDB IDYMDB00121
NameSulfide
SpeciesSaccharomyces cerevisiae
StrainBaker's yeast
DescriptionSulfide, also known as sulphide or S(2-), belongs to the class of inorganic compounds known as other non-metal sulfides. These are inorganic compounds containing a sulfur atom of an oxidation state of -2, in which the heaviest atom bonded to the oxygen belongs to the class of other non-metals. Sulfide is possibly neutral. Sulfide exists in all living species, ranging from bacteria to humans. In yeast, sulfide is involved in the metabolic pathway called the sulfur metabolism pathway.
Structure
Thumb
MOLSDFPDBSMILESInChI
Synonyms
  • sulfanediide
  • Sulfide
  • sulfur
  • sulphide
  • S(2-)
  • Sulphide(2-)
CAS number18496-25-8
WeightAverage: 32.065
Monoisotopic: 31.97207069
InChI KeyUCKMPCXJQFINFW-UHFFFAOYSA-N
InChIInChI=1S/S/q-2
IUPAC Namesulfanediide
Traditional IUPAC Namesulfanediide
Chemical FormulaS
SMILES[S--]
Chemical Taxonomy
Description belongs to the class of inorganic compounds known as other non-metal sulfides. These are inorganic compounds containing a sulfur atom of an oxidation state of -2, in which the heaviest atom bonded to the oxygen belongs to the class of other non-metals.
KingdomInorganic compounds
Super ClassHomogeneous non-metal compounds
ClassOther non-metal organides
Sub ClassOther non-metal sulfides
Direct ParentOther non-metal sulfides
Alternative ParentsNot Available
Substituents
  • Other non-metal sulfide
Molecular FrameworkNot Available
External Descriptors
Physical Properties
StateSolid
Charge-2
Melting point112 °C
Experimental Properties
PropertyValueReference
Water SolubilityNot AvailablePhysProp
LogPNot AvailablePhysProp
Predicted Properties
PropertyValueSource
logP-0.038ChemAxon
Physiological Charge-1ChemAxon
Hydrogen Acceptor Count0ChemAxon
Hydrogen Donor Count0ChemAxon
Polar Surface Area0 ŲChemAxon
Rotatable Bond Count0ChemAxon
Refractivity5.76 m³·mol⁻¹ChemAxon
Polarizability2.93 ųChemAxon
Number of Rings0ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations
  • Cytoplasm
Organoleptic PropertiesNot Available
SMPDB Pathways
Sulfur metabolismPW002483 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Sulfur metabolismec00920 Map00920
SMPDB ReactionsNot Available
KEGG ReactionsNot Available
Concentrations
Intracellular ConcentrationsNot Available
Extracellular ConcentrationsNot Available
Spectra
Spectra
Spectrum TypeDescriptionSplash KeyView
GC-MSGC-MS Spectrum - GC-MS (2 TMS)splash10-03di-1900000000-447434090a2b915c1731JSpectraViewer | MoNA
GC-MSGC-MS Spectrum - GC-MS (Non-derivatized)splash10-03di-1900000000-447434090a2b915c1731JSpectraViewer | MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-001i-9000000000-05710009cb2405db27bdJSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-001i-9000000000-05710009cb2405db27bdJSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-001i-9000000000-05710009cb2405db27bdJSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-001i-9000000000-1ca61b38a516c734a4dbJSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-001i-9000000000-1ca61b38a516c734a4dbJSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-001i-9000000000-1ca61b38a516c734a4dbJSpectraViewer
MSMass Spectrum (Electron Ionization)splash10-001i-9000000000-5373be1d46feb66d09a8JSpectraViewer | MoNA
1D NMR1H NMR SpectrumNot AvailableJSpectraViewer
References
References:
  • UniProt Consortium (2011). "Ongoing and future developments at the Universal Protein Resource." Nucleic Acids Res 39:D214-D219.21051339
  • Scheer, M., Grote, A., Chang, A., Schomburg, I., Munaretto, C., Rother, M., Sohngen, C., Stelzer, M., Thiele, J., Schomburg, D. (2011). "BRENDA, the enzyme information system in 2011." Nucleic Acids Res 39:D670-D676.21062828
  • Kobayashi, K., Yoshimoto, A. (1982). "Studies on yeast sulfite reductase. V. Effects of ionic strength on enzyme activities." Biochim Biophys Acta 709:38-45.6758853
  • Cordente, A. G., Heinrich, A., Pretorius, I. S., Swiegers, J. H. (2009). "Isolation of sulfite reductase variants of a commercial wine yeast with significantly reduced hydrogen sulfide production." FEMS Yeast Res 9:446-459.19236486
Synthesis Reference:Green, Martina; Verkoczy, Bela; Lown, Elizabeth M.; Strausz, Otto P. The reactions of sulfur atoms with propadiene and 1,2-butadiene. Canadian Journal of Chemistry (1985), 63(3), 667-75.
