KEGG   ENZYME: 1.8.3.2Help
Entry
EC 1.8.3.2                  Enzyme                                 

Name
thiol oxidase;
sulfhydryl oxidase
Class
Oxidoreductases;
Acting on a sulfur group of donors;
With oxygen as acceptor
BRITE hierarchy
Sysname
thiol:oxygen oxidoreductase
Reaction(IUBMB)
2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2 [RN:R00057]
Reaction(KEGG)
Substrate
R'C(R)SH [CPD:C01525];
O2 [CPD:C00007]
Product
R'C(R)S-S(R)CR' [CPD:C02318];
H2O2 [CPD:C00027]
Comment
R may be =S or =O, or a variety of other groups. The enzyme is not specific for R'.
History
EC 1.8.3.2 created 1961, modified 2010, modified 2011
Orthology
K10758  thiol oxidase
K17783  mitochondrial FAD-linked sulfhydryl oxidase
K17891  FAD-linked sulfhydryl oxidase
Genes
HSA: 169714(QSOX2) 2671(GFER) 5768(QSOX1)
PTR: 457558(QSOX1) 464853(QSOX2) 750034(GFER)
PPS: 100969913(GFER) 100972262(QSOX2) 100974942(QSOX1)
GGO: 101130962(GFER) 101144374(QSOX2) 101145134(QSOX1)
PON: 100443539(QSOX2) 100461175(QSOX1) 100939629(GFER)
NLE: 100589353(QSOX2) 100596713(QSOX1) 100603322(GFER)
MCC: 694203(GFER) 718589(QSOX1) 721768(QSOX2)
MCF: 102116422(QSOX2) 102132065(QSOX1) 102135288(GFER)
CSAB: 103226489(GFER) 103230499(QSOX1) 103239638(QSOX2)
RRO: 104669681(QSOX2) 104671995(QSOX1) 104681532(GFER)
RBB: 108519412(GFER) 108539878(QSOX1) 108542920
CJC: 100386261(QSOX1) 100387900(QSOX2)
SBQ: 101033026(QSOX2) 101034321(GFER) 101046710(QSOX1)
MMU: 104009(Qsox1) 11692(Gfer) 227638(Qsox2)
RNO: 100912596 27100(Gfer) 681023(Qsox2) 84491(Qsox1)
CGE: 100754501(Qsox1) 100760425(Qsox2) 100767463(Gfer)
NGI: 103731365(Qsox1) 103752445(Gfer)
HGL: 101721514(Gfer) 101724305(Qsox2) 101725167(Qsox1)
CCAN: 109685826(Qsox1) 109690199(Gfer) 109699033(Qsox2)
OCU: 100350171(QSOX1)
TUP: 102478981(QSOX2) 102483047(GFER) 102491654(QSOX1)
CFA: 479885(GFER) 490299(QSOX1) 607571(QSOX2)
AML: 100465501(QSOX1) 100466926(QSOX2) 100469274(GFER)
UMR: 103668775(GFER) 103672519(QSOX1) 103675275(QSOX2)
ORO: 101370035(GFER) 101376993(QSOX1) 101387009(QSOX2)
FCA: 101080936(QSOX1) 101082968(GFER) 101092406(QSOX2)
PTG: 102955609(GFER) 102960400(QSOX2) 102969431(QSOX1)
AJU: 106966793(QSOX1) 106982787(GFER) 106989553(QSOX2)
BTA: 522986(QSOX1) 618423(GFER) 788063(QSOX2)
BOM: 102272021(QSOX1) 102280172(QSOX2) 102281574(GFER)
BIU: 109565678(QSOX2) 109570193(QSOX1) 109578675(GFER)
PHD: 102324133(QSOX1) 102335429(QSOX2) 102341153(GFER)
CHX: 102169539(GFER) 102183992(QSOX1)
OAS: 101114838(GFER) 101117322(QSOX2) 101119660(QSOX1) 105606047
SSC: 100515774(GFER) 100620285(QSOX1) 110258062(QSOX2)
CFR: 102517159(QSOX2) 102522629(QSOX1)
CDK: 105099721(GFER) 105099987(QSOX1) 105106018(QSOX2)
BACU: 102999797(QSOX2) 103000187(GFER) 103013580(QSOX1)
