KEGG   ENZYME: 4.4.1.36Help
Entry
EC 4.4.1.36                 Enzyme                                 

Name
hercynylcysteine S-oxide lyase;
egtE (gene name)
Class
Lyases;
Carbon-sulfur lyases;
Carbon-sulfur lyases (only sub-subclass identified to date)
BRITE hierarchy
Sysname
S-(hercyn-2-yl)-L-cysteine ergothioneine-hydroxysulfanolate-lyase
Reaction(IUBMB)
S-(hercyn-2-yl)-L-cysteine S-oxide + reduced acceptor = ergothioneine + pyruvate + NH3 + acceptor (overall reaction) [RN:R11023];
(1a) S-(hercyn-2-yl)-L-cysteine S-oxide + H2O = 2-(hydroxysulfanyl)hercynine + pyruvate + NH3 [RN:R11864];
(1b) 2-(hydroxysulfanyl)hercynine + reduced acceptor = ergothioneine + acceptor + H2O (spontaneous) [RN:R11865]
Reaction(KEGG)
Substrate
S-(hercyn-2-yl)-L-cysteine S-oxide [CPD:C20994];
reduced acceptor [CPD:C00030];
H2O [CPD:C00001];
2-(hydroxysulfanyl)hercynine [CPD:C21731]
Product
ergothioneine [CPD:C05570];
pyruvate [CPD:C00022];
NH3 [CPD:C00014];
acceptor [CPD:C00028];
2-(hydroxysulfanyl)hercynine [CPD:C21731];
H2O [CPD:C00001]
Comment
Contains pyridoxal 5'-phosphate. The enzyme, characterized from the bacterium Mycobacterium smegmatis, cayalyses the last step in the pathway of ergothioneine biosynthesis. The enzyme forms a 2-(hydroxysulfanyl)hercynine intermediate, which is reduced to ergothioneine non-enzymically by a thiol. In vitro, DTT can serve this function.
History
EC 4.4.1.36 created 2017
Pathway
ec00340  Histidine metabolism
ec01100  Metabolic pathways
Orthology
K18913  hercynylcysteine S-oxide lyase
K20247  hercynylcysteine S-oxide lyase
Genes
SKO: 102800903
FCD: 110858870
HRO: HELRODRAFT_164009
LGI: LOTGIDRAFT_139590 LOTGIDRAFT_176332 LOTGIDRAFT_176333 LOTGIDRAFT_200298
CRG: 105323290
LAK: 106164788 106177793
PDAM: 113671656
SPIS: 111345223
QSU: 111985281 111992444 112001256 112036968
KLA: KLLA0_F23441g
NCS: NCAS_0A13310(NCAS0A13310)
PIC: PICST_61494(CSD1)
CAL: CAALFM_C102970WA(CaO19.2988)
NCR: NCU11365
NTE: NEUTE1DRAFT120620(NEUTE1DRAFT_120620)
MGR: MGG_17802
SSCK: SPSK_01141
MAJ: MAA_05545
CMT: CCM_01645
MBE: MBM_00771
ANI: AN6227.2
ANG: ANI_1_278024(An02g02030) ANI_1_570044(An05g02190)
CIM: CIMG_11468(CIMG05065)
PTE: PTT_08491
CNE: CNM00480
CNB: CNBM0480
ABP: AGABI1DRAFT105046(AGABI1DRAFT_105046)
ABV: AGABI2DRAFT178673(AGABI2DRAFT_178673)
SMIN: v1.2.000197.t1(symbB.v1.2.000197.t1)
MTU: Rv3700c(egtE)
MTC: MT3803
MRA: MRA_3736
MTUR: CFBS_3921
MTD: UDA_3700c
MTUE: J114_19765
MTUH: I917_25945
MTUL: TBHG_03635
MTUT: HKBT1_3905
MTUU: HKBT2_3915
MBB: BCG_3759c
MBT: JTY_3761
MBX: BCGT_3562
MAF: MAF_37080
MPA: MAP_0302c
MAO: MAP4_3569
MAVI: RC58_17735
MAVU: RE97_17765
MAV: MAV_0403
MIT: OCO_03560
MIA: OCU_03630
MID: MIP_00740
MYO: OEM_03680
MIR: OCQ_03580
MMAL: CKJ54_01720(egtE)
MUL: MUL_4284(csdB)
MMC: Mmcs_4878
MKM: Mkms_4967
MJL: Mjls_5246
MMI: MMAR_5211(csdB)
MMAE: MMARE11_50340(csdB)
MMM: W7S_01750
MLI: MULP_05488(csdB)
MHAD: B586_03760
MSHG: MSG_04704(egtE)
MVA: Mvan_5482
MGI: Mflv_1319
MFT: XA26_56010(csdB)
MPHL: MPHLCCUG_00355(egtE)
MVQ: MYVA_5372(csdB)
MTHN: 4412656_04305(egtE)
MHAS: MHAS_03905(egtE_1)
MAB: MAB_0373
MABB: MASS_0369
MSTE: MSTE_00332(egtE)
MJD: JDM601_3980(csdB)
MTER: 4434518_03927(csdB)
ASD: AS9A_3384
GBR: Gbro_4836
GOR: KTR9_4734
GRU: GCWB2_23745(egtE)
GOM: D7316_03608(egtE)
LMOI: VV02_12395
SRO: Sros_0328
FAL: FRAAL4529
GOB: Gobs_0198
MMAR: MODMU_0215(csdB)
KRA: Krad_0981
 » show all
Taxonomy
Reference
1  [PMID:20420449]
  Authors
Seebeck FP
  Title
In vitro reconstitution of Mycobacterial ergothioneine biosynthesis.
  Journal
J Am Chem Soc 132:6632-3 (2010)
DOI:10.1021/ja101721e
  Sequence
Reference
2  [PMID:24828577]
  Authors
Pluskal T, Ueno M, Yanagida M
  Title
Genetic and metabolomic dissection of the ergothioneine and selenoneine biosynthetic pathway in the fission yeast, S. pombe, and construction of an overproduction system.
  Journal
PLoS One 9:e97774 (2014)
DOI:10.1371/journal.pone.0097774
  Sequence
Reference
3  [PMID:26149121]
  Authors
Song H, Hu W, Naowarojna N, Her AS, Wang S, Desai R, Qin L, Chen X, Liu P.
  Title
Mechanistic studies of a novel C-S lyase in ergothioneine biosynthesis: the involvement of a sulfenic acid intermediate.
  Journal
Sci Rep 5:11870 (2015)
DOI:10.1038/srep11870
Other DBs
ExplorEnz - The Enzyme Database: 4.4.1.36
IUBMB Enzyme Nomenclature: 4.4.1.36
ExPASy - ENZYME nomenclature database: 4.4.1.36
BRENDA, the Enzyme Database: 4.4.1.36
LinkDB All DBs

DBGET integrated database retrieval system