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Information on EC 4.1.1.50 - adenosylmethionine decarboxylase and Organism(s) Saccharolobus solfataricus and UniProt Accession Q9UWY8

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.50 adenosylmethionine decarboxylase
IUBMB Comments
The Escherichia coli enzyme contains a pyruvoyl group.
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This record set is specific for:
Saccharolobus solfataricus
UNIPROT: Q9UWY8
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Word Map
The taxonomic range for the selected organisms is: Saccharolobus solfataricus
The enzyme appears in selected viruses and cellular organisms
Synonyms
s-adenosylmethionine decarboxylase, adometdc, samdc, s-adenosyl-l-methionine decarboxylase, adenosylmethionine decarboxylase, adomet decarboxylase, s-adenosyl methionine decarboxylase, sam-dc, sam decarboxylase, pfadometdc, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
AdoMetDC
-
-
-
-
AMDC
-
-
-
-
S-Adenosyl-L-methionine decarboxylase
-
-
-
-
S-Adenosylmethionine decarboxylase
-
-
-
-
SAM decarboxylase
-
-
-
-
SAMDC
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine carboxy-lyase [(5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium-salt-forming]
The Escherichia coli enzyme contains a pyruvoyl group.
CAS REGISTRY NUMBER
COMMENTARY hide
9036-20-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine
(5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt + CO2
show the reaction diagram
S-adenosyl-L-methionine
(5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt + CO2
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine
?
show the reaction diagram
-
major regulatory enzyme in polyamine biosynthesis
-
-
?
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
S-adenosyl-L-methionine
(5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt + CO2
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine
?
show the reaction diagram
-
major regulatory enzyme in polyamine biosynthesis
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
no requirement for a divalent metal ion
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
methylglyoxal bis(guanylhydrazone)
-
competitive
NaCNBH3
-
in presence of substrate or product
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
putrescine
-
no requirement
pyruvate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.96
S-adenosylmethionine
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.3
S-adenosyl-L-methionine
pH 8.0, 70°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50 - 90
-
50°C: about 45% of maximal activity, 90°C: about 60% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16602
2 * 16602, electrospray ionization mass spectrometry
16680
2 * 16680, calculated from sequence
33000
His10-tagged enzyme, gel filtration
32000
-
1 * 32000, SDS-PAGE
36000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
monomer
-
1 * 32000, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
-
1 h, 80% loss of activity
50
-
16 h, stable
70
-
16h, 20% loss of activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cacciapuoti, G.; Porcelli, M.; de Rosa, M.; Gambacorta, A.; Bertoldo, C.; Zappia, V.
S-Adenosylmethionine decarboxylase from the thermophilic archaebacterium Sulfolobus solfataricus
Eur. J. Biochem.
199
395-400
1991
Saccharolobus solfataricus
Manually annotated by BRENDA team
Giles, T.N.; Graham, D.E.
Crenarchaeal arginine decarboxylase evolved from an S-adenosylmethionine decarboxylase enzyme
J. Biol. Chem.
283
25829-25838
2008
Saccharolobus solfataricus (Q9UWY8), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q9UWY8)
Manually annotated by BRENDA team