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Information on EC 4.1.1.19 - arginine decarboxylase and Organism(s) Oryza sativa and UniProt Accession Q9SNN0

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.19 arginine decarboxylase
IUBMB Comments
A pyridoxal-phosphate protein.
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Select one or more organisms in this record: ?
This record set is specific for:
Oryza sativa
UNIPROT: Q9SNN0
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Word Map
The taxonomic range for the selected organisms is: Oryza sativa
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
arginine decarboxylase, spea2, argdc, spea1, biosynthetic arginine decarboxylase, ppadc, pyruvoyl-dependent arginine decarboxylase, atadc2, l-arginine decarboxylase, ptadc, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ADC
-
-
-
-
ARGDC
-
-
-
-
bADC
-
-
-
-
Biosynthetic arginine decarboxylase
-
-
-
-
dADC
-
-
-
-
Decarboxylase, arginine
-
-
-
-
L-Arginine decarboxylase
-
-
-
-
Synthetic arginine decarboxylase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
L-arginine carboxy-lyase (agmatine-forming)
A pyridoxal-phosphate protein.
CAS REGISTRY NUMBER
COMMENTARY hide
9024-77-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-arginine
agmatine + CO2
show the reaction diagram
L-Arg
?
show the reaction diagram
-
regulatory role in growth and cell division
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-arginine
agmatine + CO2
show the reaction diagram
L-Arg
?
show the reaction diagram
-
regulatory role in growth and cell division
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
-
cofactor
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-arginine
-
agmatine
-
10 mM, 57% inhibition
canavanine
-
-
hydroxylamine
-
-
methylglyoxal bisguanylhydrazone
-
-
Pyridoxine-HCl
-
-
spermidine
-
-
spermine
-
-
urethane
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
gibberellic acid
-
stimulates
indoleacetic acid
-
stimulates
kinetin
-
stimulates
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.28
L-Arg
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.9
sequence calculation, ADC1
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
Adc2 expression is restricted to stem tissue, Adc1 is expressed in leaf, root and stem
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
the enzyme sequence contains a putative N-terminal chloroplastic signal peptide
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
68000
ADC2, predicted from amino acid sequence
74000
176000
-
gel filtration
63000
-
3 * 63000, SDS-PAGE
additional information
-
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 74000, about, sequence calculation, ADC1
trimer
-
3 * 63000, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene ADC1, cloning from genomic DNA, DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic analysis, expression analysis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Choudhuri, M.M.; Ghosh, B.
Purification and partial characterization of arginine decarboxylase from rice embryos (Oryza sativa L.)
Agric. Biol. Chem.
46
739-743
1982
Evernia prunastri, Oryza sativa
-
Manually annotated by BRENDA team
Reggiani, R.
Purification and synthesis under anaerobic conditions of rice arginine decarboxylase
Plant Cell Physiol.
35
1245-1249
1994
Oryza sativa
-
Manually annotated by BRENDA team
Akiyama, T.; Jin, S.
Molecular cloning and characterization of an arginine decarboxylase gene up-regulated by chilling stress in rice seedlings
J. Plant Physiol.
164
645-654
2007
Oryza sativa (Q9SNN0), Oryza sativa
Manually annotated by BRENDA team
Peremarti, A.; Bassie, L.; Zhu, C.; Christou, P.; Capell, T.
Molecular characterization of the arginine decarboxylase gene family in rice
Transgenic Res.
19
785-797
2010
Oryza sativa (Q9SNN0), Oryza sativa
Manually annotated by BRENDA team