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Information on EC 4.1.1.19 - arginine decarboxylase and Organism(s) Synechocystis sp. and UniProt Accession P74576

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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:
Synechocystis sp.
UNIPROT: P74576
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Word Map
The taxonomic range for the selected organisms is: Synechocystis sp.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
arginine decarboxylase, spea2, argdc, spea1, biosynthetic arginine decarboxylase, ppadc, atadc2, l-arginine decarboxylase, pyruvoyl-dependent arginine decarboxylase, ptadc, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
the pyridoxal 5'-phosphate-binding domain is linked to the C-terminal domain by the N-terminus
pyridoxal 5'-phosphate
conserved binding site structure
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform ADC1
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
stabilized by two inter-subunit disulfide bonds, structural modeling
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
side-chain modification
two symmetric inter-subunit disulfide bonds seem to stabilize the dimeric structure of arginine decarboxylase
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
profiles of the steady-state accumulation of Synechocystis ADC transcripts and ADC specific activities under various environmental conditions, overview
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
salt stress clearly results in an increased steady-state transcript accumulation even though the specific activity shows no apparent change
steady-state accumulation of arginine decarboxylase transcripts and its specific activity are unaffected by dark incubation
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jantaro, S.; Kidron, H.; Chesnel, D.; Incharoensakdi, A.; Mulo, P.; Salminen, T.; Maenpaa, P.
Structural modeling and environmental regulation of arginine decarboxylase in Synechocystis sp. PCC 6803
Arch. Microbiol.
184
397-406
2006
Synechocystis sp., Synechocystis sp. (P74576)
Manually annotated by BRENDA team