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Information on EC 4.1.1.50 - adenosylmethionine decarboxylase and Organism(s) Solanum tuberosum and UniProt Accession Q04694

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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:
Solanum tuberosum
UNIPROT: Q04694
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Word Map
The taxonomic range for the selected organisms is: Solanum tuberosum
The enzyme appears in selected viruses and cellular organisms
Synonyms
s-adenosylmethionine decarboxylase, adometdc, samdc, s-adenosyl-l-methionine decarboxylase, adenosylmethionine decarboxylase, adomet decarboxylase, s-adenosyl methionine decarboxylase, sam-dc, sam decarboxylase, pfadometdc, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S-Adenosylmethionine decarboxylase
-
AdoMet decarboxylase
-
-
AdoMetDC
AMDC
-
-
-
-
S-Adenosyl-L-methionine decarboxylase
S-Adenosylmethionine decarboxylase
SAM decarboxylase
SAMDC
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine carboxy-lyase [(5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium-salt-forming]
The Escherichia coli enzyme contains a pyruvoyl group.
CAS REGISTRY NUMBER
COMMENTARY hide
9036-20-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine
(5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt + CO2
show the reaction diagram
-
-
-
?
(5-deoxy-5-adenosyl)(3-aminopropyl)-methylsulfonium + CO2
S-adenosyl-L-methionine + H+
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine
(5-deoxy-5-adenosyl)(3-aminopropyl)methylsulfonium salt + CO2
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
thiamine diphosphate
-
pyridoxal 5'-phosphate
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
does not require Mg2+ for activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-amidinoindan-1-one-2'-amidinohydrazone
-
5'-deoxy-5'-(dimethyl-sulfonio)adenosine
-
5'-deoxy-5'-(N-dimethyl)amino-8-methyl adenosine
-
5'-deoxy-5'-[N-methyl-N-(3-hydrazino-propyl)amino]adenosine
-
5'-deoxy-5'-[N-methyl-N-[(2-aminooxy)-ethyl]amino]adenosine
-
CGP48664A
i.e. 4-amidinoindan-1-one-2'-amidinohydrazone
methylglyoxalbis(guanylhydrazone)
-
(S)-(5'-deoxy-5'-adenosyl)methylthioethylhydroxylamine
-
-
5'-deoxy-5'-dimethylsulfonio-8-methyladenosine
-
-
5'-deoxy-5'-[(2-aminooxyethyl)methylamino]adenosine
-
-
5'-Deoxy-5'-[(3-hydrazinopropyl)methylamino]adenosine
-
-
5'-[[(Z)-4-amino-2-butenyl]methylamino]-5'-deoxyadenosine
-
MDL 73811
Genz-644131
-
i.e. 5'-[[(Z)-4-amino-2-butenyl]methylamino]-5'-deoxy-8-methyladenosine
methylglyoxal bis(guanylhydrazone)
-
-
SAM486A
-
previously described as CGP4864A, i.e. 4-amidinoindan-1-one-2'-amidinohydrazone
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DCAM_SOLTU
360
0
39726
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
-
estimated from amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
x-ray crystallography
heterodimer
-
x-ray crystallography
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
AdoMetDC is negatively regulated by spermidine and spermine
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bennett, E.M.; Ekstrom, J.L.; Pegg, A.E.; Ealick, S.E.
Monomeric S-adenosylmethionine decarboxylase from plants provides an alternative to putrescine stimulation
Biochemistry
41
14509-14517
2002
Solanum tuberosum (Q04694), Solanum tuberosum
Manually annotated by BRENDA team
Kim, J.H.; Kim, H.S.; Lee, Y.H.; Kim, Y.S.; Oh, H.W.; Joung, H.; Chae, S.K.; Suh, K.H.; Jeon, J.H.
Polyamine biosynthesis regulated by StARD expression plays an important role in potato wound periderm formation
Plant Cell Physiol.
49
1627-1632
2008
Solanum tuberosum
Manually annotated by BRENDA team
Bale, S.; Ealick, S.E.
Structural biology of S-adenosylmethionine decarboxylase
Amino Acids
38
451-460
2010
Trypanosoma brucei, Aquifex aeolicus (O66615), Aquifex aeolicus, Homo sapiens (P17707), Homo sapiens, Solanum tuberosum (Q04694), Solanum tuberosum, Thermotoga maritima (Q9WZC3), Thermotoga maritima
Manually annotated by BRENDA team
Pegg, A.E.
S-Adenosylmethionine decarboxylase
Essays Biochem.
46
25-45
2009
Bacillus subtilis, Saccharomyces cerevisiae, Catharanthus roseus, Clostridium acetobutylicum, Escherichia coli, Homo sapiens, Methanocaldococcus jannaschii, Solanum tuberosum, Thermotoga maritima, Trypanosoma brucei, Trypanosoma cruzi
Manually annotated by BRENDA team