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Information on EC 4.1.1.50 - adenosylmethionine decarboxylase and Organism(s) Arabidopsis thaliana and UniProt Accession Q3E9D5

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.50 adenosylmethionine decarboxylase
IUBMB Comments
The Escherichia coli enzyme contains a pyruvoyl group.
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This record set is specific for:
Arabidopsis thaliana
UNIPROT: Q3E9D5
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Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
Synonyms
s-adenosylmethionine decarboxylase, adometdc, samdc, s-adenosyl-l-methionine decarboxylase, adenosylmethionine decarboxylase, adomet decarboxylase, s-adenosyl methionine decarboxylase, sam-dc, sam decarboxylase, pfadometdc, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
AdoMetDC
-
-
-
-
AMDC
-
-
-
-
S-Adenosyl-L-methionine decarboxylase
-
-
-
-
S-Adenosylmethionine decarboxylase
-
-
-
-
SAM decarboxylase
-
-
-
-
SAMDC
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine carboxy-lyase [(5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium-salt-forming]
The Escherichia coli enzyme contains a pyruvoyl group.
CAS REGISTRY NUMBER
COMMENTARY hide
9036-20-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine
(5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt + CO2
show the reaction diagram
-
-
?
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
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
MDL73811
7% residual activity at 0.001 mM
methylglyoxal bis-(guanylhydrazone)
-
Salicylaldehyde
inactivation, substrate protects
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.023
S-adenosyl-L-methionine
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00015
methylglyoxal bis-(guanylhydrazone)
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8 - 7.3
wild-type enzyme
7.2 - 7.8
K81A mutant
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform Bud2
Uniprot
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DCAM4_ARATH
347
0
39039
Swiss-Prot
other Location (Reliability: 1)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C230A
C83A
10% residual enzymic activity
additional information
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
half-life 8 min
60
half-life 1.15 min
70
half-life 1.01 min
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme, expression in Escherichia coli
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
dialysis of salicylaldehyde inactivated enzyme restores
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Park, S.J.; Cho, Y.D.
Identification of functionally important residues of Arabidopsis thaliana S-adenosylmethionine decarboxylase
J. Biochem.
126
996-1003
1999
Arabidopsis thaliana (Q96286), Arabidopsis thaliana
Manually annotated by BRENDA team
Park, S.J.; Cho, Y.D.
Studies on the active site of the Arabidopsis thaliana S-adenosylmethionine decarboxylase: Lys81 residue involvement in catalytic activity
J. Biochem. Mol. Biol.
33
69-74
2000
Arabidopsis thaliana (Q96286)
-
Manually annotated by BRENDA team
Park, S.J.; Cho, Y.D.
Structural roles of cysteine 50 and cysteine 230 residues in Arabidopsis thaliana S-adenosylmethionine decarboxylase
J. Biochem. Mol. Biol.
35
178-185
2002
Arabidopsis thaliana (Q96286), Arabidopsis thaliana
Manually annotated by BRENDA team
Hu, W.W.; Gong, H.; Pua, E.C.
The pivotal roles of the plant S-adenosylmethionine decarboxylase 5' untranslated leader sequence in regulation of gene expression at the transcriptional and posttranscriptional levels
Plant Physiol.
138
276-286
2005
Arabidopsis thaliana
Manually annotated by BRENDA team
Ge, C.; Cui, X.; Wang, Y.; Hu, Y.; Fu, Z.; Zhang, D.; Cheng, Z.; Li, J.
BUD2, encoding an S-adenosylmethionine decarboxylase, is required for Arabidopsis growth and development
Cell Res.
16
446-456
2006
Arabidopsis thaliana (Q3E9D5)
Manually annotated by BRENDA team