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Information on EC 4.1.1.79 - sulfopyruvate decarboxylase and Organism(s) Methanocaldococcus jannaschii and UniProt Accession P58415

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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This record set is specific for:
Methanocaldococcus jannaschii
UNIPROT: P58415
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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: Methanocaldococcus jannaschii
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
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
-
-
-
-
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
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
fourth step in biosynthesis of coenzyme M
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
thiamine diphosphate
required
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
subunitb alpha, P58416, subunit beta
SwissProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
17000
alpha6beta6, 6 * 17000 + 6 * 23000, SDS-PAGE
23000
alpha6beta6, 6 * 17000 + 6 * 23000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dodecamer
alpha6beta6, 6 * 17000 + 6 * 23000, SDS-PAGE
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
inactivation by oxygen at 80°C and reactivation by reduction with dithionite
644226
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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
Manually annotated by BRENDA team