Information on EC 4.5.1.5 - S-carboxymethylcysteine synthase

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The expected taxonomic range for this enzyme is: Escherichia coli

EC NUMBER
COMMENTARY
4.5.1.5
-
RECOMMENDED NAME
GeneOntology No.
S-carboxymethylcysteine synthase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
3-chloro-L-alanine + thioglycolate = S-carboxymethyl-L-cysteine + chloride
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
beta-replacement
-
-
-
-
carbon-halide lyase reaction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
3-chloro-L-alanine chloride-lyase (adding thioglycolate; S-carboxymethyl-L-cysteine-forming)
A pyridoxal-phosphate protein.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
S-carboxymethyl-L-cysteine synthase
-
-
-
-
SC-Cys synthase
-
-
-
-
synthase, S-carboxymethylcysteine
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
124671-39-2
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain W 3110
-
-
Manually annotated by BRENDA team
Escherichia coli W 3110
strain W 3110
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
Escherichia coli, Escherichia coli W 3110
-
55% of activity compared to thioglycolate
-
?
3-chloro-L-alanine + methylmercaptan
S-methyl-L-cysteine + Cl-
show the reaction diagram
Escherichia coli, Escherichia coli W 3110
-
65% of activity compared to thioglycolate
-
?
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
Escherichia coli, Escherichia coli W 3110
-
beta-replacement reaction
-
?
additional information
?
-
-
not: L-cysteine, L-serine, L-threonine, L-cystine, 3-chloro-D-alanine, DL-homocysteine, L-methionine, L-homoserine, sodium hydrosulfide, isopropylmercaptan, 2-mercaptopropionic acid, 3-mercaptopropionic acid, enzyme catalyzes the alpha,beta-elimination reaction of 3-chloro-L-alanine, L-serine and L-cystathionine at a very low rate, constitutive enzyme
-
-
-
additional information
?
-
Escherichia coli W 3110
-
not: L-cysteine, L-serine, L-threonine, L-cystine, 3-chloro-D-alanine, DL-homocysteine, L-methionine, L-homoserine, sodium hydrosulfide, isopropylmercaptan, 2-mercaptopropionic acid, 3-mercaptopropionic acid, enzyme catalyzes the alpha,beta-elimination reaction of 3-chloro-L-alanine, L-serine and L-cystathionine at a very low rate, constitutive enzyme
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
Escherichia coli, Escherichia coli W 3110
-
constitutive enzyme
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
as cofactor, a pyridoxal phosphate protein
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
not inhibited by the substrate 3-chloro-L-alanine
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
40
-
3-chloro-L-alanine
-
pH 7.8, 37°C
15.4
-
thioglycolate
-
pH 7.8, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.8
-
-
assay at
9
10.5
-
broad, S-carboxymethyl-L-cysteine synthesis
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
assay at
50
-
-
S-carboxymethyl-L-cysteine synthesis
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
84000
-
-
HPLC gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
homodimer
-
2 * 37000, SDS-PAGE; 2 * 42000, HPLC gel filtration in presence of SDS
homodimer
Escherichia coli W 3110
-
2 * 37000, SDS-PAGE; 2 * 42000, HPLC gel filtration in presence of SDS
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
fine yellow needles
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
7.5
-
stable pH-range, S-carboxymethyl-L-cysteine synthesis
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
60
-
-
10 min, stable up to, S-carboxymethyl-L-cysteine synthesis
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
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
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE