Sulfur amino acid metabolism (Homo sapiens)

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182, 23322, 2311172819, 212928, 3091, 272, 23221514, 312, 2310, 1682025, 26, 33221262, 231334245, 73mitochondrial matrixcytosolCDO1 BETFAD BHMT2 SO4(2-)2xHC-SQRDL(1-450) CysGlyAde-RibFMN GCLH2OGSSGH2OgGluCysMTAP ATPCSAD MTRIBPL-MetHTAUAdoMetL-SerMoCo (dioxyo) 3-SulfinoalanineS2O3(2-)QH2H+MTRR:MTR(MeCbl)H+TSTSQR:FADFe2+ Mg2+ H2O2L-LanthionineH2OH2SMAT1A H2OMg2+ Fe2+ FMN Zn2+ PXLP AdeMTRR H2OAHCY:NAD+ tetramerPXLP-CBS GCLC APIP H2S2xHC-SQRDL(1-450)FAD O2MTR MRI1CTH H2O2AETPXLP ADO:Fe2+NAD+CO2MALPiMTRIBUPCTH tetramer:PXLPO2MTRR CSAD dimerSMMholo-SUOXTAUO2L-MetCBS tetramerBHMT:Zn2+ tetramerATPPiCNDP2:2Mn2+ dimerCysS-SQRDL(1-450)MAT1A multimersH+2,3-DMPP4MTOBUTACoQH+Zn2+ O2SO4(2-)AHCY H+GOT1 dimerH+HLANE1:Mg++MTAP trimerH2OADPAcireductonesulfite(2-)PXLP BHMT2:Zn2+ tetramerZn2+ MTADHTAUDHAdoHcyO2HCYSH2ONADHZn2+ MTR MeCbl SUOX Amino AcidMTRR:MTR(cob(I)alamin)MALGCLM H+CNDP2 L-Cyscob(I)alamin HCOOHheme PiSQRDL(1-450)PXLP Zn2+ ETHE1 H2ODMGLYETHE1:2Zn++ADO PiZn2+ 2-Oxoacid2OBUTACTH tetramer:PXLPNH3H2SADI1 APIP:Zn++SLC25A10FAD Fe2+ GlyPPiCTH GOT1 CDO1:Fe2+NAD+ Mn2+ BHMT K+ H2OL-CystathionineL-GluENOPH1 GSHARD:Fe++425


Description

The main sulfur amino acids are methionine, cysteine, homocysteine and taurine. Of these, the first two are proteinogenic.

This group of reactions contains all processes that 1) break down sulfur amino acids, 2) interconvert between them, and 3) synthesize them from solved sulfide which comes from sulfate assimilation and reduction. Only plants and microorganisms employ all processes. Humans cannot de novo synthesize any sulfur amino acid, nor convert cysteine to methionine (Brosnan & Brosnan, 2006). View original pathway at:Reactome.

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Bibliography

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History

View all...
CompareRevisionActionTimeUserComment
100972view21:08, 31 October 2018ReactomeTeamreactome version 65
100509view19:42, 31 October 2018ReactomeTeamreactome version 64
100055view16:26, 31 October 2018ReactomeTeamreactome version 63
99607view14:59, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
99219view12:44, 31 October 2018ReactomeTeamreactome version 62
93813view13:38, 16 August 2017ReactomeTeamreactome version 61
93357view11:21, 9 August 2017ReactomeTeamreactome version 61
88427view12:04, 5 August 2016FehrhartOntology Term : 'amino acid metabolic pathway' added !
86439view09:18, 11 July 2016ReactomeTeamreactome version 56
83464view12:29, 18 November 2015ReactomeTeamNew pathway

External references

DataNodes

View all...