LVE: 103078425(QSOX1) 103082772 103089531(GFER)
OOR: 101273856(QSOX1) 101278399(GFER) 101285505(QSOX2)
ECB: 100053280(QSOX1) 100065617(GFER) 102147928(QSOX2)
EPZ: 103540177(GFER) 103566742(QSOX2) 103567054(QSOX1)
EAI: 106833918(QSOX1) 106836230(GFER) 106845511(QSOX2)
MYB: 102259357(QSOX1) 102262999(GFER) 106723999(QSOX2)
MYD: 102766578(QSOX1) 102768595(QSOX2) 102771246(GFER)
HAI: 109375440(QSOX1) 109382440(QSOX2) 109385933(GFER)
RSS: 109435325(GFER) 109448124(QSOX1) 109460885(QSOX2)
PALE: 102881649(GFER) 102887406(QSOX1) 102888757(QSOX2)
LAV: 100658926(QSOX2) 100665320(QSOX1) 100671973(GFER)
MDO: 100012299(GFER) 100020838(QSOX2) 100022601(QSOX1)
SHR: 100914570(QSOX1) 100917660(SYNGR3) 100932311(QSOX2)
OAA: 100082336(QSOX2)
GGA: 373914(QSOX1) 416547(GFER) 417129(QSOX2)
MGP: 100546511(QSOX1) 100550597(QSOX2) 104916286(GFER)
CJO: 107317290(QSOX1) 107320736(GFER) 107321709(QSOX2)
APLA: 101794211(QSOX2) 101797357(QSOX1) 101797850(GFER)
ACYG: 106032202(GFER) 106040651(QSOX2) 106042482(QSOX1)
TGU: 100225880(QSOX2) 100228549 100231379(QSOX1) 100232826(GFER)
GFR: 102040262(QSOX2) 102043037(QSOX1) 102045083(GFER)
FAB: 101807586(QSOX1) 101807595(GFER) 101808812(QSOX2)
PHI: 102101915(QSOX1) 102102749(GFER) 102108464(QSOX2)
PMAJ: 107207881(QSOX1) 107210932(GFER) 107211924(QSOX2)
CCW: 104684749(GFER) 104688501(QSOX2) 104693635(QSOX1)
FPG: 101912544(QSOX2) 101922468(QSOX1) 101924538(GFER)
FCH: 102051410(QSOX1) 102053360(QSOX2) 102058508(GFER)
CLV: 102090317(GFER) 102091512(QSOX2) 102096598(QSOX1)
EGZ: 104127735(GFER) 104131353(QSOX2) 104132087(QSOX1)
AAM: 106484952(QSOX1) 106486997(QSOX2) 106493827(GFER)
ASN: 102373437(QSOX1) 102374695 102374951 102381951(QSOX2) 102387767(GFER)
PSS: 102446040(QSOX2) 102453424(QSOX1) 102454904(GFER)
CMY: 102931685(QSOX2) 102940737(GFER) 102942745(QSOX1)
CPIC: 101936786(GFER) 101937647(QSOX2) 101948563(QSOX1)
ACS: 100551634(gfer) 100563795(qsox1) 103281876(qsox2)
PVT: 110077060(QSOX1) 110079617(QSOX2) 110090437(GFER)
PBI: 103052234(QSOX2) 103053400(GFER) 103060390(QSOX1)
GJA: 107105476(QSOX2) 107117870(GFER) 107125704(QSOX1)
XLA: 100036793(qsox1.L) 108698855(qsox2.L) 108714997(qsox1.S) 447270(qsox2.S) 733269(gfer.L)
XTR: 100158617(qsox2) 100488306(gfer) 613045(qsox1)
NPR: 108790867(GFER) 108793113(QSOX2) 108797543(QSOX1)
DRE: 100004382(qsox1) 559603(qsox2) 560433(gfer)
IPU: 108255911(qsox2) 108257358(gfer) 108265203(qsox1)
AMEX: 103023271(qsox2) 103029228 103035841(gfer)
TRU: 101061854(gfer) 101063609(qsox2) 101077738(qsox1)
LCO: 104917626(gfer) 104929348(qsox1) 109142966
NCC: 104956837(gfer)
OLA: 101158615(qsox2) 101164970(qsox1) 101167044(gfer)
XMA: 102226623(qsox2) 102227093(gfer) 102228107
