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Information on EC 4.1.1.50 - adenosylmethionine decarboxylase and Organism(s) Caenorhabditis elegans

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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:
Caenorhabditis elegans
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Word Map
The taxonomic range for the selected organisms is: Caenorhabditis elegans
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
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
putrescine
-
enhances activity up to 350fold
spermidine
-
250fold increase of catalytic activity at 2 mM
spermine
-
90fold increase of catalytic activity at 2 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.115 - 1
S-adenosyl-L-methionine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0005
-
without activator
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DCAM_CAEEL
368
0
42143
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10000
2 * 32000, alpha, + 2 * 10000, beta, SDS-PAGE
32000
2 * 32000, alpha, + 2 * 10000, beta, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
2 * 32000, alpha, + 2 * 10000, beta, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
-
drastically reduced activation by putrescine, no activation by spermidine or spermine, no complete processing of pro-protein
K95A
-
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
T192A
-
slightly enhanced basic activity, reduced activation by putrescine, spermidine or spermine
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pharmacology
potentially important drug target for the chemotherapy of proliferative and parasitic diseases
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Da'dara, A.A.; Walter, R.D.
Molecular and biochemical characterization of S-adenosylmethionine decarboxylase from free-living nematode Caenorhabditis elegans
Biochem. J.
336
545-550
1998
Caenorhabditis elegans (O02655), Caenorhabditis elegans
Manually annotated by BRENDA team
Ndjonka, D.; Da'dara, A.; Walter, R.D.; Luersen, K.
Caenorhabditis elegans S-adenosylmethionine decarboxylase is highly stimulated by putrescine but exhibits a low specificity for activator binding
Biol. Chem.
384
83-91
2003
Caenorhabditis elegans
Manually annotated by BRENDA team