NameTypeDatabase referenceComment
2,3-DMPPMetaboliteCHEBI:58828 (ChEBI)
2-OxoacidR-NUL-1237175 (Reactome)
2AETMetaboliteCHEBI:17141 (ChEBI)
2OBUTAMetaboliteCHEBI:30831 (ChEBI)
2xHC-SQRDL(1-450) ProteinQ9Y6N5 (Uniprot-TrEMBL)
2xHC-SQRDL(1-450)ProteinQ9Y6N5 (Uniprot-TrEMBL)
3-SulfinoalanineMetaboliteCHEBI:16345 (ChEBI)
4MTOBUTAMetaboliteCHEBI:16723 (ChEBI)
ADI1 ProteinQ9BV57 (Uniprot-TrEMBL)
ADO ProteinQ96SZ5 (Uniprot-TrEMBL)
ADO:Fe2+ComplexR-HSA-6814156 (Reactome)
ADPMetaboliteCHEBI:16761 (ChEBI)
AHCY ProteinP23526 (Uniprot-TrEMBL)
AHCY:NAD+ tetramerComplexR-HSA-174358 (Reactome)
APIP ProteinQ96GX9 (Uniprot-TrEMBL)
APIP:Zn++ComplexR-HSA-1237083 (Reactome)
ARD:Fe++ComplexR-HSA-1237173 (Reactome)
ATPMetaboliteCHEBI:15422 (ChEBI)
AcireductoneMetaboliteCHEBI:58795 (ChEBI)
Ade-RibMetaboliteCHEBI:16335 (ChEBI)
AdeMetaboliteCHEBI:16708 (ChEBI)
AdoHcyMetaboliteCHEBI:16680 (ChEBI)
AdoMetMetaboliteCHEBI:15414 (ChEBI)
Amino AcidR-NUL-69599 (Reactome)
BETMetaboliteCHEBI:17750 (ChEBI)
BHMT ProteinQ93088 (Uniprot-TrEMBL)
BHMT2 ProteinQ9H2M3 (Uniprot-TrEMBL)
BHMT2:Zn2+ tetramerComplexR-HSA-5696826 (Reactome)
BHMT:Zn2+ tetramerComplexR-HSA-6798211 (Reactome)
CBS tetramerComplexR-HSA-1614610 (Reactome)
CDO1 ProteinQ16878 (Uniprot-TrEMBL)
CDO1:Fe2+ComplexR-HSA-1614609 (Reactome)
CNDP2 ProteinQ96KP4 (Uniprot-TrEMBL)
CNDP2:2Mn2+ dimerComplexR-HSA-1258421 (Reactome)
CO2MetaboliteCHEBI:16526 (ChEBI)
CSAD ProteinQ9Y600 (Uniprot-TrEMBL)
CSAD dimerComplexR-HSA-1655430 (Reactome)
CTH ProteinP32929 (Uniprot-TrEMBL)
CTH tetramer:PXLPComplexR-HSA-1625212 (Reactome)
CoQMetaboliteCHEBI:16389 (ChEBI)
CysGlyMetaboliteCHEBI:4047 (ChEBI)
CysS-SQRDL(1-450)ProteinQ9Y6N5 (Uniprot-TrEMBL)
DMGLYMetaboliteCHEBI:17724 (ChEBI)
E1:Mg++ComplexR-HSA-1237166 (Reactome)
ENOPH1 ProteinQ9UHY7 (Uniprot-TrEMBL)
ETHE1 ProteinO95571 (Uniprot-TrEMBL)
ETHE1:2Zn++ComplexR-HSA-1614521 (Reactome)
FAD MetaboliteCHEBI:16238 (ChEBI)
FMN MetaboliteCHEBI:17621 (ChEBI)
Fe2+ MetaboliteCHEBI:18248 (ChEBI)
GCLC ProteinP48506 (Uniprot-TrEMBL)
GCLM ProteinP48507 (Uniprot-TrEMBL)
GCLComplexR-HSA-174377 (Reactome)
GOT1 ProteinP17174 (Uniprot-TrEMBL)
GOT1 dimerComplexR-HSA-70579 (Reactome)
GSHMetaboliteCHEBI:16856 (ChEBI)
GSSGMetaboliteCHEBI:17858 (ChEBI)
