Information on EC 3.13.1.4 - 3-sulfinopropanoyl-CoA desulfinase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
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 enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.13.1.4
-
RECOMMENDED NAME
GeneOntology No.
3-sulfinopropanoyl-CoA desulfinase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3-sulfinopropanoyl-CoA + H2O = propanoyl-CoA + sulfite
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
3,3'-dithiodipropanoate degradation
-
-
3,3'-thiodipropanoate degradation
-
-
SYSTEMATIC NAME
IUBMB Comments
3-sulfinopropanoyl-CoA sulfinohydrolase
The enzyme from the beta-proteobacterium Advenella mimigardefordensis contains one non-covalently bound FAD per subunit.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-sulfinopropanoyl-CoA + H2O
propanoyl-CoA + sulfite
show the reaction diagram
3-sulfinopropionyl-CoA + H2O
propionyl-CoA + sulfite
show the reaction diagram
additional information
?
-
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
3-sulfinopropanoyl-CoA + H2O
propanoyl-CoA + sulfite
show the reaction diagram
3-sulfinopropionyl-CoA + H2O
propionyl-CoA + sulfite
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.013 - 0.019
3-sulfinopropanoyl-CoA
0.013 - 0.078
3-sulfinopropionyl-CoA
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.13 - 3.93
3-sulfinopropanoyl-CoA
1.1 - 4.4
3-sulfinopropionyl-CoA
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
203.2 - 237.2
3-sulfinopropanoyl-CoA
196328
41.7 - 240.8
3-sulfinopropionyl-CoA
5445
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.19
purified recombinant His6-tagged wild-type enzyme, pH 7.4, 30°C
5.26
purified recombinant His6-tagged mutant Q246E, pH 7.4, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.71
-
including His6-tag, calculated
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43531
-
4 * 43531, calculated, 4 * 44809, His6-tag, calculated
44809
-
4 * 43531, calculated, 4 * 44809, His6-tag, calculated
140000
-
experimentyl, gel filtration
157000
172000
-
theoretical, calculated
173000
174000
-
theoretical, calculated
175000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
tetramer
tri- or tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant apoenzyme and enzyme in complex with the CoA moiety from the substrate analogue succinyl-CoA, hanging drop vapour diffusion, mixing of 0.002 ml of 10 mg/ml protein in 50 mM Tris-HCl, pH 7.4, with 0.002 ml of reservoir solution containing 0.1 M Bis-Tris, pH 6.5, and 5-20% PEG 3350, in the absence or presence of 4 mM succinyl-CoA, X-ray diffraction structure determination and analysis at 1.89 A and 2.30 A resolution, respectively, molecular replacement using the monomer of an acyl-CoA dehydrogenase (Acd) from Thermus thermophilus HB8 as search model
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
His6-tagged recombinant protein
-
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) pLysS by nicke affinity chromatography and gel filtration
recombinant protein
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
heterologously expressed in Escherichia coli BL21
heterologously expressed in Escherichia coli BL21(DE3)/pLysS by using apET23a::acdDPN7 vector
-
recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3) pLysS
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DELTAacd
-
the mutant is defective in growth on 3,3'-dithiopropionate and 3-sulfinopropionate
Q246E
site-directed mutagenesis, substrate specificity of the mutant
R84K
site-directed mutagenesis, the mutant shows a complete loss of enzymatic activity
DELTAacd
-
the mutant is defective in growth on 3,3'-dithiopropionate and 3-sulfinopropionate
-
Q246E
-
site-directed mutagenesis, substrate specificity of the mutant
-
R84K
-
site-directed mutagenesis, the mutant shows a complete loss of enzymatic activity
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology