Entry
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
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
Genes
REE : electrica_04627(cuyA)
RTG : NCTC13098_02583(dcyD_1)
DDA : Dd703_1185 Dd703_1301
BGJ : AWC36_10070 AWC36_10530
BNG : EH206_10630 EH206_14450
BIZ : HC231_14730 HC231_15080
PLAL : FXN65_13345 FXN65_14445
GAG : Glaag_1613 Glaag_1767
MICC : AUP74_01091(cuyA_1)
WOC : BA177_13350 BA177_17580
NJP : NEJAP_0138 NEJAP_1593 NEJAP_3675
PNR : AT302_11325 AT302_19680
AXX : ERS451415_03296(acdS_2)
RBS : RHODOSMS8_00523(cuyA)
APRA : G3A50_13350 G3A50_21605
LABP : FJ695_09125 FJ695_16525
SIL : SPO2657 SPOA0158(cuyA)
RUA : D1823_13230 D1823_20180
RUT : FIU92_00390(cuyA) FIU92_19550(dcyD)
RUY : NOR97_00185 NOR97_17940
RLI : RLO149_c007450(cuyA)
PGA : PGA1_c25520(dcyD) PGA1_c33720(dcyD2)
SULZ : C1J03_10965 C1J03_15755
SINL : DSM14862_01602(cuyA)
RMM : ROSMUCSMR3_01902(cuyA) ROSMUCSMR3_02142(cuyA)
ROK : RAK1035_1044 RAK1035_1283
AHT : ANTHELSMS3_04525(cuyA)
PARS : DRW48_00910 DRW48_00915 DRW48_11285
NACI : NUH88_04710 NUH88_20715
PAQI : KW060_07430 KW060_07435 KW060_14185
GBX : SANA_26000 SANA_27930
AMYC : CU254_00815 CU254_14920
KPHY : AOZ06_19000 AOZ06_21100
LMAJ : GKN94_00625 GKN94_00635
MTAR : DF168_00203(cuyA_1) DF168_01335(cuyA_2)
ABAC : LuPra_03549(cuyA_2)
SMIZ : 4412673_02127(dcyD_1)
» show all
Taxonomy
Reference
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
Sequence
Other DBs
ExplorEnz - The Enzyme Database: 4.4.1.25
ExPASy - ENZYME nomenclature database: 4.4.1.25
LinkDB
All DBs