KEGG   ENZYME: 4.4.1.25
Entry
EC 4.4.1.25                 Enzyme                                 

Name
L-cysteate sulfo-lyase;
L-cysteate sulfo-lyase (deaminating);
CuyA;
L-cysteate bisulfite-lyase (deaminating;
pyruvate-forming)
Class
Lyases;
Carbon-sulfur lyases;
Carbon-sulfur lyases (only sub-subclass identified to date)
Sysname
L-cysteate hydrogensulfite-lyase (deaminating; pyruvate-forming)
Reaction(IUBMB)
L-cysteate + H2O = hydrogensulfite + pyruvate + NH3 (overall reaction) [RN:R07634];
(1a) L-cysteate = hydrogensulfite + 2-aminoprop-2-enoate;
(1b) 2-aminoprop-2-enoate = 2-iminopropanoate (spontaneous);
(1c) 2-iminopropanoate + H2O = pyruvate + NH3 (spontaneous)
Reaction(KEGG)
R07634
Substrate
L-cysteate [CPD:C00506];
H2O [CPD:C00001];
2-aminoprop-2-enoate [CPD:C02218];
2-iminopropanoate [CPD:C20904]
Product
hydrogensulfite;
pyruvate [CPD:C00022];
NH3 [CPD:C00014];
2-aminoprop-2-enoate [CPD:C02218];
2-iminopropanoate [CPD:C20904]
Comment
A pyridoxal-phosphate protein. The enzyme cleaves a carbon-sulfur bond, releasing hydrogensulfite and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. D-Cysteine can also act as a substrate, but more slowly. It is converted into hydrogen sulfide, pyruvate, and ammonia. This inducible enzyme from the marine bacterium Silicibacter pomeroyi DSS-3 forms part of the cysteate-degradation pathway.
History
EC 4.4.1.25 created 2006
Pathway
ec00270  Cysteine and methionine metabolism
ec01100  Metabolic pathways
Orthology
K17950  L-cysteate sulfo-lyase
Genes
ENF: AKI40_4522
KOX: KOX_18740
KOE: A225_2619
KOY: J415_18880
KOM: HR38_17105
KOK: KONIH1_12530
CKO: CKO_02077
CAMA: F384_24035
CFAR: CI104_20845
CTEL: GBC03_08970
RTG: NCTC13098_02583(dcyD_1)
REE: electrica_04627(cuyA)
EBF: D782_2775
RAA: Q7S_11730
ECA: ECA1531
PATR: EV46_07745
PATO: GZ59_15690
PCT: PC1_1404
PEC: W5S_1716
DDD: Dda3937_02691(dcyD)
DDQ: DDI_1238
PMAN: OU5_6079
PSIL: PMA3_13030
PAR: Psyc_1604
SPL: Spea_4164
SHL: Shal_0079
SPSW: Sps_03974
PAT: Patl_2666
MICC: AUP74_01091(cuyA_1)
LFA: LFA_0645
SALN: SALB1_2529
BGO: BM43_4559
BPH: Bphy_5685
BFN: OI25_8251
PSPU: NA29_16035
BPAR: BN117_4146
BPA: BPP4074
BBR: BB4545
AXX: ERS451415_03296(acdS_2)
RTA: Rta_27290(dcyD)
CBX: Cenrod_1469(dcyD)
HYB: Q5W_20320
JAG: GJA_4883
DAT: HRM2_15340(dcyD1)
PLA: Plav_0934
RBS: RHODOSMS8_00523(cuyA)
SMD: Smed_5532
RLG: Rleg_6848
BARH: WN72_37835
MEA: Mex_1p2360(dcyD)
MDI: METDI3140(dcyD)
MEX: Mext_2357
MCH: Mchl_2636
MPO: Mpop_2314
META: Y590_11380
MMED: Mame_04307(cuyA)
CCR: CC_2032
CAK: Caul_3180
CSE: Cseg_1395
PZU: PHZ_c2912
SIL: SPO2657 SPOA0158(cuyA)
RUT: FIU92_00390(cuyA) FIU92_19550(dcyD)
RLI: RLO149_c007450(cuyA)
DSH: Dshi_1439
PGA: PGA1_c25520(dcyD) PGA1_c33720(dcyD2)
PGD: Gal_02808
LAQU: R2C4_20010
PTP: RCA23_c24520(dcyD)
RHC: RGUI_2479
ROH: FIU89_02605(cuyA)
AHT: ANTHELSMS3_04525(cuyA)
MALU: KU6B_40360
ZMI: ZCP4_1823
ZMC: A265_01765(dcyD)
ZMR: A254_01785(dcyD)
SHUM: STHU_12380
PSAB: PSAB_12415
LHIL: G8J22_02199(cuyA)
MMAG: MMAD_31310
MARZ: MARA_41600
RER: RER_54610
REY: O5Y_26010
SHY: SHJG_8020
SMAL: SMALA_7536
SRW: TUE45_00250(dcyD)
SRJ: SRO_0788
MMAR: MODMU_3995
KRA: Krad_0767
AMN: RAM_02115
AMM: AMES_0412(dcyD)
AMZ: B737_0413(dcyD)
AOI: AORI_0427(dcyD)
AORI: SD37_39110
KAL: KALB_4130
ACTN: L083_6387
AFS: AFR_32880
AMR: AM1_1636
STI: Sthe_0126
ATM: ANT_22590
PBF: CFX0092_A3104(cuyA)
SDYN: Mal52_16510(cuyA)
GES: VT84_20045(cuyA)
FTJ: FTUN_7586
ULI: ETAA1_31550(cuyA)
ABAC: LuPra_03549(cuyA_2)
SMIZ: 4412673_02127(dcyD_1)
FBU: UJ101_01236(dcyD)
BARC: AOA65_2400
 » show all
Reference
1  [PMID:16302849]
  Authors
Denger K, Smits TH, Cook AM
  Title
L-cysteate sulpho-lyase, a widespread pyridoxal 5'-phosphate-coupled desulphonative enzyme purified from Silicibacter pomeroyi DSS-3(T).
  Journal
Biochem J 394:657-64 (2006)
DOI:10.1042/BJ20051311
  Sequence
[sil:SPOA0158]
Other DBs
ExplorEnz - The Enzyme Database: 4.4.1.25
IUBMB Enzyme Nomenclature: 4.4.1.25
ExPASy - ENZYME nomenclature database: 4.4.1.25
BRENDA, the Enzyme Database: 4.4.1.25

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