Information on EC 2.3.3.15 - sulfoacetaldehyde acetyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.3.3.15
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RECOMMENDED NAME
GeneOntology No.
sulfoacetaldehyde acetyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acetyl phosphate + sulfite = 2-sulfoacetaldehyde + phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C-S bond cleavage
-
-
-
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phosphate transfer
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transfer of phosphate
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
sulfoacetaldehyde degradation I
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sulfolactate degradation II
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sulfate reduction
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Taurine and hypotaurine metabolism
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SYSTEMATIC NAME
IUBMB Comments
acetyl-phosphate:sulfite S-acetyltransferase (acyl-phosphate hydrolysing, 2-oxoethyl-forming)
The reaction occurs in the reverse direction to that shown above. Requires Mg2+.
CAS REGISTRY NUMBER
COMMENTARY hide
9012-30-0
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Acetinobacter sp.
strain ICD
-
-
Manually annotated by BRENDA team
Acetinobacter sp. ICD
strain ICD
-
-
Manually annotated by BRENDA team
strain TAU-5
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-
Manually annotated by BRENDA team
strain TAU-5
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-
Manually annotated by BRENDA team
DSS-3
UniProt
Manually annotated by BRENDA team
taurine-decomposing strain
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
homotaurine metabolism
physiological function
XsC 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
2-sulfoacetaldehyde + phosphate
acetyl phosphate + 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
2-sulfoacetaldehyde + phosphate
acetyl phosphate + sulfite
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
thiamine diphosphate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
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5 mM, 60% inhibition
p-chloromercuribenzoate
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0.1 mM. 100% inhibition
sulfite
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above 1 mM, product inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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not stimulatory: NADH, NADPH, ADP, ATP, CoA, FAD, pyridoxal phosphate, pyridoxamine phosphate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.1 - 5
2-sulfoacetaldehyde
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.08
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crude extract
additional information
specific Xsc enzyme activity in extracts from cells grown with cysteate is 0.1 mkat/mg protein; specific Xsc enzyme activity in extracts from cells grown with sulfolactate is 0.9 mkat/mg protein; specific Xsc enzyme activity in extracts from cells grown with taurine is 1.5 mkat/mg protein
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
effectively absent in acetate grown cells, also absent in cysteate-grown cells
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
85000
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gel filtration
220000
Acetinobacter sp.
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gel zymography
252000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
4 x 63000-65000, SDS-PAGE, MALDI-TOF MS
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by anion exchange chromatography
partial
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme is expressed inducibly during growth with cysteate as a nitrogen source
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
thiamine diphosphate and MgSO4 restore enzyme activity of dialyzed preparations
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