GlyMetaboliteCHEBI:15428 (ChEBI)
H+MetaboliteCHEBI:15378 (ChEBI)
H2O2MetaboliteCHEBI:16240 (ChEBI)
H2OMetaboliteCHEBI:15377 (ChEBI)
H2SMetaboliteCHEBI:16136 (ChEBI)
HCOOHMetaboliteCHEBI:30751 (ChEBI)
HCYSMetaboliteCHEBI:17230 (ChEBI)
HLANMetaboliteCHEBI:62856 (ChEBI)
HTAUMetaboliteCHEBI:16668 (ChEBI)
HTAUDHR-HSA-1655455 (Reactome)
K+ MetaboliteCHEBI:29103 (ChEBI)
L-CysMetaboliteCHEBI:17561 (ChEBI)
L-CystathionineMetaboliteCHEBI:17482 (ChEBI)
L-GluMetaboliteCHEBI:16015 (ChEBI)
L-LanthionineMetaboliteCHEBI:21347 (ChEBI)
L-MetMetaboliteCHEBI:16643 (ChEBI)
L-SerMetaboliteCHEBI:17115 (ChEBI)
MALMetaboliteCHEBI:30797 (ChEBI)
MAT1A ProteinQ00266 (Uniprot-TrEMBL)
MAT1A multimersComplexR-HSA-174383 (Reactome)
MRI1ProteinQ9BV20 (Uniprot-TrEMBL)
MTADMetaboliteCHEBI:17509 (ChEBI)
MTAP ProteinQ13126 (Uniprot-TrEMBL)
MTAP trimerComplexR-HSA-1237147 (Reactome)
MTR ProteinQ99707 (Uniprot-TrEMBL)
MTRIBPMetaboliteCHEBI:58533 (ChEBI)
MTRIBUPMetaboliteCHEBI:58548 (ChEBI)
MTRR ProteinQ9UBK8 (Uniprot-TrEMBL)
MTRR:MTR(MeCbl)ComplexR-HSA-3149551 (Reactome)
MTRR:MTR(cob(I)alamin)ComplexR-HSA-3149516 (Reactome)
MeCbl MetaboliteCHEBI:28115 (ChEBI)
Mg2+ MetaboliteCHEBI:18420 (ChEBI)
Mn2+ MetaboliteCHEBI:29035 (ChEBI)
MoCo (dioxyo) MetaboliteCHEBI:25372 (ChEBI)
NAD+ MetaboliteCHEBI:15846 (ChEBI)
NAD+MetaboliteCHEBI:15846 (ChEBI)
NADHMetaboliteCHEBI:16908 (ChEBI)
NH3MetaboliteCHEBI:16134 (ChEBI)
O2MetaboliteCHEBI:15379 (ChEBI)
PPiMetaboliteCHEBI:29888 (ChEBI)
PXLP MetaboliteCHEBI:18405 (ChEBI)
PXLP-CBS ProteinP35520 (Uniprot-TrEMBL)
PiMetaboliteCHEBI:18367 (ChEBI)
QH2MetaboliteCHEBI:17976 (ChEBI)
S2O3(2-)MetaboliteCHEBI:16094 (ChEBI)
SLC25A10ProteinQ9UBX3 (Uniprot-TrEMBL)
SMMMetaboliteCHEBI:17728 (ChEBI)
SO4(2-)MetaboliteCHEBI:16189 (ChEBI)
SQR:FADComplexR-HSA-1614651 (Reactome)
SQRDL(1-450)ProteinQ9Y6N5 (Uniprot-TrEMBL)
SUOX ProteinP51687 (Uniprot-TrEMBL)
TAUMetaboliteCHEBI:15891 (ChEBI)
TSTProteinQ16762 (Uniprot-TrEMBL)
Zn2+ MetaboliteCHEBI:29105 (ChEBI)
cob(I)alamin MetaboliteCHEBI:15982 (ChEBI)
gGluCysMetaboliteCHEBI:17515 (ChEBI)
heme MetaboliteCHEBI:17627 (ChEBI)
holo-SUOXComplexR-HSA-1614636 (Reactome)
sulfite(2-)MetaboliteCHEBI:17359 (ChEBI)

Annotated Interactions

View all...
