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Information on EC 4.1.1.50 - adenosylmethionine decarboxylase and Organism(s) Trypanosoma cruzi and UniProt Accession O76240

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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:
Trypanosoma cruzi
UNIPROT: O76240
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The taxonomic range for the selected organisms is: Trypanosoma cruzi
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
AdoMet decarboxylase
-
-
AdoMetDC
AMDC
-
-
-
-
S-Adenosyl-L-methionine decarboxylase
-
-
-
-
S-Adenosylmethionine decarboxylase
SAM decarboxylase
-
-
-
-
SAMDC
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine = S-adenosyl 3-(methylsulfanyl)propylamine + CO2
show the reaction diagram
kinetic analysis, inverse solvent isotope effect
-
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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
(2E)-2-[(2E)-2-[(diaminomethyl)hydrazono]-1-methylethylidene]hydrazinecarboximidamide
-
i.e. MGBG, active site inhibitor
(2E)-2-[4-[amino(imino)methyl]-2,3-dihydro-1H-inden-1-ylidene]hydrazinecarboximidamide
-
i.e. CGP 48664A, stimulation in the range of 0.1-10 microM, inhibition at higher comcentration. Binds to the putrescine binding site and to the active site
(S)-(5'-deoxy-5'-adenosyl)methylthioethylhydroxylamine
-
-
3-[(E)-[(2E)-[amino[(2E)-2-[3-[amino(imino)methyl]benzylidene]hydrazino]methylene]hydrazono]methyl]benzenecarboximidamide
-
i.e. CGP40215, active site inhibitor
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
spermidine
-
weak
spermine
-
strong
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cadaverine
increase of kcat up to 9fold
putrescine
increase of kcat up to 9fold
(2E)-2-[4-[amino(imino)methyl]-2,3-dihydro-1H-inden-1-ylidene]hydrazinecarboximidamide
-
stimulation in the range of 0.1-10 microM, inhibition at higher comcentration
pi' subunit
-
-
-
putrescine
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05
S-adenosyl-L-methionine
pH 8.0, 37°C, without putrescine
0.21
S-adenosyl-L-methionine
-
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6
S-adenosyl-methionine
-
in presence of putrescine
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.2 - 104
3-[(E)-[(2E)-[amino[(2E)-2-[3-[amino(imino)methyl]benzylidene]hydrazino]methylene]hydrazono]methyl]benzenecarboximidamide
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DCAMC_TRYCR
370
0
42154
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10000
2 * 32000, alpha, + 2 * 10000, beta, SDS-PAGE, subunits derived from autocatalytically cleaved protein
32000
2 * 32000, alpha, + 2 * 10000, beta, SDS-PAGE, subunits derived from autocatalytically cleaved protein
70000
gel filtration
42000
-
estimated from amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
2 * 32000, alpha, + 2 * 10000, beta, SDS-PAGE, subunits derived from autocatalytically cleaved protein
heterodimer
-
x-ray crystallography
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
autocatalytic processing of 42000 Da protein to 32000 + 10000 Da
proteolytic modification
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C82A
-
drastically reduced single turnover rate, no solvent isotope effect, C82 may function as a general aci/base in catalysis
D174A
-
protein is fully processed, but no putrescine binding or activation
D174V
-
residue in putrescine binding site, no activation by putrescine
E15A
-
protein is fully processed, no influence on putrescine binding
E256A
-
protein is fully processed, no influence on putrescine binding
F285H
-
residue in putrescine binding site, enhanced catalytic activity
I80K/S178E
-
protein is fully processed, no influence on putrescine binding
R13L
-
no processing of enzyme
S111R
-
residue in putrescine binding site, reduced catalytic activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme, expressed in Escherichia coli
recombinant enzyme
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
AdoMetDC is negatively regulated by spermidine and spermine
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Persson, K.; Aslund, L.; Grahn, B.; Hanke, J.; Heby, O.
Trypanosoma cruzi has not lost its S-adenosylmethionine decarboxylase: characterization of the gene and the encoded enzyme
Biochem. J.
333
527-537
1998
Trypanosoma cruzi
Manually annotated by BRENDA team
Kinch, L.N.; Phillips, M.A.
Single-turnover kinetic analysis of Trypanosoma cruzi S-adenosylmethionine decarboxylase
Biochemistry
39
3336-3343
2000
Trypanosoma cruzi
Manually annotated by BRENDA team
Clyne, T.; Kinch, L.N.; Phillips, M.A.
Putrescine activation of Trypanosoma cruzi S-adenosylmethionine decarboxylase
Biochemistry
41
13207-13216
2002
Trypanosoma cruzi
Manually annotated by BRENDA team
Kinch, L.N.; Scott, J.R.; Ullman, B.; Phillips, M.A.
Cloning and kinetic characterization of the Trypanosoma cruzi S-adenosylmethionine decarboxylase
Mol. Biochem. Parasitol.
101
1-11
1999
Trypanosoma cruzi (O76240), Trypanosoma cruzi
Manually annotated by BRENDA team
Beswick, T.C.; Willert, E.K.; Phillips, M.A.
Mechanisms of allosteric regulation of Trypanosoma cruzi S-adenosylmethionine decarboxylase
Biochemistry
45
7797-7807
2006
Trypanosoma cruzi
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