KEGG   ENZYME: 4.4.1.25Help
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)
BRITE hierarchy
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)
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
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
GQU: AWC35_03525
EBF: D782_2775
ECA: ECA1531
PATR: EV46_07745
PATO: GZ59_15690
PCT: PC1_1404
PEC: W5S_1716
DDD: Dda3937_02691(dcyD)
DDQ: DDI_1238
SPSW: Sps_03974
GPS: C427_3081
LFA: LFA_0645
BPA: BPP4074
BPAR: BN117_4146
BBR: BB4545
PUT: PT7_2783
RTA: Rta_27290(dcyD)
CBX: Cenrod_1469(dcyD)
HYB: Q5W_20320
RBS: RHODOSMS8_00523(cuyA)
MMED: Mame_04307(cuyA)
CCR: CC_2032
CAK: Caul_3180
CSE: Cseg_1395
PZU: PHZ_c2912
SIL: SPO2657 SPOA0158(cuyA)
RLI: RLO149_c007450(cuyA)
DSH: Dshi_1439
PGA: PGA1_c25520(dcyD) PGA1_c33720(dcyD2)
PGD: Gal_02808
PTP: RCA23_c24520(dcyD)
RHC: RGUI_2479
AHT: ANTHELSMS3_04525(cuyA)
ZMI: ZCP4_1823
ZMC: A265_01765(dcyD)
ZMR: A254_01785(dcyD)
PSAB: PSAB_12415
KAL: KALB_4130
BARC: AOA65_2400
 » show all
Taxonomy
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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