SourceTargetTypeDatabase referenceComment
2,3-DMPPArrowR-HSA-1237140 (Reactome)
2,3-DMPPR-HSA-1237129 (Reactome)
2-OxoacidArrowR-HSA-1237102 (Reactome)
2AETR-HSA-6814153 (Reactome)
2OBUTAArrowR-HSA-1614583 (Reactome)
2OBUTAArrowR-HSA-1614631 (Reactome)
2xHC-SQRDL(1-450)R-HSA-1614665 (Reactome)
3-SulfinoalanineArrowR-HSA-1614645 (Reactome)
3-SulfinoalanineR-HSA-1655443 (Reactome)
4MTOBUTAArrowR-HSA-1237119 (Reactome)
4MTOBUTAR-HSA-1237102 (Reactome)
ADO:Fe2+mim-catalysisR-HSA-6814153 (Reactome)
ADPArrowR-HSA-174367 (Reactome)
AHCY:NAD+ tetramermim-catalysisR-HSA-174401 (Reactome)
APIP:Zn++mim-catalysisR-HSA-1237140 (Reactome)
ARD:Fe++mim-catalysisR-HSA-1237119 (Reactome)
ATPR-HSA-174367 (Reactome)
ATPR-HSA-174391 (Reactome)
AcireductoneArrowR-HSA-1237129 (Reactome)
AcireductoneR-HSA-1237119 (Reactome)
Ade-RibArrowR-HSA-174401 (Reactome)
AdeArrowR-HSA-1237160 (Reactome)
AdoHcyR-HSA-174401 (Reactome)
AdoMetArrowR-HSA-174391 (Reactome)
Amino AcidR-HSA-1237102 (Reactome)
BETR-HSA-1614654 (Reactome)
BHMT2:Zn2+ tetramermim-catalysisR-HSA-5696838 (Reactome)
BHMT:Zn2+ tetramermim-catalysisR-HSA-1614654 (Reactome)
CBS tetramermim-catalysisR-HSA-1614524 (Reactome)
CDO1:Fe2+mim-catalysisR-HSA-1614645 (Reactome)
CNDP2:2Mn2+ dimermim-catalysisR-HSA-1247910 (Reactome)
CO2ArrowR-HSA-1655443 (Reactome)
CSAD dimermim-catalysisR-HSA-1655443 (Reactome)
CTH tetramer:PXLPmim-catalysisR-HSA-1614567 (Reactome)
CTH tetramer:PXLPmim-catalysisR-HSA-1614583 (Reactome)
CTH tetramer:PXLPmim-catalysisR-HSA-1614591 (Reactome)
CTH tetramer:PXLPmim-catalysisR-HSA-1614614 (Reactome)
CTH tetramer:PXLPmim-catalysisR-HSA-1614631 (Reactome)
CoQR-HSA-1614665 (Reactome)
CysGlyR-HSA-1247910 (Reactome)
CysS-SQRDL(1-450)ArrowR-HSA-1614665 (Reactome)
CysS-SQRDL(1-450)R-HSA-1614605 (Reactome)
CysS-SQRDL(1-450)R-HSA-1614618 (Reactome)
DMGLYArrowR-HSA-1614654 (Reactome)
E1:Mg++mim-catalysisR-HSA-1237129 (Reactome)
ETHE1:2Zn++mim-catalysisR-HSA-1614605 (Reactome)
GCLmim-catalysisR-HSA-174367 (Reactome)
GOT1 dimermim-catalysisR-HSA-1237102 (Reactome)
GSHR-HSA-1655879 (Reactome)
GSSGArrowR-HSA-1655879 (Reactome)
GlyArrowR-HSA-1247910 (Reactome)
H+ArrowR-HSA-1237129 (Reactome)
H+ArrowR-HSA-1614605 (Reactome)
H+ArrowR-HSA-1655453 (Reactome)
H+ArrowR-HSA-5696838 (Reactome)
H+ArrowR-HSA-6814153 (Reactome)
H+R-HSA-1614665 (Reactome)
H+R-HSA-1655879 (Reactome)
H2O2ArrowR-HSA-1614544 (Reactome)
H2OArrowR-HSA-1237140 (Reactome)
H2OArrowR-HSA-1614524 (Reactome)
H2OR-HSA-1237129 (Reactome)
H2OR-HSA-1247910 (Reactome)
H2OR-HSA-1614544 (Reactome)
H2OR-HSA-1614583 (Reactome)
H2OR-HSA-1614605 (Reactome)
H2OR-HSA-1614614 (Reactome)
H2OR-HSA-1614631 (Reactome)
H2OR-HSA-1655453 (Reactome)
H2OR-HSA-174391 (Reactome)
H2OR-HSA-174401 (Reactome)
H2SArrowR-HSA-1614567 (Reactome)
H2SArrowR-HSA-1614591 (Reactome)
H2SArrowR-HSA-1614614 (Reactome)
H2SArrowR-HSA-1614631 (Reactome)
H2SArrowR-HSA-1655879 (Reactome)
H2SR-HSA-1614665 (Reactome)
HCOOHArrowR-HSA-1237119 (Reactome)
HCYSArrowR-HSA-1614567 (Reactome)
HCYSArrowR-HSA-174401 (Reactome)
HCYSR-HSA-1614524 (Reactome)
HCYSR-HSA-1614567 (Reactome)
HCYSR-HSA-1614631 (Reactome)
HCYSR-HSA-1614654 (Reactome)
HCYSR-HSA-174374 (Reactome)
HCYSR-HSA-5696838 (Reactome)
HLANArrowR-HSA-1614567 (Reactome)
HTAUArrowR-HSA-1655443 (Reactome)
HTAUArrowR-HSA-6814153 (Reactome)
HTAUDHmim-catalysisR-HSA-1655453 (Reactome)
HTAUR-HSA-1655453 (Reactome)
L-CysArrowR-HSA-1247910 (Reactome)
L-CysArrowR-HSA-1614583 (Reactome)
L-CysArrowR-HSA-1614591 (Reactome)
L-CysR-HSA-1614591 (Reactome)
L-CysR-HSA-1614614 (Reactome)
L-CysR-HSA-1614645 (Reactome)
L-CysR-HSA-174367 (Reactome)
L-CystathionineArrowR-HSA-1614524 (Reactome)
L-CystathionineR-HSA-1614583 (Reactome)
L-GluR-HSA-174367 (Reactome)
L-LanthionineArrowR-HSA-1614591 (Reactome)
L-MetArrowR-HSA-1237102 (Reactome)
L-MetArrowR-HSA-1614654 (Reactome)
L-MetArrowR-HSA-174374 (Reactome)
L-MetArrowR-HSA-5696838 (Reactome)
L-MetR-HSA-174391 (Reactome)
L-SerArrowR-HSA-1614614 (Reactome)
L-SerR-HSA-1614524 (Reactome)
MALArrowR-HSA-1614546 (Reactome)
MALR-HSA-1614546 (Reactome)
MAT1A multimersmim-catalysisR-HSA-174391 (Reactome)
MRI1mim-catalysisR-HSA-1237096 (Reactome)
MRI1mim-catalysisR-HSA-1299507 (Reactome)
MTADR-HSA-1237160 (Reactome)
MTAP trimermim-catalysisR-HSA-1237160 (Reactome)
MTRIBPArrowR-HSA-1237160 (Reactome)
MTRIBPArrowR-HSA-1299507 (Reactome)
MTRIBPR-HSA-1237096 (Reactome)
MTRIBUPArrowR-HSA-1237096 (Reactome)
MTRIBUPR-HSA-1237140 (Reactome)
MTRIBUPR-HSA-1299507 (Reactome)
MTRR:MTR(MeCbl)R-HSA-174374 (Reactome)
MTRR:MTR(MeCbl)mim-catalysisR-HSA-174374 (Reactome)
MTRR:MTR(cob(I)alamin)ArrowR-HSA-174374 (Reactome)
NAD+R-HSA-1655453 (Reactome)
NADHArrowR-HSA-1655453 (Reactome)
NH3ArrowR-HSA-1614583 (Reactome)
NH3ArrowR-HSA-1614631 (Reactome)
O2R-HSA-1237119 (Reactome)
O2R-HSA-1614544 (Reactome)
O2R-HSA-1614605 (Reactome)
O2R-HSA-1614645 (Reactome)
O2R-HSA-6814153 (Reactome)
PPiArrowR-HSA-174391 (Reactome)
PiArrowR-HSA-1237129 (Reactome)
PiArrowR-HSA-174367 (Reactome)
PiArrowR-HSA-174391 (Reactome)
PiR-HSA-1237160 (Reactome)
QH2ArrowR-HSA-1614665 (Reactome)
R-HSA-1237096 (Reactome) Equilibrium between 5'-methylthio ribose-1-phosphate and 5'-methylthio ribulose-1-phosphate is catalyzed by 5'-methylthio ribose-1-phosphate isomerase. (Kabuyama et al, 2009)
