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Information on EC 4.1.1.50 - adenosylmethionine decarboxylase and Organism(s) Thermotoga maritima and UniProt Accession Q9WZC3

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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:
Thermotoga maritima
UNIPROT: Q9WZC3
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Word Map
The taxonomic range for the selected organisms is: Thermotoga maritima
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
S-Adenosylmethionine decarboxylase
-
AdoMet decarboxylase
-
-
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
-
-
-
-
?
additional information
?
-
-
critical regulatory enzyme of the polyamine biosynthetic pathway
-
-
?
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
additional information
?
-
-
critical regulatory enzyme of the polyamine biosynthetic pathway
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
thiamine diphosphate
-
pyridoxal 5'-phosphate
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
does not require Mg2+ for activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-amidinoindan-1-one-2'-amidinohydrazone
-
5'-deoxy-5'-(dimethyl-sulfonio)adenosine
-
5'-deoxy-5'-(N-dimethyl)amino-8-methyl adenosine
-
5'-deoxy-5'-[N-methyl-N-(3-hydrazino-propyl)amino]adenosine
-
5'-deoxy-5'-[N-methyl-N-[(2-aminooxy)-ethyl]amino]adenosine
-
CGP48664A
i.e. 4-amidinoindan-1-one-2'-amidinohydrazone
methylglyoxalbis(guanylhydrazone)
-
(S)-(5'-deoxy-5'-adenosyl)methylthioethylhydroxylamine
-
-
5'-deoxy-5'-dimethylsulfonio-8-methyladenosine
-
-
5'-deoxy-5'-[(2-aminooxyethyl)methylamino]adenosine
-
-
5'-Deoxy-5'-[(3-hydrazinopropyl)methylamino]adenosine
-
-
5'-[[(Z)-4-amino-2-butenyl]methylamino]-5'-deoxyadenosine
-
MDL 73811
Genz-644131
-
i.e. 5'-[[(Z)-4-amino-2-butenyl]methylamino]-5'-deoxy-8-methyladenosine
methylglyoxal bis(guanylhydrazone)
-
-
SAM486A
-
previously described as CGP4864A, i.e. 4-amidinoindan-1-one-2'-amidinohydrazone
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.08
S-adenosyl-L-methionine
at pH 6.8 and 65°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1
S-adenosyl-L-methionine
at pH 6.8 and 65°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
12.5
S-adenosyl-L-methionine
at pH 6.8 and 65°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
S-adenosylmethionine decarboxylase is a critical pyruvoyl-dependent enzyme in the polyamine-biosynthetic pathway
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15000
-
estimated from amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
x-ray crystallography
heterodimer
-
x-ray crystallography
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complexes with S-adenosylmethionine methyl ester and 5'-deoxy-5'-dimethylthioadenosine, hanging drop vapor diffusion method, using 2.4-2.8 M ammonium formate and 100 mM HEPES pH 8.0
hanging drop vapour diffusion method, structures of the wild-type proenzyme and the S63A mutant at 1.55 A and 1.7 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C83A
-
mutant proenzyme is cleaved more rapidly than the wild-type enzyme
H68A
-
mutant proenzyme is cleaved much more slowly than the wild-type enzyme
S55A
-
mutant proenzyme is cleaved more rapidly than the wild-type enzyme
S63A
-
the mutation traps the enzyme in the proenzyme form
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography, gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli B834(DE3) cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
AdoMetDC is negatively regulated by spermidine and spermine
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Toms, A.V.; Kinsland, C.; McCloskey, D.E.; Pegg, A.E.; Ealick, S.E.
Evolutionary links as revealed by the structure of Thermotoga maritima S-adenosylmethionine decarboxylase
J. Biol. Chem.
279
33837-33846
2004
Thermotoga maritima
Manually annotated by BRENDA team
Bale, S.; Baba, K.; McCloskey, D.E.; Pegg, A.E.; Ealick, S.E.
Complexes of Thermotoga maritima S-adenosylmethionine decarboxylase provide insights into substrate specificity
Acta Crystallogr. Sect. D
66
181-189
2010
Thermotoga maritima (Q9WZC3), Thermotoga maritima
Manually annotated by BRENDA team
Bale, S.; Ealick, S.E.
Structural biology of S-adenosylmethionine decarboxylase
Amino Acids
38
451-460
2010
Trypanosoma brucei, Aquifex aeolicus (O66615), Aquifex aeolicus, Homo sapiens (P17707), Homo sapiens, Solanum tuberosum (Q04694), Solanum tuberosum, Thermotoga maritima (Q9WZC3), Thermotoga maritima
Manually annotated by BRENDA team
Pegg, A.E.
S-Adenosylmethionine decarboxylase
Essays Biochem.
46
25-45
2009
Bacillus subtilis, Saccharomyces cerevisiae, Catharanthus roseus, Clostridium acetobutylicum, Escherichia coli, Homo sapiens, Methanocaldococcus jannaschii, Solanum tuberosum, Thermotoga maritima, Trypanosoma brucei, Trypanosoma cruzi
Manually annotated by BRENDA team