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Information on EC 4.1.1.79 - sulfopyruvate decarboxylase and Organism(s) Methanococcus maripaludis and UniProt Accession Q6LWM0

for references in articles please use BRENDA:EC4.1.1.79
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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.79 sulfopyruvate decarboxylase
IUBMB Comments
Requires thiamine diphosphate. Does not decarboxylate pyruvate or phosphonopyruvate. The enzyme appears to be oxygen-sensitive.
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Select one or more organisms in this record: ?
This record set is specific for:
Methanococcus maripaludis
UNIPROT: Q6LWM0
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Word Map
  • 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
The taxonomic range for the selected organisms is: Methanococcus maripaludis
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
comde, sulfopyruvate decarboxylase, 3-sulfopyruvate decarboxylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylase, sulfopyruvate
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sulfopyruvate decarboxylase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
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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.
CAS REGISTRY NUMBER
COMMENTARY hide
303155-97-7
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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-sulfopyruvate
2-sulfoacetaldehyde + CO2
show the reaction diagram
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-sulfopyruvate
2-sulfoacetaldehyde + CO2
show the reaction diagram
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-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
the enzyme plays an important role in coenzyme M biosynthesis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team