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Information on EC 4.1.1.50 - adenosylmethionine decarboxylase and Organism(s) Homo sapiens and UniProt Accession P17707

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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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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: P17707
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Word Map
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The taxonomic range for the selected organisms is: Homo sapiens
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
-
-
-
-
SAM-DC
-
-
SAMDC
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine = S-adenosyl 3-(methylsulfanyl)propylamine + CO2
show the reaction diagram
mechanism
-
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
S-adenosyl-L-methionine
S-adenosyl 3-(methylthio)propylamine + CO2
show the reaction diagram
-
-
-
-
?
additional information
?
-
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
?
show the reaction diagram
additional information
?
-
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(1E)-1-(9-bromo-3-phenanthryl)ethanone oxime
75% inhibition at 0.1 mM
1,3-di-9H-fluoren-2-ylthiourea
69% inhibition at 0.1 mM
1-(4-hydroxy-5-isopropyl-2-methylphenyl)-3-(1-naphthyl)urea
61% inhibition at 0.1 mM
2'-[(9H-fluoren-2-ylamino)carbonyl]biphenyl-2-carboxylate
74% inhibition at 0.1 mM
2-[2-(diethylammonio)ethyl]-9-hydroxy-5,11-dimethyl-6H-pyrido[4,3-b]carbazol-2-ium
67% inhibition at 0.1 mM
4-amidinoindan-1-one-2'-amidinohydrazone
4-[(E)-2-(2-chlorophenyl)vinyl]quinolinium
67% inhibition at 0.1 mM
5'-deoxy 5'-[(2-guanidinoethyl)methylamino]adenosine
less than 5% inhibition at 0.1 mM
5'-deoxy-5'-(2-methylaminoethylamino)adenosine
less than 5% inhibition at 0.1 mM
5'-deoxy-5'-(3-methylaminopropylamino)-8-phenyladenosine sulfate
less than 5% inhibition at 0.1 mM
5'-deoxy-5'-(dimethyl-sulfonio)adenosine
-
5'-deoxy-5'-(N,N-dimethylamino)-8-methyladenosine
-
5'-deoxy-5'-(N,N-dimethylamino)adenosine
-
5'-deoxy-5'-(N-dimethyl)amino-8-methyl adenosine
-
5'-deoxy-5'-(N-dimethyl)amino-8-methyladenosine
-
5'-deoxy-5'-dimethylsulfonio-8-methyladenosine chloride
-
5'-deoxy-5'-dimethylsulfonioadenosine chloride
-
5'-deoxy-5'-dimethylthioadenosine
-
5'-deoxy-5'-[(2-hydrazinocarbonylethyl)methylamino]-8-methyladenosine sulfate
-
5'-deoxy-5'-[(2-hydrazinocarbonylethyl)methylamino]-adenosine sulfate
-
5'-deoxy-5'-[(2-hydrazinoethyl)methylamino]adenosine
-
5'-deoxy-5'-[(2-hydroxyamidinoethyl)methylamino]adenosine
-
5'-Deoxy-5'-[(3-hydrazinopropyl)methylamino]adenosine
-
5'-deoxy-5'-[(hydrazinocarbonylmethyl)methylamino]-8-methyladenosine
-
5'-deoxy-5'-[N-methyl-N-(3-hydrazino-propyl)amino]adenosine
-
5'-deoxy-5'-[N-methyl-N-(3-hydrazinopropyl)amino]adenosine
-
5'-deoxy-5'-[N-methyl-N-[(2-aminooxy)-ethyl]amino]adenosine
-
5'-deoxy-5'-[N-methyl-N-[(2-aminooxy)ethyl]amino]adenosine
-
5'-deoxy-8-(methylamino)-5'-(3-methylaminopropylamino)adenosine sulfate
less than 5% inhibition at 0.1 mM
5'-deoxy-8-methyl-5'-(2-methylaminoethylamino)adenosine
less than 5% inhibition at 0.1 mM
5'-[(2-aminoethyl)methylamino]-5'-deoxy-8-methyladenosine
-
5'-[(2-aminoethyl)methylamino]-5'-deoxyadenosine
less than 5% inhibition at 0.1 mM
5'-[(2-aminooxyethyl)methylamino]-5'-deoxy-8-(methylamino)adenosine sulfate
-
5'-[(2-aminooxyethyl)methylamino]-5'-deoxy-8-methyladenosine sulfate
-
5'-[(2-aminooxyethyl)methylamino]-5'-deoxy-8-phenyladenosine sulfate
less than 5% inhibition at 0.1 mM
5'-[(2-aminooxyethyl)methylamino]-5'-deoxyadenosine
-
5'-[(2-carboxamidoethyl)methyamino]-5'-deoxy-8-ethyladenosine sulfate
-
5'-[(2-carboxamidoethyl)methylamino]-5'-deoxy-8-methyladenosine sulfate
-
5'-[(2-carboxamidoethyl)methylamino]-5'-deoxyadenosine sulfate
-
5'-[(3-aminopropyl)methylamino]-5'-deoxy-8-(methylamino)adenosine sulfate
-
5'-[(3-aminopropyl)methylamino]-5'-deoxy-8-ethyladenosine sulfate
-
5'-[(3-aminopropyl)methylamino]-5'-deoxy-8-methyladenosine sulfate
-
5'-[(3-aminopropyl)methylamino]-5'-deoxy-8-phenyladenosine sulfate
less than 5% inhibition at 0.1 mM
5'-[(3-aminopropyl)methylamino]-5'-deoxyadenosine sulfate
-
5'-[(4-aminooxybutyl)methylamino]-5'-deoxy-8-(methylamino)adenosine sulfate
-
5'-[(4-aminooxybutyl)methylamino]-5'-deoxy-8-ethyladenosine sulfate
-
5'-[(4-aminooxybutyl)methylamino]-5'-deoxy-8-methyladenosine sulfate
-
5'-[(4-aminooxybutyl)methylamino]-5'-deoxy-8-oxoadenosine sulfate
-
5'-[(4-aminooxybutyl)methylamino]-5'-deoxy-8-phenyladenosine sulfate
less than 5% inhibition at 0.1 mM
5'-[(4-aminooxybutyl)methylamino]-5'-deoxyadenosine sulfate
-
5'-[(carboxamidomethyl)methylamino]-5'-deoxy-8-methyladenosine sulfate
less than 5% inhibition at 0.1 mM
5'-[[(Z)-4-amino-2-butenyl]methylamino]-5'-deoxyadenosine
-
9-amino-6-[(E)-(2,6-diaminopyridin-3-yl)diazenyl]-2-ethoxyacridinium
64% inhibition at 0.1 mM
9-hydroxy-5,11-dimethyl-2-(2-piperidinium-1-ylethyl)-6H-pyrido[4,3-b]carbazol-2-ium
69% inhibition at 0.1 mM
CGP48664A
methylglyoxal bis(guanylhydrazone)
methylglyoxalbis(guanylhydrazone)
-
(R)-alpha-methylspermine
-
-
(R,R)-alpha,omega-bismethylspermine
-
best suppressor of AdoMetDC activity
(S)-(5'-deoxy-5'-adenosyl)methylthioethylhydroxylamine
-
-
(S)-alpha-methylspermidine
-
-
2-amino-3-[(E)-(2-fluorophenyl)diazenyl]-4,5,6,7-tetrahydro-8H-cyclopenta[d]pyrazolo[1,5-a]pyrimidin-8-one
-
compound shows comparable inhibitory effects as methylglyoxal bis(guanylhydrazone)
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
5'-{[(Z)-4-Amino-2-butenyl]methylamino}-5'-deoxyadenosine
BW-1
-
85% inhibition at 2 mM, in presence of 2 mM putrescine, degree of inhibition depends on actual putrescine abundance
CGP 48664
-
specific inhibitor of AdoMetDC
Genz-643990
-
-
Genz-644043
-
-
Genz-644053
-
-
Genz-644131
iodoacetic acid
-
-
MDL 27695
-
44% inhibition at 2 mM, in presence of 2 mM putrescine
MDL73811
-
irreversible inhibitor
methylglyoxal bis(guanylhydrazone)
-
-
NaCl
-
enzyme from infected cells is unaffected up to 0.8 M, 50% inhibition of the enzyme from uninfected cells at 0.45 M
PMW-2000-11-13-1
-
52% inhibition at 2 mM, in presence of 2 mM putrescine
RHW-17-69-75
-
45% inhibition at 2 mM, in presence of 2 mM putrescine
SAM486A
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
putrescine
-
difluoromethylornithine
-
5 mM causes an induction of the enzyme activity
putrescine
pyruvate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0031 - 0.245
S-adenosyl-L-methionine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
20
S-adenosyl-L-methionine
-
pH not specified in the publication, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.45
NaCl
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0006
5'-deoxy-5'-(N,N-dimethylamino)-8-methyladenosine
Homo sapiens
-
0.009
5'-deoxy-5'-(N,N-dimethylamino)adenosine
Homo sapiens
-
0.003
5'-deoxy-5'-dimethylsulfonio-8-methyladenosine chloride
Homo sapiens
-
0.015
5'-deoxy-5'-dimethylsulfonioadenosine chloride
Homo sapiens
-
0.00017
5'-deoxy-5'-[(2-hydrazinocarbonylethyl)methylamino]-8-methyladenosine
Homo sapiens
-
0.0015
5'-deoxy-5'-[(2-hydrazinocarbonylethyl)methylamino]-adenosine sulfate
Homo sapiens
-
0.157
5'-deoxy-5'-[(2-hydroxyamidinoethyl)methylamino]adenosine
Homo sapiens
-
0.031
5'-deoxy-5'-[(hydrazinocarbonylmethyl)methylamino]-8-methyladenosine
Homo sapiens
-
0.088
5'-[(2-aminoethyl)methylamino]-5'-deoxy-8-methyladenosine
Homo sapiens
-
0.000086
5'-[(2-aminooxyethyl)methylamino]-5'-deoxy-8-(methylamino)adenosine sulfate
Homo sapiens
-
0.000007
5'-[(2-aminooxyethyl)methylamino]-5'-deoxy-8-methyladenosine sulfate
Homo sapiens
-
0.000055
5'-[(2-aminooxyethyl)methylamino]-5'-deoxyadenosine
Homo sapiens
-
0.004
5'-[(2-carboxamidoethyl)methyamino]-5'-deoxy-8-ethyladenosine sulfate
Homo sapiens
-
0.0004
5'-[(2-carboxamidoethyl)methylamino]-5'-deoxy-8-methyladenosine sulfate
Homo sapiens
-
0.007
5'-[(2-carboxamidoethyl)methylamino]-5'-deoxyadenosine sulfate
Homo sapiens
-
0.44
5'-[(3-aminopropyl)methylamino]-5'-deoxy-8-(methylamino)adenosine sulfate
Homo sapiens
-
0.42
5'-[(3-aminopropyl)methylamino]-5'-deoxy-8-ethyladenosine sulfate
Homo sapiens
-
0.07
5'-[(3-aminopropyl)methylamino]-5'-deoxy-8-methyladenosine sulfate
Homo sapiens
-
0.5
5'-[(3-aminopropyl)methylamino]-5'-deoxyadenosine sulfate
Homo sapiens
-
0.000049
5'-[(4-aminooxybutyl)methylamino]-5'-deoxy-8-(methylamino)adenosine sulfate
Homo sapiens
-
0.000015
5'-[(4-aminooxybutyl)methylamino]-5'-deoxy-8-ethyladenosine sulfate
Homo sapiens
-
0.000005
5'-[(4-aminooxybutyl)methylamino]-5'-deoxy-8-methyladenosine sulfate
Homo sapiens
-
0.000011
5'-[(4-aminooxybutyl)methylamino]-5'-deoxy-8-oxoadenosine sulfate
Homo sapiens
-
0.000018
5'-[(4-aminooxybutyl)methylamino]-5'-deoxyadenosine sulfate
Homo sapiens
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.992
-
-
121
-
plus 2 mM YZ-33-050C
148
-
plus 2 mM 33-003
152
-
plus 2 mM PMW-2000-11-13-5
176
-
plus 2 mM YZ-33-046
180
-
plus 2 mM 1,15-diamono-4,12-diazapentadecane
410
-
plus 2 mM putrescine
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2 - 7.4
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
from salivary gland, culture on fibronectin-, collagen I gel-, and Matrigel-coated substrates for 12-24 h upregulates S-adenosylmethionine decarboxylase mRNA expression and enzyme activity compared to cells cultured on non-precoated substrates
Manually annotated by BRENDA team
-
MRC5, diploid, embryonic, uninfected or infected with cytomegalovirus
Manually annotated by BRENDA team
-
transfected MCF-7
Manually annotated by BRENDA team
-
epithelial cell, culture on fibronectin-, collagen I gel-, and Matrigel-coated substrates for 12-24 h upregulates S-adenosylmethionine decarboxylase mRNA expression and enzyme activity compared to cells cultured on non-precoated substrates
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
overexpression of S-adenosylmethionine decarboxylase in rodent fibroblasts leads to aggressive transformants (Amdc-s cells) that have high invasive capacity in nude mice, invading rapidly from the subcutaneous injection site into the peritoneal cavity and its organs. Amdc-s-induced tumors show chaotic neovascularization, with abundant pleomorphic vessel-like structures that have noncontiguous or totally missing laminin (basement membrane) and CD31 (endothelial cell) immunoreactivity
physiological function
-
S-adenosylmethionine decarboxylase is a key enzyme in the biosynthesis of polyamines essential for cell proliferation
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DCAM_HUMAN
334
0
38340
Swiss-Prot
other Location (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30600
-
x * 39600, proenzyme, x * 30600, alpha, + x * 8900, beta, SDS-PAGE
32000
-
x * 32000, SDS-PAGE of recombinant alpha subunit, including His-tag
38000
-
estimated from amino acid sequence
39600
-
x * 39600, proenzyme, x * 30600, alpha, + x * 8900, beta, SDS-PAGE
8900
-
x * 39600, proenzyme, x * 30600, alpha, + x * 8900, beta, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
x-ray crystallography
heterodimer
-
x-ray crystallography
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
-
proenzyme of 39600 Da is cleaved to alpha subunit, 30600 Da, and beta subunit, 8900 Da
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
AdoMetDC F223A mutant complexed with S-adenosylmethionine and the wild type protein complexed with several substituted inhibitors, hanging drop vapor diffusion method, at 22°C in 13-16% PEG 8000, 100 mM Tris, pH 8.0-9.0, and 10 mM dithiothreitol
cocrystallized with 5'-deoxy-5'-dimethylthioadenosine and 5'-deoxy-5'-(N-dimethyl)amino-8-methyladenosine, hanging drop vapor diffusion method, at 22°C in 13-16% (w/v) polyethylene glycol 8000, 100 mM tris(hydroxymethyl)aminomethane (pH 8.0-9.0), and 10 mM dithiothreitol
in complex with different inhibitors and with a substrate analogue
docking of inhibitor 2-amino-3-[(E)-(2-fluorophenyl)diazenyl]-4,5,6,7-tetrahydro-8H-cyclopenta[d]pyrazolo[1,5-a]pyrimidin-8-one, compound binds the enzyme with interactions similar to known inhibitors. The major interactions are the ring-ring stacking interactions with Phe7 and Phe223, the polar interactions with the side-chain or main-chain atoms of Leu65, Ser68, Glu67, Asn224, and Cys226
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C82A
the mutant shows decreased kcat compared to the wild type enzyme
H243A
the mutation traps the enzyme in the ester form
S68A
themutant lacks the hydroxyl group necessary for processing and traps the enzyme in a form similar to the proenzyme
C82A
-
reduced enzymic activity, no inhibition by iodoacetic acid
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
47
-
10 min, 50% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freezing inactivates
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, stable for up to 2 weeks
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
TALON metal affinity resin column chromatography
Talon metal affinity resin column chromatography and Sephadex G-75 gel filtration
large-scale
-
Ni2+-agarose column chromatography
-
recombinant alpha subunit
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) JM109 cells
expressed in Escherichia coli JM109 cells
expression in Escherichia coli
enzyme alpha subunit, expression in Escherichia coli
-
expressed in Amdc-s cells (NIH3T3 cells transfected with human AdoMetDC cDNA)
-
expressed in Escherichia coli
-
expression in Escherichia coli
-
expression in sense and antisense orientations in mouse NIH3T3 cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
AdoMetDC is negatively regulated by spermidine and spermine
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
development of a simple, economic, and non-radioactive spectrometric enzymatic assay, which can be adapted for experimental high-throughput screening of AdoMetDC inhibitors
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
White Tabor, C.; Tabor, H.
Methionine adenosyltransferase (S-adenosylmethionine synthetase) and S-adenosylmethionine decarboxylase
Adv. Enzymol. Relat. Areas Mol. Biol.
56
251-282
1984
Bos taurus, Saccharomyces cerevisiae, Escherichia coli, Homo sapiens, Lytechinus pictus, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Manni, A.; Badger, B.; Grove, R.; Kunselman, S.; Demers, L.
Isolation and characterization of human breast cancer cell overexpressing S-adenosylmethionine decarboxylase
Cancer Lett.
95
23-28
1995
Homo sapiens
Manually annotated by BRENDA team
Shantz, L.M.; Stanley, B.A.; Secrist III, J.A.; Pegg, A.E.
Purification of human S-adenosylmethionine decarboxylase expressed in Escherichia coli and use of this protein to investigate the mechanism of inhibition by the irreversible inhibitors, 5'-deoxy-5'-[(3-hydrazinopropyl)methylamino]adenosine and 5'-[[(Z)-4-amino-2-butenyl]methylamino]-5'-deoxyadenosine
Biochemistry
31
6848-6855
1992
Homo sapiens
Manually annotated by BRENDA team
Regenass, U.; Caravatti, G.; Mett, M.; Stanek, J.; Schneider, P.; Mueller, M.; Matter, A.; Vertino, P.; Porter, C.W.
New S-adenosylmethionine decarboxylase inhibitors with potent antitumor activity
Cancer Res.
52
4712-4718
1992
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Regenass, U.; Mett, H.; Stanek, J.; Mueller, M.; Kramer, D.; Porter, C.W.
CGP 48664, a new S-adenosylmethionine decarboxylase inhibitor with broad spectrum antiproliferative and antitumor activity
Cancer Res.
54
3210-3217
1994
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
White, E.L.; Arnett, G.; Secrist III, J.A.; Shannon, W.M.
Characterization of S-adenosylmethionine decarboxylase induced by human cytomegalovirus infection
Virus Res.
31
255-263
1994
Homo sapiens
Manually annotated by BRENDA team
Xiong, H.; Stanley, B.A.; Pegg, A.E.
Role of cysteine-82 in the catalytic mechanism of human S-adenosylmethionine decarboxylase
Biochemistry
38
2462-2470
1999
Homo sapiens
Manually annotated by BRENDA team
Tolbert, W.D.; Ekstrom, J.L.; Mathews, II; Secrist, J.A., 3rd; Kapoor, P.; Pegg, A.E.; Ealick, S.E.
The structural basis for substrate specificity and inhibition of human S-adenosylmethionine decarboxylase
Biochemistry
40
9484-9494
2001
Homo sapiens (P17707), Homo sapiens
Manually annotated by BRENDA team
Ndjonka, D.; Zou, Y.; Bi, X.; Woster, P.; Walter, R.D.; Luersen, K.
The activator-binding site of Onchocerca volvulus S-adenosylmethionine decarboxylase, a potential drug target
Biol. Chem.
384
1195-1201
2003
Homo sapiens, Onchocerca volvulus
Manually annotated by BRENDA team
Nummela, P.; Yin, M.; Kielosto, M.; Leaner, V.; Birrer, M.J.; Holtta, E.
Thymosin beta4 is a determinant of the transformed phenotype and invasiveness of S-adenosylmethionine decarboxylase-transfected fibroblasts
Cancer Res.
66
701-712
2006
Homo sapiens
Manually annotated by BRENDA team
Greco, A.; Calle, A.; Morfin, F.; Thouvenot, D.; Cayre, M.; Kindbeiter, K.; Martin, L.; Levillain, O.; Diaz, J.J.
S-adenosyl methionine decarboxylase activity is required for the outcome of herpes simplex virus type 1 infection and represents a new potential therapeutic target
FASEB J.
19
1128-1130
2005
Homo sapiens
Manually annotated by BRENDA team
Lam, K.; Zhang, L.; Bewick, M.; Lafrenie, R.M.
HSG cells differentiated by culture on extracellular matrix involves induction of S-adenosylmethione decarboxylase and ornithine decarboxylase
J. Cell. Physiol.
203
353-361
2005
Homo sapiens
Manually annotated by BRENDA team
Tian, H.; Liu, X.; Zhang, B.; Sun, Q.; Sun, D.
Adenovirus-mediated expression of both antisense ornithine decarboxylase and S-adenosylmethionine decarboxylase inhibits lung cancer cell growth
Acta Biochim. Biophys. Sin.
39
423-430
2007
Homo sapiens
Manually annotated by BRENDA team
Kim, J.S.; Kim, T.L.; Kim, K.C.; Choe, C.; Chung, H.W.; Cho, E.W.; Kim, I.G.
S-Adenosylmethionine decarboxylase partially regulates cell growth of HL-60 cells by controlling the intracellular ROS level: Early senescence and sensitization to gamma-radiation
Arch. Biochem. Biophys.
456
58-70
2006
Homo sapiens (P17707)
Manually annotated by BRENDA team
Gong, L.; Zhang, B.; Zhang, Y.; Hu, H.; Zhao, Z.; Liu, X.
Cloning, expression and purification of human S-adenosylmethionine decarboxylase gene alpha subunit
Chin. J. Physiol.
50
29-33
2007
Homo sapiens
Manually annotated by BRENDA team
Gong, L.; Jiang, C.; Zhang, B.; Hu, H.; Wang, W.; Liu, X.
Adenovirus-mediated expression of both antisense ornithine decarboxylase and S-adenosylmethionine decarboxylase induces G1 arrest in HT-29 cells
J. Biochem. Mol. Biol.
39
730-736
2006
Homo sapiens
Manually annotated by BRENDA team
Brooks, W.H.; McCloskey, D.E.; Daniel, K.G.; Ealick, S.E.; Secrist, J.A.; Waud, W.R.; Pegg, A.E.; Guida, W.C.
In silico chemical library screening and experimental validation of a novel 9-aminoacridine based lead-inhibitor of human S-adenosylmethionine decarboxylase
J. Chem. Inf. Model.
47
1897-1905
2007
Homo sapiens (P17707), Homo sapiens
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
Barker, R.H.; Liu, H.; Hirth, B.; Celatka, C.A.; Fitzpatrick, R.; Xiang, Y.; Willert, E.K.; Phillips, M.A.; Kaiser, M.; Bacchi, C.J.; Rodriguez, A.; Yarlett, N.; Klinger, J.D.; Sybertz, E.
Novel S-adenosylmethionine decarboxylase inhibitors for the treatment of human African trypanosomiasis
Antimicrob. Agents Chemother.
53
2052-2058
2009
Homo sapiens, Trypanosoma brucei
Manually annotated by BRENDA team
Hyvoenen, M.T.; Howard, M.T.; Anderson, C.B.; Grigorenko, N.; Khomutov, A.R.; Vepsaelaeinen, J.; Alhonen, L.; Jaenne, J.; Keinaenen, T.A.
Divergent regulation of the key enzymes of polyamine metabolism by chiral alpha-methylated polyamine analogues
Biochem. J.
422
321-328
2009
Homo sapiens
Manually annotated by BRENDA team
Bale, S.; Brooks, W.; Hanes, J.W.; Mahesan, A.M.; Guida, W.C.; Ealick, S.E.
Role of the sulfonium center in determining the ligand specificity of human S-adenosylmethionine decarboxylase
Biochemistry
48
6423-6430
2009
Homo sapiens (P17707), Homo sapiens
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
McCloskey, D.E.; Bale, S.; Secrist, J.A.; Tiwari, A.; Moss, T.H.; Valiyaveettil, J.; Brooks, W.H.; Guida, W.C.; Pegg, A.E.; Ealick, S.E.
New insights into the design of inhibitors of human S-adenosylmethionine decarboxylase: Studies of adenine C8 substitution in structural analogues of S-adenosylmethionine
J. Med. Chem.
52
1388-1407
2009
Homo sapiens (P17707), Homo sapiens
Manually annotated by BRENDA team
Koomoa, D.L.; Borsics, T.; Feith, D.J.; Coleman, C.C.; Wallick, C.J.; Gamper, I.; Pegg, A.E.; Bachmann, A.S.
Inhibition of S-adenosylmethionine decarboxylase by inhibitor SAM486A connects polyamine metabolism with p53-Mdm2-Akt/protein kinase B regulation and apoptosis in neuroblastoma
Mol. Cancer Ther.
8
2067-2075
2009
Homo sapiens
Manually annotated by BRENDA team
Paasinen-Sohns, A.; Kaeaeriaeinen, E.; Yin, M.; Jaervinen, K.; Nummela, P.; Hoelttae, E.
Chaotic neovascularization induced by aggressive fibrosarcoma cells overexpressing S-adenosylmethionine decarboxylase
Int. J. Biochem. Cell Biol.
43
441-454
2011
Homo sapiens
Manually annotated by BRENDA team
Liao, C.; Wang, Y.; Tan, X.; Sun, L.; Liu, S.
Discovery of novel inhibitors of human S-adenosylmethionine decarboxylase based on in silico high-throughput screening and a non-radioactive enzymatic assay
Sci. Rep.
5
10754
2015
Homo sapiens
Manually annotated by BRENDA team