PRET: 103460399(qsox2) 103464083 103468569(gfer)
NFU: 107376388(gfer) 107386171(qsox2) 107393136
CSEM: 103393251(gfer) 103393534 103398047(qsox2)
ELS: 105007326(gfer) 105008529(qsox2) 105029166(qsox1)
SFM: 108919022(qsox1) 108938666(qsox2) 108941733(gfer)
LCM: 102356701(QSOX1) 102360772(GFER) 102367303
CMK: 103179964(qsox1) 103183053(qsox2) 103186838(gfer)
DSI: Dsimw501_GD17467(Dsim_GD17467) Dsimw501_GD20911(Dsim_GD20911) Dsimw501_GD21029(Dsim_GD21029) Dsimw501_GD25776(Dsim_GD25776) Dsimw501_GD28785(Dsim_GD28785)
AME: 724451(Alr) 725287(GB11873)
PXY: 105388135
ZNE: 110830654
CEL: CELE_F47B7.2(F47B7.2) CELE_F56C11.3(F56C11.3)
SHX: MS3_04220
ATH: AT1G15020(QSOX1) AT1G49880(Erv1) AT2G01270(QSOX2)
LJA: Lj0g3v0299049.1(Lj0g3v0299049.1) Lj0g3v0299049.2(Lj0g3v0299049.2) Lj0g3v0299049.3(Lj0g3v0299049.3) Lj3g3v1800450.1(Lj3g3v1800450.1) Lj3g3v1810490.1(Lj3g3v1810490.1) Lj4g3v1614530.1(Lj4g3v1614530.1) Lj4g3v1614530.2(Lj4g3v1614530.2) Lj4g3v1614530.3(Lj4g3v1614530.3) Lj5g3v2166260.1(Lj5g3v2166260.1) Lj5g3v2166260.2(Lj5g3v2166260.2)
DOSA: Os03t0206300-01(Os03g0206300) Os05t0552500-01(Os05g0552500)
ATS: 109731552(LOC109731552)
ZMA: 100281926 606424(qsox1)
SCE: YGR029W(ERV1) YPR037C(ERV2)
KMX: KLMA_50206(ERV1) KLMA_70117(ERV2)
NCS: NCAS_0A02000(NCAS0A02000) NCAS_0A14750(NCAS0A14750) NCAS_0H00650(NCAS0H00650) NCAS_0J00810(NCAS0J00810)
NDI: NDAI_0A01260(NDAI0A01260) NDAI_0D00580(NDAI0D00580) NDAI_0D03940(NDAI0D03940)
TPF: TPHA_0B01430(TPHA0B01430) TPHA_0F00990(TPHA0F00990)
TBL: TBLA_0G01160(TBLA0G01160) TBLA_0I00800(TBLA0I00800)
TDL: TDEL_0C03200(TDEL0C03200) TDEL_0D02850(TDEL0D02850)
KAF: KAFR_0A06410(KAFR0A06410) KAFR_0F03790(KAFR0F03790) KAFR_0G00990(KAFR0G00990) KAFR_0K02190(KAFR0K02190)
CAL: CAALFM_C701720WA(CaO19.6552) CAALFM_CR03010CA(ERV1)
SLB: AWJ20_1118(ERV1)
NCR: NCU02396
NTE: NEUTE1DRAFT123953(NEUTE1DRAFT_123953)
MGR: MGG_13005
MAW: MAC_00101
MAJ: MAA_04500
ANI: AN3027.2
ANG: ANI_1_1578144(An16g02470)
ABE: ARB_04693
TVE: TRV_03135
PTE: PTT_14846
CNE: CND03420
CNB: CNBD2920
LBC: LACBIDRAFT_162969(LbErv1)
ABP: AGABI1DRAFT112062(AGABI1DRAFT_112062)
ABV: AGABI2DRAFT193305(AGABI2DRAFT_193305)
MGL: MGL_3837
DFA: DFA_04720
PYO: PY17X_0204800(PY00421) PY17X_1457900(PY01490)
PCB: PCHAS_020180(PC000050.02.0) PCHAS_145770(PC000280.02.0)
TAN: TA11885
TPV: TP02_0206
BBO: BBOV_II007550(18.m06628)
SMIN: v1.2.001303.t1(symbB.v1.2.001303.t1) v1.2.005139.t1(symbB.v1.2.005139.t1) v1.2.018764.t1(symbB.v1.2.018764.t1) v1.2.022980.t1(symbB.v1.2.022980.t1) v1.2.023569.t1(symbB.v1.2.023569.t1) v1.2.024769.t1(symbB.v1.2.024769.t1) v1.2.030713.t1(symbB.v1.2.030713.t1)
 » show all
Taxonomy
Reference
1  [PMID:13863296]
  Authors
AURBACH GD, JAKOBY WB.
  Title
The multiple functions of thiooxidase.
  Journal
J. Biol. Chem. 237 (1962) 565-8.
Reference
2  [PMID:13549489]
  Authors
NEUFELD HA, GREEN LF, LATTERELL FM, WEINTRAUB RL.
  Title
Thioxidase, a new sulfhydryl-oxidizing enzyme from Piricularia oryzae and Polyporus versicolor.
  Journal
J. Biol. Chem. 232 (1958) 1093-9.
Reference
3  [PMID:7397095]
  Authors
Ostrowski MC, Kistler WS
  Title
Properties of a flavoprotein sulfhydryl oxidase from rat seminal vesicle secretion.
  Journal
Biochemistry. 19 (1980) 2639-45.
Reference
4  [PMID:8940019]
  Authors
Hoober KL, Joneja B, White HB 3rd, Thorpe C
  Title
A sulfhydryl oxidase from chicken egg white.
  Journal
J. Biol. Chem. 271 (1996) 30510-6.
Reference
5  [PMID:17944490]
  Authors
Jaje J, Wolcott HN, Fadugba O, Cripps D, Yang AJ, Mather IH, Thorpe C
  Title
A flavin-dependent sulfhydryl oxidase in bovine milk.
  Journal
Biochemistry. 46 (2007) 13031-40.
  Sequence
[bta:522986]
Reference
6  [PMID:11584268]
  Authors
Sevier CS, Cuozzo JW, Vala A, Aslund F, Kaiser CA
  Title
A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation.
  Journal
Nat. Cell. Biol. 3 (2001) 874-82.
  Sequence
[sce:YPR037C]
Reference
7  [PMID:17972915]
  Authors
Dabir DV, Leverich EP, Kim SK, Tsai FD, Hirasawa M, Knaff DB, Koehler CM
  Title
A role for cytochrome c and cytochrome c peroxidase in electron shuttling from Erv1.
  Journal
EMBO. J. 26 (2007) 4801-11.
Reference
8  [PMID:15683237]
  Authors
Farrell SR, Thorpe C
  Title
Augmenter of liver regeneration: a flavin-dependent sulfhydryl oxidase with cytochrome c reductase activity.
  Journal
Biochemistry. 44 (2005) 1532-41.
Reference
9  [PMID:16407158]
  Authors
Gross E, Sevier CS, Heldman N, Vitu E, Bentzur M, Kaiser CA, Thorpe C, Fass D
  Title
Generating disulfides enzymatically: reaction products and electron acceptors of  the endoplasmic reticulum thiol oxidase Ero1p.
  Journal
Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 299-304.
Reference
10 [PMID:3427078]
  Authors
de la Motte RS, Wagner FW
  Title
Aspergillus niger sulfhydryl oxidase.
  Journal
Biochemistry. 26 (1987) 7363-71.
Reference
11 [PMID:19498160]
  Authors
Riemer J, Bulleid N, Herrmann JM
  Title
Disulfide formation in the ER and mitochondria: two solutions to a common process.
  Journal
Science. 324 (2009) 1284-7.
Other DBs
ExplorEnz - The Enzyme Database: 1.8.3.2
IUBMB Enzyme Nomenclature: 1.8.3.2
ExPASy - ENZYME nomenclature database: 1.8.3.2
UM-BBD (Biocatalysis/Biodegradation Database): 1.8.3.2
BRENDA, the Enzyme Database: 1.8.3.2
CAS: 9029-39-4

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