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Information on EC 4.1.1.79 - sulfopyruvate decarboxylase
for references in articles please use BRENDA:EC4.1.1.79
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IUBMB Comments
Requires thiamine diphosphate. Does not decarboxylate pyruvate or phosphonopyruvate. The enzyme appears to be oxygen-sensitive.
The expected taxonomic range for this enzyme is: Archaea, Bacteria
- 4.1.1.79
- streptococcus
-
two-component
-
competence-stimulating
-
caries
-
ciarh
-
pneumococcal
-
comcde
-
bacteriocins
-
vicrk
-
mutacins
-
cariogenic
-
csp-induced
-
biofilm-related
-
comab
-
competence-specific
-
sub-mic
showSynonyms
comde, sulfopyruvate decarboxylase, 3-sulfopyruvate decarboxylase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ComDE
decarboxylase, sulfopyruvate
-
-
-
-
sulfopyruvate decarboxylase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3-sulfopyruvate = 2-sulfoacetaldehyde + CO2
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
decarboxylation
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
coenzyme M biosynthesis I, coenzyme M biosynthesis II, sulfolactate degradation II
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SYSTEMATIC NAME
IUBMB Comments
3-sulfopyruvate carboxy-lyase (2-sulfoacetaldehyde-forming)
Requires thiamine diphosphate. Does not decarboxylate pyruvate or phosphonopyruvate. The enzyme appears to be oxygen-sensitive.
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CAS REGISTRY NUMBER
COMMENTARY
303155-97-7
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-sulfopyruvate
2-sulfoacetaldehyde + CO2
Substrates: -
Products: -
Products: -
?
3-sulfopyruvate
2-sulfoacetaldehyde + CO2
Substrates: fourth step in biosynthesis of coenzyme M
Products: -
Products: -
?
3-sulfopyruvate
2-sulfoacetaldehyde + CO2
Substrates: -
Products: -
Products: -
?
3-sulfopyruvate
2-sulfoacetaldehyde + CO2
-
Substrates: -
Products: -
Products: -
?
3-sulfopyruvate
2-sulfoacetaldehyde + CO2
A3SN11; A3SN10
Substrates: -
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-sulfopyruvate
2-sulfoacetaldehyde + CO2
Substrates: fourth step in biosynthesis of coenzyme M
Products: -
Products: -
?
3-sulfopyruvate
2-sulfoacetaldehyde + CO2
Substrates: -
Products: -
Products: -
?
3-sulfopyruvate
2-sulfoacetaldehyde + CO2
A3SN11; A3SN10
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Bacteremia
The Streptococcus pneumoniae competence regulatory system influences respiratory tract colonization.
Meningitis
In vivo proteomics identifies the competence regulon and AliB oligopeptide transporter as pathogenic factors in pneumococcal meningitis.
Meningitis, Pneumococcal
In vivo proteomics identifies the competence regulon and AliB oligopeptide transporter as pathogenic factors in pneumococcal meningitis.
Pneumonia
The Streptococcus pneumoniae competence regulatory system influences respiratory tract colonization.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
A3SN11; A3SN10
specific ComDE enzyme activity in extracts from cells grown with sulfolactate is 0.9 mkat/mg protein, 0 mM Tris-HCl (pH 7.5), 1 mM thiamine diphosphate, 1 to 5 mM sulfopyruvate, and protein (0.1-1.0 mg/ml)
additional information
-
specific ComDE enzyme activity in extracts from cells grown with sulfolactate is 0.9 mkat/mg protein, 0 mM Tris-HCl (pH 7.5), 1 mM thiamine diphosphate, 1 to 5 mM sulfopyruvate, and protein (0.1-1.0 mg/ml)
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
disruption of the gene comE by transposon mutagenesis results in a partial coenzyme M auxotroph, which grows poorly in the absence of coenzyme M and retains less than 3% of the wild type level of coenzyme M biosynthesis. Upon coenzyme M addition, normal growth of the mutant is restored. Complementation of the mutation with the wild type comE gene in trans restores full growth in the absence of coenzyme M
physiological function
physiological function
A3SN11; A3SN10
ComDE is involved in sulfonate degradation
physiological function
the enzyme plays an important role in coenzyme M biosynthesis
physiological function
-
