Information on EC 4.1.1.50 - adenosylmethionine decarboxylase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY
4.1.1.50
-
RECOMMENDED NAME
GeneOntology No.
adenosylmethionine decarboxylase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine = S-adenosyl 3-(methylthio)propylamine + CO2
show the reaction diagram
-
-
-
-
S-adenosyl-L-methionine = S-adenosyl 3-(methylthio)propylamine + CO2
show the reaction diagram
mechanism
-
S-adenosyl-L-methionine = S-adenosyl 3-(methylthio)propylamine + CO2
show the reaction diagram
kinetic analysis, inverse solvent isotope effect
-
S-adenosyl-L-methionine = S-adenosyl 3-(methylthio)propylamine + CO2
show the reaction diagram
kinetics, mechanism
-
S-adenosyl-L-methionine = S-adenosyl 3-(methylthio)propylamine + CO2
show the reaction diagram
allosteric metal ion activation
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
-
-
-
-
decarboxylation
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Arginine and proline metabolism
-
-
Cysteine and methionine metabolism
-
-
Metabolic pathways
-
-
polyamine pathway
-
-
spermidine biosynthesis I
-
-
spermidine biosynthesis III
-
-
spermine biosynthesis
-
-
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.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ado-MetDC
-
-
Ado-MetDC
-
-
-
AdoMetDC
-
-
-
-
AdoMetDC
-
-
AdoMetDC
P17707
-
AdoMetDC
Q25264
-
AdoMetDC
-
-
AdoMetDC
Q9UWY8
-
AdoMetDC
Q9UWY8
-
-
AdoMetDC
Q9WZC3
-
AdoMetDC
Trypanosoma brucei brucei Lab 110 EATRO
-
-
-
AdoMetDC
-
-
AdoMetDC/ODC
-
bifunctional enzyme
AdoMetDC/ODC
-
ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (AdoMetDC) form a single bifunctional protein in Plasmodium falciparum
AMDC
-
-
-
-
BjSAMDC1
Q42613
-
BjSAMDC2
O49972
-
BjSAMDC3
Q9SDM8
-
BjSAMDC4
Q6QJ69
-
MdSAMDC1
Q852S9
-
MdSAMDC2
Q852S8
-
OsSAMDC
-
-
PfAdoMetDC
-
-
protein SSO0585
Q9UWY8
-
protein SSO0585
Q9UWY8
-
-
S-adenosyl methionine decarboxylase
-
-
S-adenosyl methionine decarboxylase
D2K8S5
-
S-Adenosyl-L-methionine decarboxylase
-
-
-
-
S-Adenosyl-L-methionine decarboxylase
-
-
S-Adenosyl-L-methionine decarboxylase
-
-
S-Adenosyl-L-methionine decarboxylase
-
-
S-Adenosyl-L-methionine decarboxylase
Q841K9
-
S-adenosyl-methionine-decarboxylase
-
-
S-adenosyl-methionine-decarboxylase
-
-
-
S-adenosylmethionine decarboxy-lase/ornithine decarboxylase
-
bifunctional enzyme
S-Adenosylmethionine decarboxylase
-
-
-
-
S-Adenosylmethionine decarboxylase
-
-
S-Adenosylmethionine decarboxylase
-
-
S-Adenosylmethionine decarboxylase
-
-
S-Adenosylmethionine decarboxylase
-
-
S-Adenosylmethionine decarboxylase
-
-
S-Adenosylmethionine decarboxylase
Q96555
-
S-Adenosylmethionine decarboxylase
-
-
S-Adenosylmethionine decarboxylase
-
-
S-Adenosylmethionine decarboxylase
P17707
-
S-Adenosylmethionine decarboxylase
-
-
S-Adenosylmethionine decarboxylase
-
-
S-Adenosylmethionine decarboxylase
-
-
S-Adenosylmethionine decarboxylase
Q0JC10
-
S-Adenosylmethionine decarboxylase
-
-
S-Adenosylmethionine decarboxylase
-
-
S-Adenosylmethionine decarboxylase
-
-
S-Adenosylmethionine decarboxylase
-
-
S-Adenosylmethionine decarboxylase
-
-
S-Adenosylmethionine decarboxylase
Q9WZC3
-
S-Adenosylmethionine decarboxylase
-
-
S-Adenosylmethionine decarboxylase
-
-
S-Adenosylmethionine decarboxylase
Trypanosoma brucei brucei Lab 110 EATRO
-
-
-
S-Adenosylmethionine decarboxylase
-
-
S-Adenosylmethionine decarboxylase
-
-
S-Adenosylmethionine decarboxylase
-
-
S-Adenosylmethionine decarboxylase
-
-
S-adenosylmethionine decarboxylase 1
Q42613
-
S-adenosylmethionine decarboxylase 2
O49972
-
S-adenosylmethionine decarboxylase 3
Q9SDM8
-
S-adenosylmethionine decarboxylase 4
Q6QJ69
-
SAM decarboxylase
-
-
-
-
SAM decarboxylase
-
-
SAM decarboxylase
D2K8S5
-
SAM decarboxylase
-
-
SAM-DC
-
-
SAMDC
-
-
-
-
SAMDC
Q96555
-
SAMDC
-
-
SAMDC
D2K8S5
-
CAS REGISTRY NUMBER
COMMENTARY
9036-20-8
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Neff strain
-
-
Manually annotated by BRENDA team
Acanthamoeba castellanii NEFF
Neff strain
-
-
Manually annotated by BRENDA team
variant deliciosa
-
-
Manually annotated by BRENDA team
isoform Bud2
Uniprot
Manually annotated by BRENDA team
calf
-
-
Manually annotated by BRENDA team
S-adenosylmethionine decarboxylase proenzyme 1; cv. Indian Mustard
SwissProt
Manually annotated by BRENDA team
S-adenosylmethionine decarboxylase proenzyme 2; cv. Indian Mustard
SwissProt
Manually annotated by BRENDA team
S-adenosylmethionine decarboxylase proenzyme 3; cv. Indian Mustard
SwissProt
Manually annotated by BRENDA team
S-adenosylmethionine decarboxylase proenzyme 4; cv. Indian Mustard
SwissProt
Manually annotated by BRENDA team
cultivar Newhall
-
-
Manually annotated by BRENDA team
increase in enzyme activity during exponential growth
-
-
Manually annotated by BRENDA team
proenzyme
UniProt
Manually annotated by BRENDA team
recombinant protein expressed in Oryza sativa
UniProt
Manually annotated by BRENDA team
recombinant enzyme
-
-
Manually annotated by BRENDA team
strain HT527
-
-
Manually annotated by BRENDA team
strain W
-
-
Manually annotated by BRENDA team
Escherichia coli HT527
strain HT527
-
-
Manually annotated by BRENDA team
enzyme alpha subunit
-
-
Manually annotated by BRENDA team
proenzyme
SwissProt
Manually annotated by BRENDA team
recombinant protein, expression in Escherichia coli
-
-
Manually annotated by BRENDA team
cultivars Sahara and Clipper
-
-
Manually annotated by BRENDA team
Mill. var. domestica (Borkh.) Mansf.
SwissProt
Manually annotated by BRENDA team
enzyme is essential for embryonic development
-
-
Manually annotated by BRENDA team
no activity in Vibrio cholerae
-
-
-
Manually annotated by BRENDA team
proenzyme; cultivars Arbequina and Picual
UniProt
Manually annotated by BRENDA team
S-adenosylmethionine decarboxylase proenzyme; cold-tolerant japonica cultivar Yukihikari and cold-susceptible indica variety TKM9
-
-
Manually annotated by BRENDA team
bifunctional enzyme, S-adenosylmethionine decarboxylase/ornithine decarboxylase
SwissProt
Manually annotated by BRENDA team
strain NF54
-
-
Manually annotated by BRENDA team
recombinant enzyme, expression in Escherichia coli
Uniprot
Manually annotated by BRENDA team
recombinant enzyme, expression in Escherichia coli
-
-
Manually annotated by BRENDA team
proenzyme
UniProt
Manually annotated by BRENDA team
subspecies Trypanosoma brucei rhodesiense strain STIB 900 and subspecies Trypanosoma brucei brucei strains LAB 110 EATRO and STIB 795
-
-
Manually annotated by BRENDA team
strain Lab 110 EATRO
-
-
Manually annotated by BRENDA team
Trypanosoma brucei brucei Lab 110 EATRO
strain Lab 110 EATRO
-
-
Manually annotated by BRENDA team
strains KETRI 243 and 2538
-
-
Manually annotated by BRENDA team
recombinant enzyme, His-tag, expression in Escherichia coli
-
-
Manually annotated by BRENDA team
cultivar jiagongno.7
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
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
metabolism
-
key enzyme in the biosynthesis of spermidine
metabolism
Q9WZC3
S-adenosylmethionine decarboxylase is a critical pyruvoyl-dependent enzyme in the polyamine-biosynthetic pathway
metabolism
-
SAMDC is a key enzyme in polyamine metabolism
metabolism
-
S-adenosylmethionine decarboxylase is the rate-limiting enzyme for polyamine biosynthesis
metabolism
-
key enzyme in the biosynthesis of spermidine
-
physiological function
-
AdoMetDC activity controls the expression levels of the other spermidine biosynthetic enzymes
physiological function
-
S-adenosylmethionine decarboxylase is a key enzyme in the biosynthesis of polyamines essential for cell proliferation
physiological function
D2K8S5
the expression of SAMDC is involved in the ovary development
physiological function
-
expression of the yeast enzyme in tomato reverses the ripening associated decline in spermidine and spermine levels observed in the azygous control fruit. About 2-3fold higher levels of labeled-spermidine in transgenic fruit expressing yeast enzyme confirm the enzymatic function of the introduced gene
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(5-deoxy-5-adenosyl)(3-aminopropyl)-methylsulfonium + CO2
S-adenosyl-L-methionine + H+
show the reaction diagram
-
-
-
-
?
Adenosylethionine
?
show the reaction diagram
-
poor substrate
-
-
-
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
(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
(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
P0DMN7
-
-
-
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
(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
(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
(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
(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
(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
(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
(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
(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
(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
(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
(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
(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
(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
(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
(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
(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
(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
(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
(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
(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
A5HNV7
-
-
-
?
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
(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
O02655
-
-
-
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
(5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt + CO2
show the reaction diagram
O76240
-
-
-
-
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
(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
(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
(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
(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
(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
(5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt + CO2
show the reaction diagram
Q9WZC3
-
-
-
?
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
(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
(5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt + CO2
show the reaction diagram
O66615
-
-
-
?
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
(5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt + CO2
show the reaction diagram
Q96286
-
-
?
S-adenosyl-L-methionine
(5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt + CO2
show the reaction diagram
O76240
-
-
?
S-adenosyl-L-methionine
(5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt + CO2
show the reaction diagram
P17707
-
-
-
?
