Information on EC 4.5.1.5 - S-carboxymethylcysteine synthase

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The expected taxonomic range for this enzyme is: Escherichia coli

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EC NUMBER
COMMENTARY hide
4.5.1.5
-
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RECOMMENDED NAME
GeneOntology No.
S-carboxymethylcysteine synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3-chloro-L-alanine + thioglycolate = S-carboxymethyl-L-cysteine + chloride
show the reaction diagram
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
beta-replacement
-
-
-
-
carbon-halide lyase reaction
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
3-chloro-L-alanine chloride-lyase (adding thioglycolate; S-carboxymethyl-L-cysteine-forming)
A pyridoxal-phosphate protein.
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CAS REGISTRY NUMBER
COMMENTARY hide
124671-39-2
-
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-chloro-L-alanine + 1-thioglycerol
S-2,3-dihydroxypropyl-L-cysteine + Cl-
show the reaction diagram
-
93% of activity compared to thioglycolate
-
?
3-chloro-L-alanine + 2-mercaptoethanol
S-2-hydroxyethyl-L-cysteine + Cl-
show the reaction diagram
-
242% of activity compared to thioglycolate
-
?
3-chloro-L-alanine + benzylmercaptan
S-benzyl-L-cysteine + Cl-
show the reaction diagram
-
35% of activity compared to thioglycolate
-
?
3-chloro-L-alanine + ethylmercaptan
S-ethyl-L-cysteine + Cl-
show the reaction diagram
3-chloro-L-alanine + methylmercaptan
S-methyl-L-cysteine + Cl-
show the reaction diagram
3-chloro-L-alanine + n-propylmercaptan
S-propyl-L-cysteine + Cl-
show the reaction diagram
-
4% of activity compared to thioglycolate
-
?
3-chloro-L-alanine + phenylmercaptan
S-phenyl-L-cysteine + Cl-
show the reaction diagram
-
207% of activity compared to thioglycolate
-
?
3-chloro-L-alanine + thioglycolate
S-carboxymethyl-L-cysteine + Cl-
show the reaction diagram
additional information
?
-
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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
additional information
?
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
as cofactor, a pyridoxal phosphate protein
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
not inhibited by the substrate 3-chloro-L-alanine
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
40
3-chloro-L-alanine
-
pH 7.8, 37°C
15.4
thioglycolate
-
pH 7.8, 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8
-
assay at
9 - 10.5
-
broad, S-carboxymethyl-L-cysteine synthesis
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
50
-
S-carboxymethyl-L-cysteine synthesis
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37000
-
2 * 37000, SDS-PAGE
42000
-
2 * 42000, HPLC gel filtration in presence of SDS
84000
-
HPLC gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
fine yellow needles
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7.5
-
stable pH-range, S-carboxymethyl-L-cysteine synthesis
648766
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
-
10 min, stable up to, S-carboxymethyl-L-cysteine synthesis
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
long-term storage of enzyme as ammonium sulfate precipitate decreases activity, reactivation by dialysis against 0.1 M potassium phosphate buffer, pH 7.8, containing 10 mM 2-mercaptoethanol, 0.02 mM pyridoxal phosphate, 4 mM EDTA
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 4.5.1.5)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)