during degradation of 2,3-dihydroxypropane-1-sulfonate, Dinoroseobacter shibae primarily utilizes sulfolactate sulfo-lyase, and sulfopyruvate decarboxylase followed by sulfoacetaldehyde acetyltransferase, respectively, to complete desulfonation releasing the sulfonate-moiety
physiological function
-
during degradation of 2,3-dihydroxypropane-1-sulfonate, Roseobacter denitrificans primarily utilizes sulfolactate sulfolyase, and sulfopyruvate decarboxylase followed by sulfoacetaldehyde acetyltransferase, respectively, to complete desulfonation releasing the sulfonate-moiety
physiological function
-
during degradation of 2,3-dihydroxypropane-1-sulfonate, Dinoroseobacter shibae primarily utilizes sulfolactate sulfo-lyase, and sulfopyruvate decarboxylase followed by sulfoacetaldehyde acetyltransferase, respectively, to complete desulfonation releasing the sulfonate-moiety
-
Show AA Sequence and Transmembrane Helices (379 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
235000
A3SN11; A3SN10
native protein with alpha6beta6-structure, determined by gel filtration
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
inactivation by oxygen at 80°C and reactivation by reduction with dithionite
644226
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
purified ComDE is stable under an air atmosphere, it can be stored at 4°C for at least a month without loss of activity
A3SN11; A3SN10
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by anion exchange chromatography, hydrophobic interaction chromatography and gel filtration
A3SN11; A3SN10
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) RIL cells containing vector pDG121
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
degradation
degradation
-
during degradation of 2,3-dihydroxypropane-1-sulfonate, Dinoroseobacter shibae primarily utilizes sulfolactate sulfo-lyase, and sulfopyruvate decarboxylase followed by sulfoacetaldehyde acetyltransferase, respectively, to complete desulfonation releasing the sulfonate-moiety
degradation
-
during degradation of 2,3-dihydroxypropane-1-sulfonate, Roseobacter denitrificans primarily utilizes sulfolactate sulfolyase, and sulfopyruvate decarboxylase followed by sulfoacetaldehyde acetyltransferase, respectively, to complete desulfonation releasing the sulfonate-moiety
degradation
-
during degradation of 2,3-dihydroxypropane-1-sulfonate, Dinoroseobacter shibae primarily utilizes sulfolactate sulfo-lyase, and sulfopyruvate decarboxylase followed by sulfoacetaldehyde acetyltransferase, respectively, to complete desulfonation releasing the sulfonate-moiety
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Graupner, M.; Xu, H.; White, R.H.
Identification of the gene encoding sulfopyruvate decarboxylase, an enzyme involved in biosynthesis of coenzyme M
J. Bacteriol.
182
4862-4867
2000
Methanocaldococcus jannaschii (P58415), Methanocaldococcus jannaschii
brenda
Graham, D.E.; Taylor, S.M.; Wolf, R.Z.; Namboori, S.C.
Convergent evolution of coenzyme M biosynthesis in the Methanosarcinales: cysteate synthase evolved from an ancestral threonine synthase
Biochem. J.
424
467-478
2009
Methanosarcina acetivorans
brenda
Denger, K.; Mayer, J.; Buhmann, M.; Weinitschke, S.; Smits, T.H.; Cook, A.M.
Bifurcated degradative pathway of 3-sulfolactate in Roseovarius nubinhibens ISM via sulfoacetaldehyde acetyltransferase and (S)-cysteate sulfolyase
J. Bacteriol.
191
5648-5656
2009
Roseovarius nubinhibens (A3SN11 and A3SN10), Roseovarius nubinhibens
brenda
Sarmiento, F.; Ellison, C.K.; Whitman, W.B.
Genetic confirmation of the role of sulfopyruvate decarboxylase in coenzyme M biosynthesis in Methanococcus maripaludis
Archaea
2013
185250
2013
Methanococcus maripaludis, Methanococcus maripaludis (Q6LWM0)
brenda
Chen, X.; Liu, L.; Gao, X.; Dai, X.; Han, Y.; Chen, Q.; Tang, K.
Metabolism of chiral sulfonate compound 2,3-dihydroxypropane-1-sulfonate (DHPS) by Roseobacter bacteria in marine environment
Environ. Int.
157
106829
2021
Dinoroseobacter shibae, Dinoroseobacter shibae DFL 12, Roseobacter denitrificans
brenda
EXTERNAL LINKS (specific for EC-Number 4.1.1.79)
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Release 2026.1 (March 2026)
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