S-adenosyl-L-methionine
(5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt + CO2
show the reaction diagram
Q9WZC3
-
-
-
?
S-adenosyl-L-methionine
(5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt + CO2
show the reaction diagram
Q96555
-
-
-
?
S-adenosyl-L-methionine
(5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt + CO2
show the reaction diagram
Q0JC10
-
-
-
?
S-adenosyl-L-methionine
(5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt + CO2
show the reaction diagram
Q9UWY8
-
-
-
?
S-adenosyl-L-methionine
(5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt + CO2
show the reaction diagram
-
high specificity
-
?
S-adenosyl-L-methionine
(5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt + CO2
show the reaction diagram
Q9UWY8
the crenarchaeal S-adenosylmethionine decarboxylase has no arginine decarboxylase activity
-
-
?
S-adenosyl-L-methionine
(5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt + CO2
show the reaction diagram
Trypanosoma brucei brucei Lab 110 EATRO
-
-
-
-
?
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
Escherichia coli HT527
-
-
-
-
S-adenosyl-L-methionine
(5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt + CO2
show the reaction diagram
Q9UWY8
the crenarchaeal S-adenosylmethionine decarboxylase has no arginine decarboxylase activity
-
-
?
S-adenosyl-L-methionine
(5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt + CO2
show the reaction diagram
Acanthamoeba castellanii NEFF
-
-
-
-
S-adenosyl-L-methionine
?
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine
?
show the reaction diagram
-
key enzyme in the biosynthetic pathway for spermidine and spermine
-
-
-
S-adenosyl-L-methionine
?
show the reaction diagram
-
major regulatory enzyme in polyamine biosynthesis
-
-
-
S-adenosyl-L-methionine
?
show the reaction diagram
-
major regulatory enzyme in polyamine biosynthesis
-
-
-
S-adenosyl-L-methionine
?
show the reaction diagram
-
key enzyme in polyamine biosynthesis
-
-
-
S-adenosyl-L-methionine
?
show the reaction diagram
-
key enzyme in polyamine biosynthesis
-
-
-
S-adenosyl-L-methionine
?
show the reaction diagram
-
key enzyme in polyamine biosynthesis
-
-
-
S-adenosyl-L-methionine
?
show the reaction diagram
-
the enzyme protein turns over very rapidly in growing or differentiating tissues
-
-
-
S-adenosyl-L-methionine
?
show the reaction diagram
-
EC 4.1.1.50 and EC 2.5.1.16 appear to function in sequence in animals and microorganisms in the synthesis of spermidine
-
-
-
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
S-adenosyl 3-(methylthio)propylamine + CO2
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine
S-adenosyl 3-(methylthio)propylamine + CO2
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine
S-adenosyl 3-(methylthio)propylamine + CO2
show the reaction diagram
Q25264
-
-
-
?
S-adenosyl-L-methionine
S-adenosyl 3-(methylthio)propylamine + CO2
show the reaction diagram
Q841K9
-
-
-
?
L-lysine
?
show the reaction diagram
Q96286
-
-
?
additional information
?
-
-
adhesion-dependent expression of S-adenosylmethionine decarboxylase contributes to extracellular matrix-dependent differentiation of human salivary gland epithelial cells
-
-
-
additional information
?
-
-
critical regulatory enzyme of the polyamine biosynthetic pathway
-
-
-
additional information
?
-
O49972, Q42613, Q6QJ69, Q9SDM8
key enzyme involved in polyamine biosynthetic pathway
-
-
-
additional information
?
-
-
key enzyme of polyamine biosynthetic pathway
-
-
-
additional information
?
-
-
key rate-controlling enzyme in the synthesis of spermidine and spermine. Overexpression of AdoMetDC does not produce an overt cardiac phenotype, but there is an increased cardiac hypertrophy after beta-adrenergic stimulation, and crosses of alpha-myosin heavy chain/ADoMetDC mice with alpha-myosin heavy chain/ornithine decarboxylase mice are lethal at an early embryonic stage
-
-
-
additional information
?
-
Q852S8, Q852S9
MdSAMDC1 is mainly involved in fruit development and cell growth
-
-
-
additional information
?
-
Q852S8, Q852S9
MdSAMDC2 is mainly involved in stress responses
-
-
-
additional information
?
-
-
S-adenosyl-L-methionine decarboxylase gene of cold-tolerant japonica cultivar Yukihikari and cold-susceptible indica variety TKM9 is differentially expressed under low temperature stress. Upon exposure to cold stress (5C) the level of OsSAMDC transcripts in the cold-resistant Yukihihari genotype continues to increase for up to 72 h. There is no change in OsSAMDC transcription in the cold-susceptible indica cultivar TLM9 under the same conditions
-
-
-
additional information
?
-
-
key rate-limiting enzyme located in the polyamine biosynthesis pathway. The SAMDC 5'-leader sequence participates in gene regulation at both the transcriptional and the posttranslational levels, which enables plants to sense their internal polyamine or environmental changes
-
-
-
additional information
?
-
-
S-adenosylmethionine decarboxylase is a key enzyme in the synthesis of polyamines essential for cell growth and proliferation. Its overexpression induces the transformation of murine fibroblasts in both sense and antisense orientations, yielding highly invasive tumors in nude mice. Thymosin B4 is a determinant of the transformed phenotype and invasiveness of S-adenosylmethionine decarboxylasetransfected fibroblasts
-
-
-
additional information
?
-
-
synthesis of the triamine spermidine and the tetramine spermine is achieved by the sequential addition of aminopropyl moieties from decarboxylated S-adenosylmethionine, synthesized by the enzyme S-adenosylmethionine decarboxylase
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
Q9UWY8
-
-
-
?
S-adenosyl-L-methionine
?
show the reaction diagram
-
key enzyme in the biosynthetic pathway for spermidine and spermine
-
-
-
S-adenosyl-L-methionine
?
show the reaction diagram
-
major regulatory enzyme in polyamine biosynthesis
-
-
-
S-adenosyl-L-methionine
?
show the reaction diagram
-
major regulatory enzyme in polyamine biosynthesis
-
-
-
S-adenosyl-L-methionine
?
show the reaction diagram
-
key enzyme in polyamine biosynthesis
-
-
-
S-adenosyl-L-methionine
?
show the reaction diagram
-
key enzyme in polyamine biosynthesis
-
-
-
S-adenosyl-L-methionine
?
show the reaction diagram
-
key enzyme in polyamine biosynthesis
-
-
-
S-adenosyl-L-methionine
?
show the reaction diagram
-
the enzyme protein turns over very rapidly in growing or differentiating tissues
-
-
-
S-adenosyl-L-methionine
?
show the reaction diagram
-
EC 4.1.1.50 and EC 2.5.1.16 appear to function in sequence in animals and microorganisms in the synthesis of spermidine
-
-
-
S-adenosyl-L-methionine
S-adenosyl 3-(methylthio)propylamine + CO2
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine
S-adenosyl 3-(methylthio)propylamine + CO2
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine
S-adenosyl 3-(methylthio)propylamine + CO2
show the reaction diagram
Q25264
-
-
-
?
S-adenosyl-L-methionine
S-adenosyl 3-(methylthio)propylamine + CO2
show the reaction diagram
Q841K9
-
-
-
?
S-adenosyl-L-methionine
(5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt + CO2
show the reaction diagram
Q9UWY8
-
-
-
?
additional information
?
-
-
adhesion-dependent expression of S-adenosylmethionine decarboxylase contributes to extracellular matrix-dependent differentiation of human salivary gland epithelial cells
-
-
-
additional information
?
-
-
critical regulatory enzyme of the polyamine biosynthetic pathway
-
-
-
additional information
?
-
O49972, Q42613, Q6QJ69, Q9SDM8
key enzyme involved in polyamine biosynthetic pathway
-
-
-
additional information
?
-
-
key enzyme of polyamine biosynthetic pathway
-
-
-
additional information
?
-
-
key rate-controlling enzyme in the synthesis of spermidine and spermine. Overexpression of AdoMetDC does not produce an overt cardiac phenotype, but there is an increased cardiac hypertrophy after beta-adrenergic stimulation, and crosses of alpha-myosin heavy chain/ADoMetDC mice with alpha-myosin heavy chain/ornithine decarboxylase mice are lethal at an early embryonic stage
-
-
-
additional information
?
-
Q852S8, Q852S9
MdSAMDC1 is mainly involved in fruit development and cell growth
-
-
-
additional information
?
-
Q852S8, Q852S9
MdSAMDC2 is mainly involved in stress responses
-
-
-
additional information
?
-
-
S-adenosyl-L-methionine decarboxylase gene of cold-tolerant japonica cultivar Yukihikari and cold-susceptible indica variety TKM9 is differentially expressed under low temperature stress. Upon exposure to cold stress (5C) the level of OsSAMDC transcripts in the cold-resistant Yukihihari genotype continues to increase for up to 72 h. There is no change in OsSAMDC transcription in the cold-susceptible indica cultivar TLM9 under the same conditions
-
-
-
additional information
?
