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Information on EC 4.1.1.19 - arginine decarboxylase and Organism(s) Avena sativa and UniProt Accession P22220
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4.1.1.19 arginine decarboxylaseIUBMB Comments
A pyridoxal-phosphate protein.
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Word Map
- 4.1.1.19
- polyamine
- putrescine
- ornithine
- spermidine
- s-adenosylmethionine
- arginase
-
diamine
- samdc
- decarboxylases
- agmatinase
- deiminase
- alpha-difluoromethylornithine
- cadaverine
-
imidazoline
- d-arginine
- pao
-
3.5.3.1
-
iminohydrolase
-
arginine-dependent
-
scots
-
ureohydrolase
- difluoromethylornithine
-
pyrogenic
- drug development
- agriculture
- hyoscyamine
- trifoliata
- poncirus
- speb
-
tropane
- dl-alpha-difluoromethylornithine
- antizyme
- datura
The taxonomic range for the selected organisms is: Avena sativa
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
arginine decarboxylase, spea2, argdc, spea1, biosynthetic arginine decarboxylase, ppadc, l-arginine decarboxylase, pyruvoyl-dependent arginine decarboxylase, atadc2, ptadc, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ADC
-
-
-
-
ARGDC
-
-
-
-
bADC
-
-
-
-
Biosynthetic arginine decarboxylase
-
-
-
-
dADC
-
-
-
-
Decarboxylase, arginine
-
-
-
-
L-Arginine decarboxylase
-
-
-
-
Synthetic arginine decarboxylase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
L-arginine carboxy-lyase (agmatine-forming)
A pyridoxal-phosphate protein.
CAS REGISTRY NUMBER
COMMENTARY
9024-77-5
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-arginine
agmatine + CO2
first reaction of a putrescine synthetic pathway found in bacteria and plants
-
-
?
L-arginine
agmatine + CO2
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in abiotic stress response
-
-
?
L-arginine
agmatine + CO2
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in stress response
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-arginine
agmatine + CO2
first reaction of a putrescine synthetic pathway found in bacteria and plants
-
-
?
L-arginine
agmatine + CO2
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in abiotic stress response
-
-
?
L-arginine
agmatine + CO2
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in stress response
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
ADC belongs to the group IV pyridoxal 5'-phosphate-dependent decarboxylases
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
MG-132
ADC proteins are degraded by ubiquitin-dependent mechanisms carried out by 26S proteasome, the major degradation pathway for soluble proteins. Experiments carry out with ADC-transgenic cultures of Trypanosoma cruzi incubated with the peptide aldehyde proteasome inhibitor MG-132 show a marked increase of ADC activity probably due to the reduction of the enzyme turnover rate as shown after blocking protein synthesis with cycloheximide.
pyridoxal 5'-phosphate
-
recombinant enzyme, extracts from Trypanosoma cruzi have an about six times higher activity in the presence of pyridoxal 5-phosphate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
To ascertain whether the ADC enzyme expressed in transgenic Trypanosoma cruzi has a modified metabolic turnover when attached to the His-tag, cycloheximide is added to parasite cultures transformed with plasmids to stop protein synthesis. ADC half-life inside the parasite is 150 min, the enzyme attached to the His-tail is more stable, with a half-life of about 14 h.