R-HSA-1237102 (Reactome) In the last step MOB gets transaminated to methionine. The reaction was confirmed in yeast, where several transaminases catalyze it, which appears to be also the case in rat. At the moment, the human enzymes involved are unknown but due to homology to the respective enzyme in the parasite Crithidia fasciculata we feel supported to state that human GOT is probably one of the involved transaminases. (Berger et al, 2001)
R-HSA-1237119 (Reactome) Acireducone (1,2-Dihydroxy-3-oxo-5'-methylthiopentene) is oxidized using acireductone dioxygenase and dioxygen. There are two reactions possible, dependent on the metal cofactor: the alternative product 3-methylthiopropionate using nickel was confirmed in Klebsiella. In eukaryotes using iron(II) the result is 4-methylthio-2-oxobutanoate (MOB). (Ju et al, 2006)
R-HSA-1237129 (Reactome) Acireductone synthase (also: enolase-phosphatase E1) catalyzes the dephosphorylation and conversion to enolate of 2,3-dioxo-5'-methylthiopentane-1-phosphate, yielding acireductone. (Wang et al, 2005)
R-HSA-1237140 (Reactome) The human enzyme with 5'-methylthio ribulose-1-phosphate isomerase activity is probably produced from the APIP gene, according to its orthology with the yeast Mde1p enzyme.
R-HSA-1237160 (Reactome) MTA phosphorylase catalyzes the cleavage of adenine from S-methylthioadenosine (MTA) and subsequent phosphorylation of the product, yielding 5'-methylthio ribose-1-phosphate (Kamatani et al. 1981). The active form of the enzyme is a homotrimer (Della Ragione et al. 1985). Mutations in the gene are associated with a rare bone dysplasia and cancer syndrome, DMS-MFH (Camacho-Vanegas et al. 2012).
R-HSA-1247910 (Reactome) Cytosolic, non-specific peptidase (CNDP2) can hydrolyse cysteinylglycine (CysGly) to release cysteine (L-Cys) and glycine (Gly) (Tuefel et al. 2003). CNDP2 is functional as a homodimer and requires 2 Mn2+ ion per subunit.
R-HSA-1299507 (Reactome) Equilibrium between 5'-methylthio ribose-1-phosphate and 5'-methylthio ribulose-1-phosphate is catalyzed by 5'-methylthio ribose-1-phosphate isomerase. (Kabuyama et al, 2009)
R-HSA-1614524 (Reactome) The first step of homocysteine conversion to cysteine is catalyzed by cystathionine beta-lyase, which adds a serine molecule to the substrate. The enzyme is a tetramer with two heme molecules as cofactor (Janosik et al. 2001).
R-HSA-1614544 (Reactome) Sulfite oxidase oxidizes sulfite to sulfate which is among the most important macronutrients in cells and the fourth most abundant anion in human plasma (300 micromolar). The enzyme has a molybdenum-molybdopterin cofactor (MoCo) bound (Wilson et al. 2006, Feng et al. 2007).