-
-
synthesis of the triamine spermidine and the tetramine spermine is achieved by the sequential addition of aminopropyl moieties from decarboxylated S-adenosylmethionine, synthesized by the enzyme S-adenosylmethionine decarboxylase
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
cofactor
pyridoxal 5'-phosphate
-
absent
pyridoxal 5'-phosphate
-
no effect
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
O66615
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
Q96555
-
pyridoxal 5'-phosphate
Q0JC10
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
thiamine diphosphate
O66615
-
thiamine diphosphate
-
-
thiamine diphosphate
Q9WZC3
-
thiamine diphosphate
-
-
[4Fe-4S]-center
Q841K9
the fully reconstituted His6-tagged enzyme contains approximately 6.8 iron equivalents per monomer
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Al3+
-
activation, no significant influence on the rate-limiting step. Km value 0.850 mM
Ca2+
-
requires a divalent cation, Mg2+, Ca2+ or Mn2+
Ca2+
-
Mg2+ required, Mn2+ or Ca2+ can partially replace
Ca2+
-
activation, no significant influence on the rate-limiting step. Km value 0.117 mM
Co2+
-
activation, no significant influence on the rate-limiting step. Km value 0.286 mM
Eu3+
-
activation, no significant influence on the rate-limiting step. Km value 0.095 mM
Fe2+
-
activation, no significant influence on the rate-limiting step. Km value 0.121 mM
Fe3+
-
activation, no significant influence on the rate-limiting step. Km value 0.194 mM
Gd3+
-
activation, no significant influence on the rate-limiting step. Km value 0.043 mM
Li+
-
activation, no significant influence on the rate-limiting step. Km value 0.219 mM
Mg2+
-
no stimulaton
Mg2+
-
no requirement
Mg2+
-
requires a divalent cation, Mg2+, Ca2+ or Mn2+
Mg2+
-
no effect
Mg2+
-
activation, no significant influence on the rate-limiting step. Km value 0.106 mM
Mn2+
-
affinity for Mn2+ is increased in presence of substrate; requires a divalent cation, Mg2+, Ca2+ or Mn2+
Mn2+
-
requires a divalent cation, Mg2+, Ca2+ or Mn2+
Mn2+
-
Mg2+ required, Mn2+ or Ca2+ can partially replace
Tb3+
-
activation, no significant influence on the rate-limiting step. Km value 0.151 mM
Mn2+
-
activation, no significant influence on the rate-limiting step. Km value 0.045 mM
additional information
-
no requirement for Mg2+
additional information
-
no requirement for a divalent metal ion
additional information
-
no requirement for a divalent metal ion
additional information
-
unaffected by divalent cations
additional information
-
no requirement for a divalent metal ion
additional information
-
no significant levels of metals
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1E)-1-(9-bromo-3-phenanthryl)ethanone oxime
-
75% inhibition at 0.1 mM
(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
(2E)-2-[4-[amino(imino)methyl]-2,3-dihydro-1H-inden-1-ylidene]hydrazinecarboximidamide
-
i.e. CGP48664A, SAM486A, active site inhibitor, in addition suppresses HIV-1 replication
(2R,3R,4R,5R)-2-([[(2Z)-4-aminobut-2-en-1-yl](methyl)amino]methyl)-5-(6-amino-9H-purin-9-yl)-4-fluorotetrahydrofuran-3-ol
-
-
(2R,3R,4S,5R)-2-([[(2Z)-4-aminobut-2-en-1-yl](methyl)amino]methyl)-5-(6-amino-9H-purin-9-yl)-4-fluorotetrahydrofuran-3-ol
-
-
(2R,3S,4R,5R)-2-([[(2Z)-4-aminobut-2-en-1-yl](methyl)amino]methyl)-5-(6-amino-2-chloro-9H-purin-9-yl)tetrahydrofuran-3,4-diol
-
-
(5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt
-
competitive with respect to S-adenosylmethionine; i.e. decarboxylated S-adenosylmethionine
(5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt
-
irreversible
(5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt
-
-
(5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt
-
-
(5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt
-
competitive with respect to S-adenosylmethionine
(5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt
-
-
(R)-alpha-methylspermine
-
-
(R,R)-alpha,omega-bismethylspermine
-
best suppressor of AdoMetDC activity
(S)-alpha-methylspermidine
-
-
1,1'-[(Methylethanediylidene)dinitrilo] bis(3-aminoguanidine)
-
-
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'-Chlorodeoxyadenosine
-
-
2'-[(9H-fluoren-2-ylamino)carbonyl]biphenyl-2-carboxylate
-
74% inhibition at 0.1 mM
2,2'-Dihydroxy-6,6'-dinaphthyl disulfide
-
-
2,2'-dipyridyl
-
-
2-[2-(diethylammonio)ethyl]-9-hydroxy-5,11-dimethyl-6H-pyrido[4,3-b]carbazol-2-ium
-
67% inhibition at 0.1 mM
3-[(E)-[(2E)-[amino[(2E)-2-[3-[amino(imino)methyl]benzylidene]hydrazino]methylene]hydrazono]methyl]benzenecarboximidamide
-
i.e. CGP40215, active site inhibitor
4-Amidinoindan-1-(2'-amidino)hydrazone
-
i.e. CGP 48664
4-Amidinoindan-1-(2'-amidino)hydrazone
-
i.e. CGP 48664
4-Amidinoindan-1-(2'-amidino)hydrazone
-
i.e. CGP 48664
4-Amidinoindan-1-(2'-amidino)hydrazone
-
-
4-amidinoindan-1-one-2'-amidinohydrazone
O66615
-
4-amidinoindan-1-one-2'-amidinohydrazone
-
-
4-amidinoindan-1-one-2'-amidinohydrazone
Q9WZC3
-
4-amidinoindan-1-one-2'-amidinohydrazone
-
-
4-amidinoindan-1-one-2'-amidinohydrazone
P17707
CGP48664A
4-Bromo-3-hydroxybenzoyloxyamine dihydrogen phosphate
-
i.e. NSD-1055
4-Bromo-3-hydroxybenzyloxyamine
-
-
4-[(E)-2-(2-chlorophenyl)vinyl]quinolinium
-
67% inhibition at 0.1 mM
5'-([(Z)-4-Amino-2-butenyl]methylamino)-5'-deoxyadenosine
-
i.e. MDL 73811
5'-deoxy 5'-[(2-guanidinoethyl)methylamino]adenosine
P17707
less than 5% inhibition at 0.1 mM
5'-deoxy-5'-(2-methylaminoethylamino)adenosine
P17707
less than 5% inhibition at 0.1 mM
5'-deoxy-5'-(3-methylaminopropylamino)-8-phenyladenosine sulfate
P17707
less than 5% inhibition at 0.1 mM
5'-deoxy-5'-(dimethyl-sulfonio)adenosine
O66615
-
5'-deoxy-5'-(dimethyl-sulfonio)adenosine
-
-
5'-deoxy-5'-(dimethyl-sulfonio)adenosine
Q9WZC3
-
5'-deoxy-5'-(dimethyl-sulfonio)adenosine
-
-
5'-deoxy-5'-(N,N-dimethylamino)-8-methyladenosine
P17707
-
5'-deoxy-5'-(N,N-dimethylamino)adenosine
P17707
-
5'-deoxy-5'-(N-dimethyl)amino-8-methyl adenosine
O66615
-
5'-deoxy-5'-(N-dimethyl)amino-8-methyl adenosine
-
-
5'-deoxy-5'-(N-dimethyl)amino-8-methyl adenosine
Q9WZC3
-
5'-deoxy-5'-(N-dimethyl)amino-8-methyl adenosine
-
-
5'-deoxy-5'-(N-dimethyl)amino-8-methyladenosine
-
-
5'-deoxy-5'-dimethylsulfonio-8-methyladenosine chloride
P17707
-
5'-deoxy-5'-dimethylsulfonioadenosine chloride
P17707
-
5'-deoxy-5'-dimethylthioadenosine
-
-
5'-deoxy-5'-[(2-hydrazinocarbonylethyl)methylamino]-8-methyladenosine sulfate
P17707
-
5'-deoxy-5'-[(2-hydrazinocarbonylethyl)methylamino]-adenosine sulfate
P17707
-
5'-deoxy-5'-[(2-hydrazinoethyl)methylamino]adenosine
P17707
-
5'-deoxy-5'-[(2-hydroxyamidinoethyl)methylamino]adenosine
P17707
-
5'-Deoxy-5'-[(3-hydrazinopropyl)methylamino]adenosine
-
irreversible
5'-Deoxy-5'-[(3-hydrazinopropyl)methylamino]adenosine
-
-
5'-deoxy-5'-[(hydrazinocarbonylmethyl)methylamino]-8-methyladenosine
P17707
-
5'-deoxy-5'-[N-methyl-N-(3-hydrazino-propyl)amino]adenosine
O66615
-
5'-deoxy-5'-[N-methyl-N-(3-hydrazino-propyl)amino]adenosine
-
-
5'-deoxy-5'-[N-methyl-N-(3-hydrazino-propyl)amino]adenosine
Q9WZC3
-
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
O66615
-
5'-deoxy-5'-[N-methyl-N-[(2-aminooxy)-ethyl]amino]adenosine
-
-
5'-deoxy-5'-[N-methyl-N-[(2-aminooxy)-ethyl]amino]adenosine
Q9WZC3
-
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
P17707
less than 5% inhibition at 0.1 mM
5'-deoxy-8-methyl-5'-(2-methylaminoethylamino)adenosine
P17707
less than 5% inhibition at 0.1 mM
5'-dimethylthioadenosine sulfonium salt
-
-
5'-methylthioadenosine
-
-
5'-[(2-aminoethyl)methylamino]-5'-deoxy-8-methyladenosine
P17707
-
5'-[(2-aminoethyl)methylamino]-5'-deoxyadenosine
P17707
less than 5% inhibition at 0.1 mM
5'-[(2-aminooxyethyl)methylamino]-5'-deoxy-8-(methylamino)adenosine sulfate
P17707
-
5'-[(2-aminooxyethyl)methylamino]-5'-deoxy-8-methyladenosine sulfate
P17707
-
5'-[(2-aminooxyethyl)methylamino]-5'-deoxy-8-phenyladenosine sulfate
P17707
less than 5% inhibition at 0.1 mM
5'-[(2-aminooxyethyl)methylamino]-5'-deoxyadenosine
P17707
-
5'-[(2-carboxamidoethyl)methyamino]-5'-deoxy-8-ethyladenosine sulfate
P17707
-
5'-[(2-carboxamidoethyl)methylamino]-5'-deoxy-8-methyladenosine sulfate
P17707
-
5'-[(2-carboxamidoethyl)methylamino]-5'-deoxyadenosine sulfate
P17707
-
5'-[(3-aminopropyl)methylamino]-5'-deoxy-8-(methylamino)adenosine sulfate
P17707
-
5'-[(3-aminopropyl)methylamino]-5'-deoxy-8-ethyladenosine sulfate
P17707
-
5'-[(3-aminopropyl)methylamino]-5'-deoxy-8-methyladenosine sulfate
P17707
-
5'-[(3-aminopropyl)methylamino]-5'-deoxy-8-phenyladenosine sulfate
P17707
less than 5% inhibition at 0.1 mM
5'-[(3-aminopropyl)methylamino]-5'-deoxyadenosine sulfate
P17707
-
5'-[(4-aminooxybutyl)methylamino]-5'-deoxy-8-(methylamino)adenosine sulfate
P17707
-
5'-[(4-aminooxybutyl)methylamino]-5'-deoxy-8-ethyladenosine sulfate
P17707
-
5'-[(4-aminooxybutyl)methylamino]-5'-deoxy-8-methyladenosine sulfate
P17707
-
5'-[(4-aminooxybutyl)methylamino]-5'-deoxy-8-oxoadenosine sulfate
P17707
-
5'-[(4-aminooxybutyl)methylamino]-5'-deoxy-8-phenyladenosine sulfate
P17707
less than 5% inhibition at 0.1 mM
5'-[(4-aminooxybutyl)methylamino]-5'-deoxyadenosine sulfate
P17707
-
5'-[(carboxamidomethyl)methylamino]-5'-deoxy-8-methyladenosine sulfate
P17707
less than 5% inhibition at 0.1 mM
5'-[[(2Z)-4-aminobut-2-en-1-yl](methyl)amino]-5'-deoxy-2-methyladenosine
-
-
5'-[[(2Z)-4-aminobut-2-en-1-yl](methyl)amino]-5'-deoxy-8-ethyladenosine
-
-
5'-[[(2Z)-4-aminobut-2-en-1-yl](methyl)amino]-5'-deoxy-8-methyladenosine
-
-
5'-[[(2Z)-4-aminobut-2-en-1-yl](methyl)amino]-5'-deoxy-8-propyladenosine
-
-
5'-[[(Z)-4-amino-2-butenyl]methylamino]-5'-deoxyadenosine
P17707
-
5'-[[(Z)-4-aminobut-2-enyl](methylamino)]adenosine
-
MDL-73811
5'-{[(Z)-4-Amino-2-butenyl]methylamino}-5'-deoxyadenosine
-
irreversible; the inhibitor leads to transamination of the pyruvate prosthetic group
5'-{[(Z)-4-Amino-2-butenyl]methylamino}-5'-deoxyadenosine
-
irreversible
5,5'-dithiobis(2-nitrobenzoate)
-
-
8-methyl-5'-[[(Z)-4-aminobut-2-enyl]-(methylamino)]adenosine
-
Genz-644131, potent inhibitor
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
agmatine
-
-
Aminoguanidine
-
irreversible
Berenil
-
13% inhibition at 1 mM
Berenil
-
irreversible
Berenil
-
reversible
Bis[[3-(aminoiminomethyl)phenyl]methylene]carbonimidic dihydrazide trihydrochloride
-
i.e. CGP 40215A
BW-1
-
85% inhibition at 2 mM, in presence of 2 mM putrescine, degree of inhibition depends on actual putrescine abundance
BW-1
-
99% inhibition at 2 mM, in presence of 2 mM putrescine, degree of inhibition depends on actual putrescine abundance
Ca2+
-
0.5 mM CaCl2
Canaline
-
at high concentrations
Cd2+
-
0.5 mM CdCl2
CGP 48664
-
specific inhibitor of AdoMetDC
CGP 48664A
-
i.e. 4-amidinoindan-1-one-20-amidinohydrazone, also known as SAM486A
CGP48664
-
non-competitive inhibition, i.e. 4-amidinoindan-1-one-2'-amidinohydrazone
CGP48664A
O66615
i.e. 4-amidinoindan-1-one-2'-amidinohydrazone
CGP48664A
-
i.e. 4-amidinoindan-1-one-2'-amidinohydrazone
CGP48664A
Q9WZC3
i.e. 4-amidinoindan-1-one-2'-amidinohydrazone
CGP48664A
-
i.e. 4-amidinoindan-1-one-2'-amidinohydrazone
CGP48664A
-
i.e. 4-amidinoindan-1-one-2'-amidinohydrazone
Co2+
-
0.5 mM CoCl2
Di-N'''-Methylglyoxal bis(guanylhydrazone)
-
-
Di-N''-Methylglyoxal bis(guanylhydrazone)
-
-
Dimethylglyoxal bis(guanylhydrazone)
-
-
EDTA
-
above 1 mM
Ethambutol
-
14% inhibition at 1 mM
Ethidium bromide
-
-
ethylglyoxal bis(guanylhydrazone)
-
-
ethylglyoxal bis(guanylhydrazone)
-
specific inhibitor of SAMDC
FeCl2
-
0.5 mM
Glyoxal bis(guanylhydrazone)
-
-
hydroxylamine
-
-
Hydroxystilbamidine
-
-
iodoacetamide
-
-
iodoacetic acid
-
-
iodoacetic acid
-
after treatment with iodoacetic acid at 37C for 1 h, the activity of AdoMetDC in the absence of putrescine is almost completely inhibited
Isonicotinic acid hydrazide
-
at high concentrations
MDL 27695
-
44% inhibition at 2 mM, in presence of 2 mM putrescine
MDL 27695
-
86% inhibition at 2 mM, in presence of 2 mM putrescine
MDL 73811
-
-
MDL 73822
-
irreversibel
-
MDL73811
-
7% residual activity at 0.001 mM
MDL73811
-
i.e. 5'-[[(Z)-4-amino-2-butenyl]methylamino]-5'-deoxyadenosine, complete inhibition at 0.005 mM
MDL73811
-
irreversible inhibitor
MDL73811
-
-
MDL73811
-
irreversible inhibitor, i.e. 5'-([(Z)-4-amino-2-butenyl]methylamino)-5'-deoxyadenosine
methylglyoxal bis(guanylhydrazone)
-
13% inhibition at 10 mM, 58% inhibition at 10 mM
methylglyoxal bis(guanylhydrazone)
-
irreversible
methylglyoxal bis(guanylhydrazone)
-
strong
methylglyoxal bis(guanylhydrazone)
-
competitive
methylglyoxal bis(guanylhydrazone)
-
reversible
methylglyoxal bis(guanylhydrazone)
-
-
methylglyoxal bis(guanylhydrazone)
-
strong
methylglyoxal bis(guanylhydrazone)
-
-
methylglyoxal bis(guanylhydrazone)
-
poor
methylglyoxal bis(guanylhydrazone)
-
and analogues
methylglyoxal bis(guanylhydrazone)
-
-
methylglyoxal bis(guanylhydrazone)
-
-
methylglyoxal bis(guanylhydrazone)
-
competitive
methylglyoxal bis(guanylhydrazone)
-
-
methylglyoxal bis(guanylhydrazone)
-
-
methylglyoxal bis(guanylhydrazone)
-
competitive, binds at a single site per enzyme heterodimer
methylglyoxal bis(guanylhydrazone)
-
-
methylglyoxal bis(guanylhydrazone)
-
-
methylglyoxal bis(guanylhydrazone)
-
-
methylglyoxal bis(guanylhydrazone)
-
-
methylglyoxal bis(guanylhydrazone)
P17707
competitive inhibitor
methylglyoxal bis-(guanylhydrazone)
-
-
methylglyoxal-bis (guanylhydrazone)
-
-
methylglyoxal-bis (guanylhydrazone)
-
competitive inhibitor
methylglyoxal-bis(guanylhydrazone)
-
50% inhibition at 0.012 mM
methylglyoxal-bis(guanylhydrazone)
-
in the absence of phenanthrene, treatment with 2.0 mM methylglyoxal-bis(guanylhydrazone) inhibits SAMDC activity by 73%
methylglyoxalbis(guanylhydrazone)
O66615
-
methylglyoxalbis(guanylhydrazone)
-
-
methylglyoxalbis(guanylhydrazone)
Q9WZC3
-
methylglyoxalbis(guanylhydrazone)
-
-
MgCl2
-
0.5 mM
n-Butylglyoxal bis(guanylhydrazone)
-
-
NaBH4
-
-
NaCl
-
enzyme from infected cells is unaffected up to 0.8 M, 50% inhibition of the enzyme from uninfected cells at 0.45 M
NaCNBH3
-
irreversible
-
NaCNBH3
-
-
-
NaCNBH3
-
inactivation in presence of adenosylmethionine and Mg2+, no inactivation in absence of substrate and Mg2+
-
NaCNBH3
-
in presence of substrate or product
-
NaCNBH3
-
inactivation in presence of substrate
-
NEM
-
-
NH4Cl
-
0.5 mM
p-chloromercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
p-Hydroxymercuriphenylsulfonate
-
-
Pentamidine
-
irreversible
Pentamidine
-
-
Pentane dialdehyde bis(guanylhydrazone)
-
-
Pentane dialdehyde bis(guanylhydrazone)
-
weak
phenylhydrazine
-
strong
phenylhydrazine
-
-
phenylhydrazine
-
-
PMW-2000-11-13-1
-
52% inhibition at 2 mM, in presence of 2 mM putrescine
PMW-2000-11-13-1
-
97% inhibition at 2 mM, in presence of 2 mM putrescine
Propamidine
-
-
Propane dialdehyde bis(guanylhydrazone)
-
-
Propane dialdehyde bis(guanylhydrazone)
-
weak
putrescine
-
weak
RHW-17-69-75
-
45% inhibition at 2 mM, in presence of 2 mM putrescine
RHW-17-69-75
-
97% inhibition at 2 mM, in presence of 2 mM putrescine
S-(5'-Adenosyl)-methylthio-2-aminooxyethane
-
potent irreversible inhibitor
S-(5'-Deoxy-5'-adenosyl)methylthioethylhydroxylamine
-
69% inhibition at 0.5 mM
S-(5'-Deoxy-5'-adenosyl)methylthioethylhydroxylamine
-
irreversible
S-Adenosyl-4-methylthiobutyric acid
-
-
S-adenosyl-L-methionine
-
substrate inactivation results in the conversion of the pyruvoyl group to an alanyl residue. The mechanism of inactivation involves the transamination of the nascent product to the pyruvoyl group, followed by the elimination of methylthioadenosine and the generation of a 2-propenal equivalent which can undergo a Michael addition to the enzyme
S-adenosyl-L-methionine
-
in presence of saturating concentrations of putrescine
S-Methyl-S-adenosyl-L-cysteine
-
-
S-methyladenosylhomocysteamine
-
strong
Salicylaldehyde
-
inactivation, substrate protects
SAM486A
-
also known as CGP48664
Semicarbazide
-
-
spermidine
-
-
spermidine
-
weak
spermidine
-
-
spermine
-
strong
spermine
-
-
spermine
-
inhibits the enzyme from liver from sham-operated rats, no effect on regenerating liver enzyme
Zn2+
-
0.5 mM
MnCl2
-
0.5 mM
additional information
-
no inhibition by 1-aminooxy-3-aminopropane
-
additional information
-
inhibited by CGP 51467A, CGP 48009A, and CGP 62577A
-
additional information
-
inhibitors with potent antitumor activity
-
additional information
-
unaffected by divalent cations
-
additional information
-
not inhibitory are: MgCl2, CaCl2, EDTA, putrescine at 10 mM each, or KCl at 50 mM
-
additional information
-
the enzyme is almost insensitive to feedback inhibition at neutral pH
-
additional information
-
no inhibition by Tris
-
additional information
-
inhibition of SAMDC by methylglyoxal-bis(guanylhydrazone), and hence reduced spermidine and spermine synthesis limits the ability of plants to recover following exposure to phenanthrene to a slightly greater extent than inhibition of arginine decarboxylase; inhibition of SAMDC results in much greater levels of oxidative damage than seen in plants treated with 0.5 microM phenanthrene; treatment of plants exposed to phenanthrene with DL-alpha-difluoromethylarginine does not result in any major changes to the trends in SAMDC activity observed in plants exposed to phenanthrene
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(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
1,15-diamino-4,12-diazapentadecane
-
-
1,3-Diaminopropane
-
stimulates
1,3-Diaminopropane
-
activates; stimulates
1,3-Diaminopropane
-
enzyme from psoas is stimulated more than enzyme from liver
1,3-Diaminopropane
-
stimulates
1,5-Diaminopentane
-
stimulates
1,5-Diaminopentane
-
57% of activation by putrescine
1,6-diaminohexane
-
58% of activation by putrescine
1,7-Diaminoheptane
-
45% of activation by putrescine
cadaverine
-
activates
cadaverine
O76240
increase of kcat up to 9fold
N1-acetylspermidine
-
60% of activation by putrescine
phenanthrene
-
concentrations of phenanthrene up to 0.5 microM cause significant increases in the activity of SAMDC, with a resultant increase in tissue polyamine levels
PMW-2000-11-13-5
-
-
putrescine
-
weak stimulation, relatively insensitive to activation as compared with the mammalian enzyme
putrescine
-
no stimulation
putrescine
-
required; stimulation
putrescine
-
required
putrescine
-
0.25 mM required for maximal activation; stimulation
putrescine
-
stimulation
putrescine
-
stimulation
putrescine
-
stimulation
putrescine
-
stimulation
putrescine
-
accelarates the conversion of the proenzyme into the enzyme subunits; stimulation
putrescine
-
stimulation
putrescine
-
maximal stimulation at 1 mM; stimulation
putrescine
-
stimulation
putrescine
-
stimulation
putrescine
-
no requirement
putrescine
-
-
putrescine
-
enhances activity up to 350fold
putrescine
-
strong
putrescine
O76240
increase of kcat up to 9fold
putrescine
-
stimulates ration kcat/Km for wild-type 27fold, also stimulates binding of inhibitors (2E)-2-[4-[amino(imino)methyl]-2,3-dihydro-1H-inden-1-ylidene]hydrazinecarboximidamide and 3-[(E)-[(2E)-[amino[(2E)-2-[3-[amino(imino)methyl]benzylidene]hydrazino]methylene]hydrazono]methyl]benzenecarboximidamide
putrescine
-
-
putrescine
-
the activity and processing of S-adenosylmethionine decarboxylase is stimulated by putrescine. About 80% of its activity remained after treatment with iodoacetic acid in the presence of putrescine
putrescine
-
-
pyruvate
-
contains pyruvate
pyruvate
-
cofactor; contains 1 pyruvoyl residue for each alphabeta pair
pyruvate
-
-
pyruvate
-
each subunit contains one covalently linked pyruvate
pyruvate
-
each subunit contains one covalently linked pyruvate
pyruvate
-
each subunit contains one covalently linked pyruvate
pyruvate
-
cofactor
pyruvate
-
essential for activity
pyruvate
-
alpha-subunit contains an N-terminal pyruvoyl group
pyruvate
-
contains approximately 0.8 mol pyruvate per mol of enzyme; covalently linked prosthetic group
spermidine
-
weak stimulation
spermidine
-
stimulates
spermidine
-
-
spermidine
-
-
spermidine
-
stimulates
spermidine
-
no effect
spermidine
-
82% of activation by putrescine
spermidine
-
250fold increase of catalytic activity at 2 mM
spermine
-
weak stimulation
spermine
-
13% of activation by putrescine
spermine
-
90fold increase of catalytic activity at 2 mM
YZ-33-046
-
-
YZ-33-050C
-
-
difluoromethylornithine
-
5 mM causes an induction of the enzyme activity
additional information
-
DL-alpha-difluoromethylornithine does not influence the general trend of increased SAMDC activity observed in plants exposed to 0.1 or 0.5 microM phenanthrene
-
additional information
-
increased enzyme activity after wounding of the potatoe
-
additional information
-
not activated by putrescine
-
additional information
-
the AdoMetDC activity in the bifunctional enzyme is not stimulated by putrescine
-
additional information
-
enzyme activation likely involves a conformational change of the N-terminal peptide
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00193
S-adenosyl-L-methionine
Q841K9
wild type enzyme, in 50 mM HEPES buffer (pH 8.0), at 25C
0.00196
S-adenosyl-L-methionine
Q841K9
mutant enzyme M37Y, in 50 mM HEPES buffer (pH 8.0), at 25C
0.00204
S-adenosyl-L-methionine
Q841K9
mutant enzyme M37W, in 50 mM HEPES buffer (pH 8.0), at 25C
0.00215
S-adenosyl-L-methionine
Q841K9
mutant enzyme M37F, in 50 mM HEPES buffer (pH 8.0), at 25C
0.005
S-adenosyl-L-methionine
-
-
0.02 - 0.11
S-adenosyl-L-methionine
-
-
0.023
S-adenosyl-L-methionine
-
-
0.03
S-adenosyl-L-methionine
-
-
0.03
S-adenosyl-L-methionine
-
in presence of 2 mM putrescine
0.036
S-adenosyl-L-methionine
-
-
0.038
S-adenosyl-L-methionine
-
-
0.043
S-adenosyl-L-methionine
-
bifunctional AdoMetDC/ODC enzyme, in 50 mM KH2PO4 pH 7.5, 1 mM EDTA, 1 mM dithiothreitol, at 37C
0.05
S-adenosyl-L-methionine
-
pH 7.5, in presence of 2.5 mM putrescine
0.05
S-adenosyl-L-methionine
-
enzyme from liver
0.05
S-adenosyl-L-methionine
O76240
pH 8.0, 37C, without putrescine
0.058
S-adenosyl-L-methionine
-
native wild type AdoMetDC enzyme, in 50 mM KH2PO4 pH 7.5, 1 mM EDTA, 1 mM dithiothreitol, at 37C
0.08
S-adenosyl-L-methionine
Q9WZC3
at pH 6.8 and 65C
0.095
S-adenosyl-L-methionine
-
pH 7.5
0.1
S-adenosyl-L-methionine
-
enzyme from psoas
0.1
S-adenosyl-L-methionine
-
-
0.11
S-adenosyl-L-methionine
A5HNV7
enzyme in complex with prozyme, absence of putrescine, 37C, pH 8.0
0.115
S-adenosyl-L-methionine
-
in presence of 2 mM putrescine
0.12
S-adenosyl-L-methionine
-
pH 7.4, 25C
0.14
S-adenosyl-L-methionine
-
wild type homodimeric enzyme, with 5 mM putrescine, at pH 8.0 and 37C
0.146
S-adenosyl-L-methionine
-
enzyme from infected cells
0.17
S-adenosyl-L-methionine
A5HNV7
enzyme in complex with prozyme, presence of putrescine, 37C, pH 8.0
0.2
S-adenosyl-L-methionine
-
pH 7.5, 28
0.21
S-adenosyl-L-methionine
-
-
0.24
S-adenosyl-L-methionine
A5HNV7
free enzyme, presence of putrescine, 37C, pH 8.0
0.245
S-adenosyl-L-methionine
-
enzyme from uninfected cells
0.25
S-adenosyl-L-methionine
-
recombinant AdoMetDC enzyme, in 50 mM KH2PO4 pH 7.5, 1 mM EDTA, 1 mM dithiothreitol, at 37C
0.38
S-adenosyl-L-methionine
A5HNV7
free enzyme, absence of putrescine, 37C, pH 8.0
0.4
S-adenosyl-L-methionine
-
wild type homodimeric enzyme, without putrescine, at pH 8.0 and 37C
0.47
S-adenosyl-L-methionine
-
in presence of 0.5 mM putrescine
0.6
S-adenosyl-L-methionine
-
pH 7.4, 70C
1
S-adenosyl-L-methionine
-
in presence of 0.3 mM putrescine
0.06
S-adenosylmethionine
-
-
0.09
S-adenosylmethionine
-
in presence of putrescine
0.5
S-adenosylmethionine
-
in absence of putrescine
0.96
S-adenosylmethionine
-
-
1.518
lysine
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
O76240
addition of putrescine increases Km up to 2-fold
-
additional information
additional information
-
ratio of kcat/Km value, wild-type 3.5 per M and s in absence, 100 per M and s in presence of putrescine, mutant S111R 2.0 per M and s in absence, 6.4 per M and s in presence of putrescine, mutant D174V 36.6 per M and s in absence, 5 per M and s in presence of putrescine, mutant F285 1.8 per M and s in absence, 650 per M and s in presence of putrescine
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0013
S-adenosyl-L-methionine
A5HNV7
free enzyme, absence of putrescine, 37C, pH 8.0
0.0058
S-adenosyl-L-methionine
-
wild type homodimeric enzyme, without putrescine, at pH 8.0 and 37C
0.0065
S-adenosyl-L-methionine
-
wild type homodimeric enzyme, with 5 mM putrescine, at pH 8.0 and 37C
0.0075
S-adenosyl-L-methionine
-
22 C, pH 7.5
0.0082
S-adenosyl-L-methionine
A5HNV7
free enzyme, presence of putrescine, 37C, pH 8.0
0.021
S-adenosyl-L-methionine
Q841K9
mutant enzyme M37Y, in 50 mM HEPES buffer (pH 8.0), at 25C
0.024
S-adenosyl-L-methionine
Q841K9
mutant enzyme M37F, in 50 mM HEPES buffer (pH 8.0), at 25C; mutant enzyme M37W, in 50 mM HEPES buffer (pH 8.0), at 25C
0.027
S-adenosyl-L-methionine
Q841K9
wild type enzyme, in 50 mM HEPES buffer (pH 8.0), at 25C
0.088
S-adenosyl-L-methionine
-
recombinant AdoMetDC enzyme, in 50 mM KH2PO4 pH 7.5, 1 mM EDTA, 1 mM dithiothreitol, at 37C
1
S-adenosyl-L-methionine
Q9WZC3
at pH 6.8 and 65C
1.4
S-adenosyl-L-methionine
A5HNV7
enzyme in complex with prozyme, absence of putrescine, 37C, pH 8.0
1.7
S-adenosyl-L-methionine
A5HNV7
enzyme in complex with prozyme, presence of putrescine, 37C, pH 8.0
6
S-adenosyl-methionine
-
in presence of putrescine
additional information
additional information
-
increase of turnover-number 38-fold at physiological temperature of 80C
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.3
S-adenosyl-L-methionine
Q9UWY8
pH 8.0, 70C
24
12.5
S-adenosyl-L-methionine
Q9WZC3
at pH 6.8 and 65C
24
630
S-adenosyl-L-methionine
Q841K9
mutant enzyme M37Y, in 50 mM HEPES buffer (pH 8.0), at 25C
24
680
S-adenosyl-L-methionine
Q841K9
mutant enzyme M37F, in 50 mM HEPES buffer (pH 8.0), at 25C
24
700
S-adenosyl-L-methionine
Q841K9
mutant enzyme M37W, in 50 mM HEPES buffer (pH 8.0), at 25C
24
840
S-adenosyl-L-methionine
Q841K9
wild type enzyme, in 50 mM HEPES buffer (pH 8.0), at 25C
24
15000
S-adenosyl-L-methionine
-
wild type homodimeric enzyme, without putrescine, at pH 8.0 and 37C
24
46000
S-adenosyl-L-methionine
-
wild type homodimeric enzyme, with 5 mM putrescine, at pH 8.0 and 37C
24
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.003
CGP48664
-
native wild type AdoMetDC enzyme, in 50 mM KH2PO4 pH 7.5, 1 mM EDTA, 1 mM dithiothreitol, at 37C
0.00407
CGP48664
-
recombinant AdoMetDC enzyme, in 50 mM KH2PO4 pH 7.5, 1 mM EDTA, 1 mM dithiothreitol, at 37C
0.00033
MDL73811
-
recombinant AdoMetDC enzyme, in 50 mM KH2PO4 pH 7.5, 1 mM EDTA, 1 mM dithiothreitol, at 37C
0.0016
MDL73811
-
bifunctional AdoMetDC/ODC enzyme, in 50 mM KH2PO4 pH 7.5, 1 mM EDTA, 1 mM dithiothreitol, at 37C
2 - 5
methylglyoxal bis(guanylhydrazone)
-
-
0.00015
methylglyoxal bis-(guanylhydrazone)
-
-
0.45
NaCl
-
enzyme from infected cells is unaffected up to 0.8 M; inhibition of the enzyme from uninfected cells
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.2
3-[(E)-[(2E)-[amino[(2E)-2-[3-[amino(imino)methyl]benzylidene]hydrazino]methylene]hydrazono]methyl]benzenecarboximidamide
-
mutant F285H, presence of putrescine, 37C, pH 8.0
3.2
3-[(E)-[(2E)-[amino[(2E)-2-[3-[amino(imino)methyl]benzylidene]hydrazino]methylene]hydrazono]methyl]benzenecarboximidamide
-
wild-type, presence of putrescine, 37C, pH 8.0
13
3-[(E)-[(2E)-[amino[(2E)-2-[3-[amino(imino)methyl]benzylidene]hydrazino]methylene]hydrazono]methyl]benzenecarboximidamide
-
mutant D174V, absence of putrescine, 37C, pH 8.0
14
3-[(E)-[(2E)-[amino[(2E)-2-[3-[amino(imino)methyl]benzylidene]hydrazino]methylene]hydrazono]methyl]benzenecarboximidamide
-
mutant D174V, presence of putrescine, 37C, pH 8.0
26
3-[(E)-[(2E)-[amino[(2E)-2-[3-[amino(imino)methyl]benzylidene]hydrazino]methylene]hydrazono]methyl]benzenecarboximidamide
-
mutant F285H, absence of putrescine, 37C, pH 8.0
32
3-[(E)-[(2E)-[amino[(2E)-2-[3-[amino(imino)methyl]benzylidene]hydrazino]methylene]hydrazono]methyl]benzenecarboximidamide
-
wild-type, absence of putrescine, 37C, pH 8.0
96
3-[(E)-[(2E)-[amino[(2E)-2-[3-[amino(imino)methyl]benzylidene]hydrazino]methylene]hydrazono]methyl]benzenecarboximidamide
-
mutant S111R, absence of putrescine, 37C, pH 8.0
104
3-[(E)-[(2E)-[amino[(2E)-2-[3-[amino(imino)methyl]benzylidene]hydrazino]methylene]hydrazono]methyl]benzenecarboximidamide
-
mutant S111R, presence of putrescine, 37C, pH 8.0
0.0006
5'-deoxy-5'-(N,N-dimethylamino)-8-methyladenosine
P17707
-
0.009
5'-deoxy-5'-(N,N-dimethylamino)adenosine
P17707
-
0.003
5'-deoxy-5'-dimethylsulfonio-8-methyladenosine chloride
P17707
-
0.015
5'-deoxy-5'-dimethylsulfonioadenosine chloride
P17707
-
0.00017
5'-deoxy-5'-[(2-hydrazinocarbonylethyl)methylamino]-8-methyladenosine
P17707
-
0.0015
5'-deoxy-5'-[(2-hydrazinocarbonylethyl)methylamino]-adenosine sulfate
P17707
-
0.157
5'-deoxy-5'-[(2-hydroxyamidinoethyl)methylamino]adenosine
P17707
-
0.031
5'-deoxy-5'-[(hydrazinocarbonylmethyl)methylamino]-8-methyladenosine
P17707
-
0.088
5'-[(2-aminoethyl)methylamino]-5'-deoxy-8-methyladenosine
P17707
-
0.000086
5'-[(2-aminooxyethyl)methylamino]-5'-deoxy-8-(methylamino)adenosine sulfate
P17707
-
0.000007
5'-[(2-aminooxyethyl)methylamino]-5'-deoxy-8-methyladenosine sulfate
P17707
-
0.000055
5'-[(2-aminooxyethyl)methylamino]-5'-deoxyadenosine
P17707
-
0.004
5'-[(2-carboxamidoethyl)methyamino]-5'-deoxy-8-ethyladenosine sulfate
P17707
-
0.0004
5'-[(2-carboxamidoethyl)methylamino]-5'-deoxy-8-methyladenosine sulfate
P17707
-
0.007
5'-[(2-carboxamidoethyl)methylamino]-5'-deoxyadenosine sulfate
P17707
-
0.44
5'-[(3-aminopropyl)methylamino]-5'-deoxy-8-(methylamino)adenosine sulfate
P17707
-
0.42
5'-[(3-aminopropyl)methylamino]-5'-deoxy-8-ethyladenosine sulfate
P17707
-
0.07
5'-[(3-aminopropyl)methylamino]-5'-deoxy-8-methyladenosine sulfate
P17707
-
0.5
5'-[(3-aminopropyl)methylamino]-5'-deoxyadenosine sulfate
P17707
-
0.000049
5'-[(4-aminooxybutyl)methylamino]-5'-deoxy-8-(methylamino)adenosine sulfate
P17707
-
0.000015
5'-[(4-aminooxybutyl)methylamino]-5'-deoxy-8-ethyladenosine sulfate
P17707
-
0.000005
5'-[(4-aminooxybutyl)methylamino]-5'-deoxy-8-methyladenosine sulfate
P17707
-
0.000011
5'-[(4-aminooxybutyl)methylamino]-5'-deoxy-8-oxoadenosine sulfate
P17707
-
0.000018
5'-[(4-aminooxybutyl)methylamino]-5'-deoxyadenosine sulfate
P17707
-
0.001
MDL73811
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0005
-
without activator
0.00126
-
-
0.088
-
native wild type AdoMetDC enzyme, in 50 mM KH2PO4 pH 7.5, 1 mM EDTA, 1 mM dithiothreitol, at 37C
0.102
-
-
0.11
Q9UWY8
pH 8.0, 70C
0.14
-
recombinant AdoMetDC enzyme, in 50 mM KH2PO4 pH 7.5, 1 mM EDTA, 1 mM dithiothreitol, at 37C
1.3
-
without activator
1.992
-
-
8
-
plus 2 mM 1,15-diamino-4,12-diazapentadecane; plus 2 mM 33-003
19
-
pus 2 mM YZ-33-050C
26
-
plus 2 mM PMW-2000-11-13-5
46
-
plus 2 mM YZ-33-046
79
-
plus 2 mM putrescine
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
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7
-
putrescine-stimulated enzyme
7.2 - 7.4
-
-
7.3 - 7.4
-
phosphate buffer
7.5 - 8
-
spermidine-stimulated enzyme
7.5
-
-
7.6
-
-
7.6
-
assay at
8
Q9UWY8
assay at
8.6
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.8 - 7.3
-
wild-type enzyme
7.2 - 7.8
-
K81A mutant
7.2 - 9.5
-
pH 7.2: about 45% of maximal activity, pH 9.5: about 65% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
assay at
40
-
-
70
Q9UWY8
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50 - 90
-
50C: about 45% of maximal activity, 90C: about 60% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
high level of OsSAMDC mRNA
Manually annotated by BRENDA team
-
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
-
incubaion of the cut flower with water increases both enzyme activity and spermine content 2fold, which are followed by ethylene production
Manually annotated by BRENDA team
D2K8S5
in olive flowers, SAMDC gene transcripts are highly expressed in ovary wall, placenta and ovules, whereas no labeling is seen in the vascular bundle
Manually annotated by BRENDA team
Q852S8, Q852S9
MdSAMDC1 is diferentially regulated in fruits depending on developmental stage and in cell suspension during the culture period, not induced by cold and salt stresses
Manually annotated by BRENDA team
Q852S8, Q852S9
MdSAMDC2 is induced by cold and salt stresses, MdSAMDC2 is not differentially regulated in fruits depending on developmental stage and in cell suspension during the culture period
Manually annotated by BRENDA team
-
moderate level of OsSAMDC mRNA
Manually annotated by BRENDA team
-
intermediate level of OsSAMDC mRNA
Manually annotated by BRENDA team
-
of growing healthy or virus-infected plants
Manually annotated by BRENDA team
O49972, Q42613, Q6QJ69, Q9SDM8
expression is low in young leafs and petioles, expression is upregulated differentially in response to stress such as chilling and exogenous 1-aminocyclopropane-1-carboxylic acid. Putrescine upregulates the expression of BjSAMDC1, spermidine and spermine down-regulates its expression
Manually annotated by BRENDA team
-
expression is low in young leaves and petioles, expression is upregulated differentially in response to stress such as chilling and exogenous 1-aminocyclopropane-1-carboxylic acid
Manually annotated by BRENDA team
-
high level of OsSAMDC mRNA
Manually annotated by BRENDA team
-
high level of OsSAMDC mRNA
Manually annotated by BRENDA team
-
regenerating liver and liver from sham-operated rats
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
-
high level of OsSAMDC mRNA
Manually annotated by BRENDA team
D2K8S5
nucellus, integuments and inner epidermis tissues of fertilized ovules
Manually annotated by BRENDA team
-
high levels of soluble SAMDCare found starting from the late uninucleate microspore stage, very high SAMDC activity is found in the wall residues of the aborted pollen
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
-
germination is accompanied by a rapid increase in enzyme activity and maximal activity occurs in 5-day-old seedlings
Manually annotated by BRENDA team
-
intermediate level of OsSAMDC mRNA
Manually annotated by BRENDA team
additional information
-
expression is high in reproductive organs
Manually annotated by BRENDA team
additional information
Q7XZQ9
similar levels of enzyme mRNA in all tissues tested
Manually annotated by BRENDA team
additional information
-
soluble SAMDC is absent in male-sterile anthers
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
from leaves of growing healthy or virus-infected plants
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Aquifex aeolicus (strain VF5)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
14000
-
estimated from amino acid sequence
703505
15000
-
estimated from amino acid sequence
703505
25000
-
gel filtration
4674
30000
-
PAGE
651672
30000
-
estimated from amino acid sequence
703505
32000
-
estimated from amino acid sequence
703505
33000
Q9UWY8
His10-tagged enzyme, gel filtration
719848
35000
-
gel filtration
651672
36000
-
gel filtration
4695
37000
-
estimated from amino acid sequence
701647
38000
-
estimated from amino acid sequence
703505
39000
-
estimated from amino acid sequence
703505
40000
-
estimated from amino acid sequence
703505
40200
Q841K9
gel filtration
728618
42000
-
estimated from amino acid sequence
703505
44000
-
liver, gel filtration
4679
44000
-
estimated from amino acid sequence
703505
46000
-
estimated from amino acid sequence
703505
47000
-
uterus, gel filtration
4679
52000
-
liver, sucrose density gradient centrifugation; prostate, gel filtration
4679
56000
-
gel filtration
4678
66000
-
gel filtration
4691
68000
-
gel filtration
4670, 4673
68000
-
gel filtration
4675
70000
O76240
gel filtration
653168
74000
-
sucrose density gradient centrifugation
4675
88000
-
non-denaturing PAGE
4668, 4671
88000
-
gel filtration
4694
108000
-
-
4668, 4672
115000
-
meniscus depletion method
4680
136000
-
gel filtration
4662
additional information
-
-
4668
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 32000, SDS-PAGE
?
-
x * 39600, proenzyme, x * 30600, alpha, + x * 8900, beta, SDS-PAGE
?
-
x * 46000, including His6-tag of recombinant protein, SDS-PAGE
?
O49972, Q42613, Q6QJ69, Q9SDM8
x * 40400, calculated from sequence
?
O49972, Q42613, Q6QJ69, Q9SDM8
x * 40500, calculated from sequence
?
O49972, Q42613, Q6QJ69, Q9SDM8
x * 40500, calculation from nucleotide sequence
?
O49972, Q42613, Q6QJ69, Q9SDM8
x * 40600, calculation from nucleotide sequence
?
-
x * 32000, SDS-PAGE of recombinant alpha subunit, including His-tag
?
D2K8S5
x * 39086, calculated from amino acid sequence
dimer
-
2 * 32500, SDS-PAGE
dimer
-
2 * 32000, SDS-PAGE
dimer
-
2 * 41000, SDS-PAGE
dimer
-
x-ray crystallography
dimer
Q9WZC3
x-ray crystallography
dimer
O66615
x-ray crystallography
dimer
Q9UWY8
2 * 16602, electrospray ionization mass spectrometry, 2 * 16680, calculated from sequence
dimer
-
2 * 16680, calculated from sequence
dimer
-
2 * 16602, electrospray ionization mass spectrometry, 2 * 16680, calculated from sequence
-
heterodimer
-
1 * 70000 + 1 * 9000, recombinant enzyme, SDS-PAGE
heterodimer
-
MALDI-TOF mass spectrometry
heterodimer
Trypanosoma brucei brucei Lab 110 EATRO
-
-
-
heterotetramer
-
2 * 6000, alpha, + 2 * 8000, beta, SDS-PAGE, 2 * 6793 * 2 * 6990, MALDI-TOF
hexamer
-
6 * 17000
homodimer
-
-
monomer
-
1 * 32000, SDS-PAGE
monomer
-
1 * 66000, SDS-PAGE
octamer
-
4 * 19000, alpha, + 4 * 14000, beta, (alphabeta)4 structure, SDS-PAGE
octamer
Escherichia coli HT527
-
4 * 19000, alpha, + 4 * 14000, beta, (alphabeta)4 structure, SDS-PAGE
-
tetramer
O02655
2 * 32000, alpha, + 2 * 10000, beta, SDS-PAGE
tetramer
-
2 * 32500, alpha, + 2 * 14600, beta, SDS-PAGE
tetramer
O76240
2 * 32000, alpha, + 2 * 10000, beta, SDS-PAGE, subunits derived from autocatalytically cleaved protein
tetramer
Acanthamoeba castellanii NEFF
-
2 * 32500, alpha, + 2 * 14600, beta, SDS-PAGE
-
monomer
Q841K9
1 * 40200, His6-tagged enzyme, SDS-PAGE
additional information
-
-
additional information
-
enzyme forms a four-layer alpha-beta-beta-alpha sandwich, crystallization data
additional information
A5HNV7
Trypanosoma brucei contains both a functional enzyme and a prozyme that has lost catalytic activity. The prozyme forms a high-affinity heterodimer with the enzyme that stimulates its activity up to 1200fold, the heterodimer is the functional enzyme in vivo
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
-
-
proteolytic modification
-
proenzyme of 39600 Da is cleaved to alpha subunit, 30600 Da, and beta subunit, 8900 Da
proteolytic modification
-
protein of 37000 Da is converted into the enzyme subunit of MW 32000. Putrescine accelerates the conversion
side-chain modification
P21182
alkylation of a Cys residue, mechanism-based suicide inactivation
proteolytic modification
-
the recombinant protein undergoes autocatalytic cleavage, generating a 33000-34000 Da alpha-subunit and a 9000 Da beta-subunit
proteolytic modification
O76240
autocatalytic processing of 42000 Da protein to 32000 + 10000 Da
proteolytic modification
-
processing does not require putrescine
additional information
O66615
AdoMetDC is expressed as an inactive proenzyme that undergoes autoprocessing to the active enzyme. The autoprocessing involves an internal serinolysis reaction leading to the cleavage of the backbone to alpha and beta subunits with the latter being the smaller subunit and to generation of a pyruvoyl group at the N-terminus of the alpha chain
proteolytic modification
O02655
alpha-subunit, 32000 Da, and beta-subunit, 10000 Da, are derived from cleavage of the proenzyme. The mRNA has an unusually long 5'-untranslated region of 477 nucleotides. This region has a small open reading frame, which can encode a putative peptide of 17000 residues
additional information
-
half-life of enzyme is about 3 min
side-chain modification
-
alkylation of Cys140, mechanism-based suicide inactivation
additional information
-
AdoMetDC is expressed as an inactive proenzyme that undergoes autoprocessing to the active enzyme. The autoprocessing involves an internal serinolysis reaction leading to the cleavage of the backbone to alpha and beta subunits with the latter being the smaller subunit and to generation of a pyruvoyl group at the N-terminus of the alpha chain
side-chain modification
-
alkylation of a Cys residue, mechanism-based suicide inactivation
additional information
-
AdoMetDC is expressed as an inactive proenzyme that undergoes autoprocessing to the active enzyme. The autoprocessing involves an internal serinolysis reaction leading to the cleavage of the backbone to alpha and beta subunits with the latter being the smaller subunit and to generation of a pyruvoyl group at the N-terminus of the alpha chain
additional information
Q9WZC3
AdoMetDC is expressed as an inactive proenzyme that undergoes autoprocessing to the active enzyme. The autoprocessing involves an internal serinolysis reaction leading to the cleavage of the backbone to alpha and beta subunits with the latter being the smaller subunit and to generation of a pyruvoyl group at the N-terminus of the alpha chain
additional information
-
AdoMetDC is expressed as an inactive proenzyme that undergoes autoprocessing to the active enzyme. The autoprocessing involves an internal serinolysis reaction leading to the cleavage of the backbone to alpha and beta subunits with the latter being the smaller subunit and to generation of a pyruvoyl group at the N-terminus of the alpha chain
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 22C in 13-16% PEG 8000, 100 mM Tris, pH 8.0-9.0, and 10 mM dithiothreitol
P17707
cocrystallized with 5'-deoxy-5'-dimethylthioadenosine and 5'-deoxy-5'-(N-dimethyl)amino-8-methyladenosine, hanging drop vapor diffusion method, at 22C 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
-
hanging drop vapour diffusion method, structures of the wild-type proenzyme and the S63A mutant at 1.55 A and 1.7 A resolution
-
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
Q9WZC3
molecular modeling using enzymes from Solanum tuberosum and Homo sapiens as templates
Q7XZQ9
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4
-
5C, 3 days, complete loss of activity
4674
7 - 8
-
5C, 3 days, stable
4674
9
-
5C, 3 days, complete loss of activity
4674
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
rapid loss of activity
4671
47
-
10 min, 50% loss of activity
4693
50
-
16 h, stable
4695
50
-
half-life 8 min
651827
55
-
the activity of AdoMetDC incubated at 37C for 1 h in the absence of putrescine is decreased by 55%
714391
60
-
half-life 1.15 min
651827
70
-
16h, 20% loss of activity
4695
70
-
3 h, full stability
651672
70
-
half-life 1.01 min
651827
100
-
1 h, 80% loss of activity
4695
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
rapid inactivation by low ionic strength or dialysis in the absence of EDTA
-
freezing inactivates
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, stable for at least 2 months
-
4C, stable for up to 2 weeks
-
4C, 10 mM Tris-HCl buffer, pH 7.6, in presence of 0.4 M NaCl and 0.01% deoxycholate, stable for at least 1 month
-
-20C, native wild type enzyme, 2 weeks, 55% loss of activity
-
4C and -20C, recombinant enzyme, 2 weeks, no loss of activity
-
4C, native wild type enzyme, 2 weeks, 16% loss of activity
-
0-2C, in presence of putrescine, stable for at least 6 weeks
-
2C, without putrescine, 80% loss of activity after 14 h
-
-20C, 20 mM Tris-HCl, 1 mM EDTA, pH 7.4, stable for up to 2 months
-
-70C, rapid loss of activity
-
2C, stable for 3 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme, expression in Escherichia coli
-
large-scale
-
Ni2+-agarose column chromatography
-
recombinant alpha subunit
-
TALON metal affinity resin column chromatography
-
Talon metal affinity resin column chromatography and Sephadex G-75 gel filtration
P17707
IMAC column chromatography and Superdex 75 gel filtration
Q25264
after expression in Escherichia coli
-
Strep-Tactin affinity chromatography
-
Ni-NTA column chromatography, and gel filtration
Q841K9
Ni-NTA column chromatography, gel filtration
Q9WZC3
Ni2+-agarose column chromatography
-
recombinant enzyme
-
recombinant enzyme, expressed in Escherichia coli
O76240
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
cDNA of Datura stramonium is introduced in Nicotiana tabacum L. cv. Xanthi in antisense orientation under the CaMV 35S promoter, by means of Agrobacterium tumefaciens and leaf disc transformation. Primary transformants efficiently transcribe the antisense SAMDC gene, but SAMDC activity and PA titers do not change. By contrast, in most transgenic shoots of the second generation, SAMDC activity is remarkably lower than in controls, and the putrescine-to-spermidine ratio is altered, mainly due to increased putrescine, even though putrescine oxidising activity (diamine oxidase, EC 1.4.3.6) does not change relative to controls. Despite the reduction in SAMDC activity, the production of ethylene, which shares with PAs the common precursor SAM, is not influenced by the foreign gene. Some plants are transferred to pots and acclimatised in a growth chamber. In these in vivo-grown second generation transgenic plants, at the vegetative stage, SAMDC activity is scarcely reduced, and PA titres do not change. Finally, the rhizogenic potential of in vitro-cultured leaf explants excised from antisense plants is significantly diminished as compared with WTones, and the response to methyl jasmonate, a stress-mimicking compound, in terms of PA conjugation, is higher and differentially affected in transgenic leaf discs relative to WT ones
Q96555
expressed in Oryza sativa
-
expressed in Oryza sativa subspecies Japonica cultivar EYI105
Q96555
expression in Nicotiana tabacum
-
enzyme alpha subunit, expression in Escherichia coli
-
expressed in Amdc-s cells (NIH3T3 cells transfected with human AdoMetDC cDNA)
-
expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) JM109 cells
P17707
expressed in Escherichia coli JM109 cells
-
expression in Escherichia coli
-
expression in sense and antisense orientations in mouse NIH3T3 cells
-
expressed in Saccharomyces cerevisiae strain INVSc2 using the expression vector pYES-DEST52
-
expressed in Escherichia coli TG1 cells
Q25264
;
Q852S8, Q852S9
expression in Escherichia coli
P0DMN7
expression in Escherichia coli
-
expressed in Escherichia coli BL21 Star cells
-
expressed in Solanum lycopersicum cultivar Ohio 8245 fruit
-
expressed in Solanum lycopersicum plants
-
expressed in Escherichia coli BL21 cells
Q841K9
expression in Escherichia coli
Q9UWY8
expression in Arabidopsis thaliana Heynh. under the control of the cauliflower mosaic virus 35S promoter. The overexpression causes unusual visible phenotypes to various extents in transformants grown on agar plates containing sucrose. In transformants the contents of certain amino acids of the aspartic and glutamic families are markedly increased, while those of aromatic amino acids are significantly decreased
-
expressed in Escherichia coli B834(DE3) cells
Q9WZC3
expressed in Escherichia coli
-
expressed in Escherichia coli Top10 cells
-
expression in Escherichia coli
-
microinjection of 1 ng of SAMDC mRNA per egg results in more than 200fold overexpression of the mRNA
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
SAMDC is active early during pollen hydration and germination in vitro
-
AdoMetDC is negatively regulated by spermidine and spermine
-
transcriptional levels of SAMDC in shoots are enhanced by treatment with 10% (w/v) polyethylene glycol. The steady state level of SAMDC mRNA varies in genotypes with varying levels of tolerance to salinity or to low temperature stress
-
AdoMetDC is negatively regulated by spermidine and spermine
-
exogenous methyl jasmonate transiently inhibits the expression of Samdc gene in the polyamine biosynthesis pathway, the level of Samdc1 mRNA falls by 50% after 6 h exposure to 0.2 mM methyl jasmonate, but returns to near initial levels after 48 h
-
the levels of SAMDC1 mRNA are reduced after 3 d of drought stress, but after 6 d of stress and throughout the recovery period, steady-state SAMDC1 mRNA levels return to normal
Q96555
AdoMetDC is negatively regulated by spermidine and spermine
-
in barley cultivar Sahara, expression of SAMDC is up-regulated 1.7times by boron treatment surpassing the expression level in cultivar Clipper under boron condition. In cultivar Clipper, the gene is up-regulated 1.1fold
-
AdoMetDC is negatively regulated by spermidine and spermine
-
during early fruit development, SAMDC transcript levels decline relative to the basal closed flower level at 7 days post anthesis A in both cultivars Arbequina and Picual. From 14 to 28 days post anthesis, SAMDC mRNA levels decrease to 50% in cultivar Arbequina fruit
D2K8S5
at flower opening, SAMDC transcript levels rise 40fold and 5fold in comparison with those observed in the closed flower of olive cultivars Arbequina and Picual, respectively. The SAMDC mRNA accumulates at a constant level from 7 to 28 days post anthesis in cultivar Picual fruit and from 7 to 14 days post anthesis in cultivar Arbequina fruit
D2K8S5
the levels of SAMDC1 mRNA are reduced after 3 d of drought stress, but after 6 d of stress and throughout the recovery period, steady-state SAMDC1 mRNA levels return to normal
Q0JC10
AdoMetDC is negatively regulated by spermidine and spermine
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the steady-state protein level of AdoMetDC is unaffected by alpha-difluoromethylornithine treatment
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AdoMetDC is negatively regulated by spermidine and spermine
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in all leaf areas, the biosynthetic enzyme activity of SAMDC sharply decreases with leaf age
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C230A
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minimal effect on caqtalytic activity
C230A
-
minimal effect on catalytic activity, thermally unstable, higher alpha-helix content and lower coiled-coil content than wild type
C50A
-
minimal effect on caqtalytic activity
C50A
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minimal effect on catalytic activity, thermally unstable, higher alpha-helix content and lower coiled-coil content than wild type
C83A
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10% residual enzymic activity
K81A
-
60% residual enzymic activity, altered substrate specificity
D190N
-
reduced activation by putrescine, spermidine or spermine
E194Q
-
strongly enhanced basic activity, little activation by putrescine, spermidine or spermine
E274Q
-
slightly enhanced basic activity, reduced activation by putrescine, spermidine or spermine
E33Q
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drastically reduced activation by putrescine, no activation by spermidine or spermine, no complete processing of pro-protein
K95A
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no activation, no complete processing of pro-protein
R91A
-
drastically reduced activation by putrescine, spermidine or spermine, no complete processing of pro-protein
S128A
-
drastically reduced activation by putrescine, spermidine or spermine
S83A
-
no activation, no processing of pro-protein
C82A
-
reduced enzymic activity, no inhibition by iodoacetic acid
C82A
-
the mutant shows decreased kcat compared to the wild type enzyme
C505S
-
the expression level and specific activity of the mutant is unchanged compared to the wild type enzyme. The mutant protein occurs mainly as a monomer
K15A
-
mutant enzyme is 50% less active compared to wild-type
R11L
-
mutant enzyme is almost inactive
M37F
Q841K9
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
M37W
Q841K9
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
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
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
K81A
-
6fold higher substrate specificity with lysine, higher pH-optimum
additional information
Q3E9D5
enzyme deletion results in bushy and dwarf mutant plants, with enlarged vascular systems in inflorescences, roots and petioles, and an altered homeostasis of polyamines. The double mutant of bud2 and samdc1, another S-adenosylmethionine decarboxylase, is embryo lethal
T192A
-
slightly enhanced basic activity, reduced activation by putrescine, spermidine or spermine
additional information
-
overexpression of enzyme in tobacco results in accumulation of polyamines in transgenic plants. Transgenic tobacco does not show any difference in organ phenotype compared to wild-type. The number and weight of seeds increases, and net photosynthetic rate also increases. Abiotic stress-induced damage is attenuated in transgenic plants
H243A
-
the mutation traps the enzyme in the ester form
additional information
-
adenovirus-mediated expression of both antisense ornithine decarboxylase and S-adenosylmethionine decarboxylase in lung cancer cell line A-549. Antisense enzyme expression inhibits tumor cell growth through blocking the polyamine synthesis pathway. Tumor cells are arrested at G1 phase and invasivness is reduced
additional information
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adenovirus-mediated expression of both antisense ornithine decarboxylase and S-adenosylmethionine decarboxylase significantly induces G1 arrest, decreases levels of cyclin D1 protein and mRNA and suppresses the promoter activity. Antisense ornithine decarboxylase and S-adenosylmethionine decarboxylase also inhibit nuclear translocation of beta-catenin
additional information
-
suppression of enzyme expression in HL-60 cells by RNAi results in overproduction of reactive oxygen species, leading to growth defect and partial cell death. Reactive oxygen species is caused by a decrease of the total glutathione and the ratio of reduced to oxidized glutathione, and by an increase of the intracellular iron uptake
S68A
-
themutant lacks the hydroxyl group necessary for processing and traps the enzyme in a form similar to the proenzyme
additional information
-
targeted disruption of enzyme gene, heterozygous animals were viable, normal and fertile, homozygous embryos died early in embryonic development, homozygous blastocysts at E3.5 arrested cell proliferation which was rescued by addition of spermidine
K215A
-
mutant enzyme is 50% less active compared to wild-type
additional information
Q9U8D4
deletion of parasite-specific regions, analysis of influence on catalytic activities and domain interactions, co-incubation of monofunctional heterotetrameric S-adenosyl-L-methionine decarboxylase domain with monofunctional, homodimeric ornithine decarboxylase domain produces an active hybrid complex of 330,000 Da
M37Y
Q841K9
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
additional information
Q9UWY8
modeling and activity of a chimeric arginine decarboxylase/S-adenosylmethionine decarboxylase proteins. A chimeric protein containing the beta subunit of arginine decarboxylase (SSO0536) and the alpha subunit of S-adenosylmethionine decarboxylase (SSO0585) has arginine decarboxylase activity and no S-adenosylmethionine decarboxylase activity, implicating residues responsible for substrate specificity in the beta subunit
additional information
-
modeling and activity of a chimeric arginine decarboxylase/S-adenosylmethionine decarboxylase proteins. A chimeric protein containing the beta subunit of arginine decarboxylase (SSO0536) and the alpha subunit of S-adenosylmethionine decarboxylase (SSO0585) has arginine decarboxylase activity and no S-adenosylmethionine decarboxylase activity, implicating residues responsible for substrate specificity in the beta subunit
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S111R
-
residue in putrescine binding site, reduced catalytic activity
additional information
Q7XZQ9
expression without the two upstream ORFs results in 50fold increase in activity compared to expression of full length DNA
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
dialysis of salicylaldehyde inactivated enzyme restores
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pharmacology
O02655
potentially important drug target for the chemotherapy of proliferative and parasitic diseases
biotechnology
Q96555
overexpression of enzyme is sufficient for accumulation of spermidine in leaves and spermidine and spermine in seeds
medicine
-
S-adenosyl methionine decarboxylase activity is required for the outcome of herpes simplex virus type 1 infection and represents a new potential therapeutic target, inhibition of the enzyme by methylglyoxal bis(guanylhydrazone) prevents HSV-1 infection
medicine
-
adenovirus-mediated expression of both antisense ornithine decarboxylase and S-adenosylmethionine decarboxylase in lung cancer cell line A-549. Antisense enzyme expression inhibits tumor cell growth through blocking the polyamine synthesis pathway. Tumor cells are arrested at G1 phase and invasivness is reduced
medicine
-
enzyme inhibitor (2E)-2-[4-[amino(imino)methyl]-2,3-dihydro-1H-inden-1-ylidene]hydrazinecarboximidamide, i.e. CGP48664A, SAM486A, suppresses HIV-1 replication, including the replication of viruses that are resistant to multiple reverse transcriptase and protease inhibitos. Antiretroviral effect is based on the fact that regulatory protein Rev activity is severely compromised in drug-treated cells. No toxic effects on cellular metabolism are observed
medicine
-
essential role of enzyme in embryonic development, polyamines are required for cell proliferation after E3.5
pharmacology
-
the enzyme is a target for cancer chemotherapy
pharmacology
-
potential target for therapeutic agents against various parasitic diseases and proliferating disorders
pharmacology
-
potentially important target for chemotherapy of filiarial infection
agriculture
-
incubation of the cut flower with water increases both enzyme activity and spermine content 2fold, which are followed by ethylene production. Reaction may be a resistance mechanism against fungal and bacterial infection. Overexpression of enzyme may be a tool to improve rose cultivars for the common usage