KEGG   ENZYME: 4.4.1.25Help
Entry
EC 4.4.1.25                 Enzyme                                 

Name
L-cysteate sulfo-lyase;
L-cysteate sulfo-lyase (deaminating);
CuyA
Class
Lyases;
Carbon-sulfur lyases;
Carbon-sulfur lyases (only sub-subclass identified to date)
BRITE hierarchy
Sysname
L-cysteate bisulfite-lyase (deaminating; pyruvate-forming)
Reaction(IUBMB)
L-cysteate + H2O = bisulfite + pyruvate + NH3 (overall reaction) [RN:R07634];
(1a) L-cysteate = bisulfite + 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;
2-iminopropanoate
Product
bisulfite [CPD:C11481];
pyruvate [CPD:C00022];
NH3 [CPD:C00014];
2-aminoprop-2-enoate;
2-iminopropanoate (spontaneous)
Comment
A pyridoxal-phosphate protein. The enzyme cleaves a carbon-sulfur bond, releasing bisulfite 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
Cysteine and methionine metabolism
Orthology
K17950  
L-cysteate sulfo-lyase
Genes
ECA: 
PATR: 
PATO: 
PCT: 
PCV: 
PWA: 
PEC: 
KOX: 
KOE: 
KOY: 
KOK: 
KOM: 
CKO: 
SFO: 
DDA: 
DDD: 
ROR: 
CED: 
EBF: 
VTU: 
ACD: 
GPS: 
SPIU: 
BPA: 
BPAR: 
BBR: 
BBM: 
BBH: 
PUT: 
RTA: 
Rta_27290(dcyD)
CBX: 
CCR: 
CCS: 
CAK: 
CSE: 
PZU: 
BSB: 
SIL: 
RDE: 
RLI: 
PAMI: 
DSH: 
PGA: 
PGD: 
LMD: 
PTP: 
ZMI: 
ZMC: 
ZMR: 
ZMP: 
APB: 
PSAB: 
KAL: 
 » 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 (2006) 657-64.
  Sequence
[sil:SPOA0158]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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