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
enzyme activities of extracts obtained from ADC or ADCH-transfected parasites are higher in the presence of oxidized glutathione than under reducing conditions with dithiothreitol in the reaction mixture
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SPE1_AVESA
607
0
66706
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
24000
1 * 42000 + 1 * 24000, determined by SDS-polyacrylamide gel electrophoresis
42000
1 * 42000 + 1 * 24000, determined by SDS-polyacrylamide gel electrophoresis
66000
inactive precursor protein, active recombinant ADC is formed in vivo by a complex of two His-tagged polypeptide chains of 42 and 24 kDa by a subsequent incubation during different times with extracts of Arabidopsis seedlings which contain a proteolytic activity, processing of oat ADC does not require a specific protease
115000
-
presence of 5 different enzymatic active and immunoreactive molecular forms of ADC with MW of 195000 Da, 115000 Da, 66000 Da, 38000 Da and 23000 Da, gel filtration
195000
-
presence of 5 different enzymatic active and immunoreactive molecular forms of ADC with MW of 195000 Da, 115000 Da, 66000 Da, 38000 Da and 23000 Da, gel filtration
23000
-
presence of 5 different enzymatic active and immunoreactive molecular forms of ADC with MW of 195000 Da, 115000 Da, 66000 Da, 38000 Da and 23000 Da, gel filtration
38000
-
presence of 5 different enzymatic active and immunoreactive molecular forms of ADC with MW of 195000 Da, 115000 Da, 66000 Da, 38000 Da and 23000 Da, gel filtration
66000
-
presence of 5 different enzymatic active and immunoreactive molecular forms of ADC with MW of 195000 Da, 115000 Da, 66000 Da, 38000 Da and 23000 Da, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterodimer
1 * 42000 + 1 * 24000, determined by SDS-polyacrylamide gel electrophoresis
additional information
-
the full-length 66000 MW arginine decarboxylase polypeptide is synthesized and then cleaved to produce a 42000 MW polypeptide containing the original terminus and a 24000 polypeptide containing the original carboxyl terminus. Both of these are found in the enzyme and held together by disulfide bonds
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
post-translational proteolysis of ADC depends on the presence of a protease-sensitive loop in the structure of the protein
proteolytic modification
-
the protein is synthesized as a 66000 Da precursor that is proteolytically processed into two polypeptides of 42000 and 24000 da
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ADC protein attached to the six-His tag at the C-terminal end is purified from parasite extracts by immobilized metal affinity chromatography through a Ni2+-agarose column
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
oat enzyme is expressed in Trypanosoma cruzi epimastigotes after transfection with a C-terminal six-His tag and as untagged enzyme, active ADC is expressed in the parasites and the primary translational product is cleaved into 2 polypeptides through a proteolytic process. When the his-tag is added to the C-terminal end of ADC it causes very significant changes on the metabolic stability and catalytic parameters of the heterologous enzyme expressed in the transformed parasites.
expressed in Trypanosoma cruzi, which lacks arginine decarboxylase in wild type
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Birecka, H.; Bitonti, A.J.; McCann, P.P.
Activities of arginine and ornithine decarboxylases in various plant species
Plant Physiol.
79
515-519
1985
Avena sativa, Heliotropium angiospermum, Heliotropium indicum, Heliotropium procumbens, Heliotropium spathulatum, Hordeum vulgare, Lactuca sativa, Phaseolus vulgaris, Pisum sativum, Zea mays
Smith, T.A.
Arginine decarboxylase (oat seedlings)
Methods Enzymol.
94
176-180
1983
Avena sativa
-
Smith, T.A.
Arginine decarboxylase of oat seedlings
Phytochemistry
18
1447-1452
1979
Avena sativa
-
Smith, T.A.; Ng, W.Y.
Determination and purification of arginine decarboxylase from oat seedlings
Biochem. Soc. Trans.
7
391-393
1979
Avena sativa
Malmberg, R.L.; Smith, K.E.; Bell, E.; Cellino, M.L.
Arginine decarboxylase of oats is clipped from a precursor into two polypeptides found in the soluble enzyme
Plant Physiol.
100
146-152
1992
Avena sativa
Ruiz, O.A.; Bortolotti, C.; Masgrau, C.; Tiburcio, A.F.; Altabella, T.
Molecular forms of arginine decarboxylase in oat leaves
Physiol. Plant.
108
370-375
2000
Avena sativa
-
Carrillo, C.; Serra, M.P.; Pereira, C.A.; Huber, A.; Gonzalez, N.S.; Algranati, I.D.
Heterologous expression of a plant arginine decarboxylase gene in Trypanosoma cruzi
Biochim. Biophys. Acta
1674
223-230
2004
Avena sativa
Chiesa, M.A.; Ruiz, O.A.; Sanchez, D.H.
Lotus hairy roots expressing inducible arginine decarboxylase activity
Biotechnol. Lett.
26
729-733
2004
Avena sativa
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