R-HSA-1614546 (Reactome) Sulfate leaves the mitochondrion with the help of the dicarboxylate carrier, via antiport with malate (Crompton et al. 1974, Fiemont et al. 1999)
R-HSA-1614567 (Reactome) Excess homocysteine will change the enzymatic activity of CBS such that other reactions than transsulfuration take place. In these reactions, oxobutanoate, lanthionine, and homolanthionine are produced by cystathionine gamma-lyase (CTH) (Chiku et al. 2009, Steegborn et al. 1999)
R-HSA-1614583 (Reactome) Cystathionine is cleaved to cysteine, oxobutanoate, and ammonia by the alpha,gamma-elimination activity of cystathionine gamma-lyase (CTH) (Chiku et al. 2009, Steegborn et al. 1999).
R-HSA-1614591 (Reactome) Excess homocysteine will change the enzymatic activity of CBS such that other reactions than transsulfuration take place. In these reactions, oxobutanoate, lanthionine, and homolanthionine are produced by cystathionine gamma-lyase (CTH) (Chiku et al. 2009, Steegborn et al. 1999)
R-HSA-1614605 (Reactome) The sulfur dioxygenase ETHE1 converts persulfides to sulfite. Loss of this activity leads to the rare ethylmalonyl encephalopathy where the body can no longer detoxify H2S (Tiranti et al, 2009).
R-HSA-1614614 (Reactome) alpha,beta-elimination activity of cystathionine-gamma-lyase (CTH) replaces the sulfur in cysteine with oxygen from water, resulting in serine and toxic hydrogen sulfide, which is further oxidized in mitochondria (Chiku et al. 2009, Steegborn et al. 1999).
R-HSA-1614618 (Reactome) The main reaction catalyzed by rhodanase is not the name-giving detoxification of cyanide to thiocyanate, but the transfer of a sulfur atom from SQR-S-SH onto sulfite yielding thiosulfate during sulfide oxidation. The activity of human rhodanase was inferred from the rat orthologue by Hildebrandt & Grieshaber, 2008.
R-HSA-1614631 (Reactome) Excess homocysteine will change the enzymatic activity of CBS such that other reactions than transsulfuration take place. In these reactions, oxobutanoate, lanthionine, and homolanthionine are produced by cystathionine gamma-lyase (CTH) (Chiku et al. 2009, Steegborn et al. 1999)
R-HSA-1614645 (Reactome) Oxidation of the thiol moiety of cysteine yields sulfinoalanine, which itself is processed to hypotaurine by an as of yet uncharacterized enzyme in humans . Whether further oxidation of hypotaurine to taurine needs an enzyme is unknown at present (Ye et al. 2007).
R-HSA-1614654 (Reactome) Remethylation of homocysteine (HCYS) to methionine (L-Met) can also proceed by using betaine (BET) as a methyl donor, which is oxidised to dimethylglycine (DMGLY). This reaction is also part of choline catabolism, thereby providing a link to folate-dependent, one-carbon metabolism (Li et al. 2008).
R-HSA-1614665 (Reactome) When SQR is in the oxidized state, it can bind hydrogen sulfide as persulfide to one of its own cysteine residue, the electrons being transferred to ubiquinone. After that the additional sulfur is dioxygenated by another enzyme (ETHE1). The activity of human SQR was deduced from the orthologue in Arenicola marina (Theissen et al. 2003, Hildebrandt & Grieshaber 2008).
R-HSA-1655443 (Reactome) Cysteine sulfinic acid decarboxylase (CSAD) mediates the decarboxylase of 3-sulfinoalanine to produce hypotuarine. CSAD functions as a homodimer and requires pyridoxal phosphate as a cofactor. Purification, characterisation and activity of CSAD has been determined from rat liver (Guion-Rain et al. 1975).
R-HSA-1655453 (Reactome) The as yet uncharacterised human enzyme hypotaurine dehydrogenase mediates the oxidation of hypotaurine to produce taurine. All studies to date have been performed predominantly in rat (Nakamura et al. 2006).
R-HSA-1655879 (Reactome) Thiosulfate is able to transfer its sulfur atom to glutathione, a reaction investigated in yeast (Chauncey & Westley 1983). No human enzyme has been characterised yet for this reaction.