External Links:
ResourceLink
CHEBI ID15138
HMDB IDHMDB00598
Pubchem Compound ID5362487
Kegg IDC00087
ChemSpider ID27079
FOODB IDFDB022136
WikipediaSulfide
BioCyc IDCPD-249

Enzymes

Protein Details
1. Putative cysteine synthase
General function:
Involved in cysteine biosynthetic process from serine
Specific function:
O(3)-acetyl-L-serine + H(2)S = L-cysteine + acetate
Gene Name:
Not Available
Uniprot ID:
P53206
Molecular weight:
42800.5
Reactions
O(3)-acetyl-L-serine + H(2)S → L-cysteine + acetate.
Protein Details
2. Protein MET17
General function:
Involved in pyridoxal phosphate binding
Specific function:
Transforms O-acetylhomoserine into homocysteine and O- acetylserine into cysteine
Gene Name:
MET17
Uniprot ID:
P06106
Molecular weight:
48671.39844
Reactions
O-acetyl-L-homoserine + methanethiol → L-methionine + acetate.
O(3)-acetyl-L-serine + H(2)S → L-cysteine + acetate.
Protein Details
3. Biotin synthase, mitochondrial
General function:
Involved in catalytic activity
Specific function:
Dethiobiotin + sulfur + 2 S-adenosyl-L- methionine = biotin + 2 L-methionine + 2 5'-deoxyadenosine
Gene Name:
BIO2
Uniprot ID:
P32451
Molecular weight:
41883.80078
Reactions
Dethiobiotin + sulfur + 2 S-adenosyl-L-methionine → biotin + 2 L-methionine + 2 5'-deoxyadenosine.
Protein Details
4. Sulfite reductase [NADPH] subunit beta
General function:
Involved in iron ion binding
Specific function:
Catalyzes the reduction of sulfite to sulfide, one of several activities required for the biosynthesis of L-cysteine from sulfate
Gene Name:
ECM17
Uniprot ID:
P47169
Molecular weight:
161218.0
Reactions
H(2)S + 3 NADP(+) + 3 H(2)O → sulfite + 3 NADPH.
Protein Details
5. Sulfite reductase [NADPH] flavoprotein component
General function:
Involved in oxidoreductase activity
Specific function:
This enzyme catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate
Gene Name:
MET10
Uniprot ID:
P39692
Molecular weight:
114827.0
Reactions
H(2)S + 3 NADP(+) + 3 H(2)O → sulfite + 3 NADPH.
Protein Details
6. Lipoyl synthase, mitochondrial
General function:
Involved in catalytic activity
Specific function:
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives (Probable)
Gene Name:
LIP5
Uniprot ID:
P32875
Molecular weight:
46246.80078
Reactions
Protein N(6)-(octanoyl)lysine + 2 sulfur + 2 S-adenosyl-L-methionine → protein N(6)-(lipoyl)lysine + 2 L-methionine + 2 5'-deoxyadenosine.