Information on EC 4.4.1.25 - L-cysteate sulfo-lyase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Search Reference ID:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Proteobacteria

EC NUMBER
COMMENTARY hide
4.4.1.25
-
RECOMMENDED NAME
GeneOntology No.
L-cysteate sulfo-lyase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-aminoprop-2-enoate = 2-iminopropanoate
show the reaction diagram
spontaneous
-
-
-
2-iminopropanoate + H2O = pyruvate + NH3
show the reaction diagram
spontaneous
-
-
-
L-cysteate + H2O = HSO3- + pyruvate + NH3
show the reaction diagram
overall reaction
-
-
-
L-cysteate = HSO3- + 2-aminoprop-2-enoate
show the reaction diagram
(1a)
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C-S bond cleavage
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Cysteine and methionine metabolism
-
-
cysteine metabolism
-
-
sulfolactate degradation III
-
-
SYSTEMATIC NAME
IUBMB Comments
L-cysteate bisulfite-lyase (deaminating; pyruvate-forming)
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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
RZATAU
-
-
Manually annotated by BRENDA team
RZATAU
-
-
Manually annotated by BRENDA team
strain RZACYSA and strain GRZCYSA
-
-
Manually annotated by BRENDA team
DSS-3
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
CuyA is involved in sulfonate degradation
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-cysteate + H2O
HSO3- + pyruvate + NH3
show the reaction diagram
-
-
-
-
?
L-cysteate + H2O
pyruvate + bisulfite + NH3
show the reaction diagram
additional information
?
-
-
enzyme also catalyzes the D-cysteine desulphhydrase reaction
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-cysteate + H2O
pyruvate + bisulfite + NH3
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
tightly bound to the enzyme
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
11.7
L-cysteate
-
pH 9.0, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.02
-
crude extract
additional information
-
specific CuyA enzyme activity in extracts from cells grown with cysteate is 5.2 mkat/mg protein; specific CuyA enzyme activity in extracts from cells grown with sulfolactate is 1.0 mkat/mg protein
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.8 - 9
-
enzyme in crude cell extract, 50 mM Tris buffer
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35000
-
SDS-PAGE
100000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 39000, SDS-PAGE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
frozen samples lose about 90% of the activity on thawing
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 2 months without significant loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by anion exchange chromatography
-