R-HSA-174367 (Reactome) The first step in the formation of glutathione is the ligation of glutamate with cysteine, catalysed by the dimeric protein glutamate-cysteine ligase, GCL (Gipp et al. 1995, Misra & Griffith 1998).
R-HSA-174374 (Reactome) A methyl group from 5-methyltetrahydrofolate is transferred to homocysteine (HCYS) via a meCbl intermediate, forming methionine (L-Met) (Leclerc et al. 1996).
R-HSA-174391 (Reactome) S-adenosylmethionine (AdoMet, SAM) is an essential metabolite in all cells. AdoMet is a precursor in the synthesis of polyamines. Methionine adenosyltransferases (MAT) catalyse the only known AdoMet biosynthetic reaction from methionine (L-Met) and ATP. In mammalian tissues, three different forms of MAT (MAT I, MAT III and MAT II) have been identified that are the product of two different genes (MAT1A and MAT2A). MAT1A binds 1 K+ and 2 Mg2+ (or Co2+, not shown here) in tetrameric or dimeric form (Corrales et al. 2002, Mato et al. 1997).
R-HSA-174401 (Reactome) Adenosylhomocysteinase (AHCY) is a tetrameric, NAD+-bound, cytosolic protein that regulates all adenosylmethionine-(AdoMet) dependent transmethylations by hydrolysing the feedback inhibitor adenosylhomocysteine (AdoHcy) to homocysteine (HCYS) and adenosine (Ade-Rib) (Turner et al. 1998, Yang et al. 2003).
R-HSA-5696838 (Reactome) L-homocysteine (LHCYS) is derived from L-methionine (L-Met) and can either be remethylated to reform L-Met or take part in cysteine biosynthesis via the trans-sulfuration pathway. LHCYS remethylation can occur by the action of two enzymes; cobalamin-dependent methionine synthase and betaine-homocysteine methyltransferase, using methyltetrahydrofolate and betaine respectively as methyl donors. A third enzyme, S-methylmethionine-homocysteine S-methyltransferase (BHMT2), can use S-methylmethionine (SMM) as the methyl donor to methylate LHCYS and reform L-Met. BHMT2 is a tetrameric, cytosolic enzyme that requires one Zn2+ ion per subunit as cofactor (Szegedi et al. 2008).
R-HSA-6814153 (Reactome) Cysteine metabolism to its sulfoxidation end-products is dependent upon two iron-dependent enzymes that are the only known mammalian thiol dioxygenases. These two thiol dioxygenases are cysteine dioxygenase (CDO) and 2-aminoethanethiol dioxygenase (ADO, cysteamine dioxygenase ). Both of these thiol dioxygenases are essential for hypotaurine and taurine biosynthesis. ADO adds molecular oxygen to the sulfhydryl group of 2-aminoethanethiol (2AET, cysteamine) to form the sulfinic acid hypotaurine (HTAU) (Dominy et al. 2007).
S2O3(2-)ArrowR-HSA-1614618 (Reactome)
S2O3(2-)R-HSA-1655879 (Reactome)
SLC25A10mim-catalysisR-HSA-1614546 (Reactome)
SMMR-HSA-5696838 (Reactome)
SO4(2-)ArrowR-HSA-1614544 (Reactome)
SO4(2-)ArrowR-HSA-1614546 (Reactome)
SO4(2-)R-HSA-1614546 (Reactome)
SQR:FADmim-catalysisR-HSA-1614665 (Reactome)
SQRDL(1-450)ArrowR-HSA-1614605 (Reactome)
SQRDL(1-450)ArrowR-HSA-1614618 (Reactome)
TAUArrowR-HSA-1655453 (Reactome)
TSTmim-catalysisR-HSA-1614618 (Reactome)
gGluCysArrowR-HSA-174367 (Reactome)
holo-SUOXmim-catalysisR-HSA-1614544 (Reactome)
sulfite(2-)ArrowR-HSA-1614605 (Reactome)
sulfite(2-)ArrowR-HSA-1655879 (Reactome)
sulfite(2-)R-HSA-1614544 (Reactome)
sulfite(2-)R-HSA-1614618 (Reactome)
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