Information on EC 4.1.1.19 - Arginine decarboxylase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY
4.1.1.19
-
RECOMMENDED NAME
GeneOntology No.
Arginine decarboxylase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
L-arginine = agmatine + CO2
show the reaction diagram
-
-
-
-
L-arginine = agmatine + CO2
show the reaction diagram
the K148-loop movement may be kinetically linked to the rate-limiting step of product release, active site structure, mechanism
Paramecium bursaria chlorella virus
-
L-arginine = agmatine + CO2
show the reaction diagram
reaction mechanism via geminal diamine intermediate
Q8ZHG8
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
decarboxylation
-
-
-
-
decarboxylation
Q5NT93, -
-
decarboxylation
-
-
decarboxylation
P22220
-
decarboxylation
B3Y023, -
-
decarboxylation
-
-
decarboxylation
-
-
decarboxylation
-
-
PATHWAY
KEGG Link
MetaCyc Link
Arginine and proline metabolism
-
arginine degradation III (arginine decarboxylase/agmatinase pathway)
-
arginine degradation IV (arginine decarboxylase/agmatine deiminase pathway)
-
arginine dependent acid resistance
-
Metabolic pathways
-
putrescine biosynthesis I
-
putrescine biosynthesis II
-
putrescine biosynthesis IV
-
spermidine biosynthesis III
-
SYSTEMATIC NAME
IUBMB Comments
L-arginine carboxy-lyase (agmatine-forming)
A pyridoxal-phosphate protein.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
AaxB protein
-
-
acid-induced biodegradative arginine decarboxylase
P28629
-
ADC
-
-
-
-
ADC
P22220
-
ADC
Bacillus subtilis 168
-
-
-
ADC
Campylobacter jejuni NCTC 11168
Q0PAC6
-
-
ADC
Clostridium difficile
-
-
ADC
P21170
-
ADC
Q96A70
-
ADC
Q71S28
-
ADC
Q9SNN0
-
ADC
Paramecium bursaria chlorella virus
-
-
ADC
Q71SB4
-
ADC
B3Y023
-
ADC
Trypanosoma cruzi RA
-
-
-
ADC
Q7MK24
-
ADC
Q8ZHG8
-
AdiA
Salmonella enterica subsp. enterica serovar Typhimurium CECT 44, Salmonella enterica subsp. enterica serovar Typhimurium CECT 443
-
-
-
ARGDC
-
-
-
-
ARGDC
Chlamydia pneumoniae Kajaani
-
-
-
ARGDC
P28629
-
ARGDC
Q9UWU1
-
-
arginine decarboxlase 2
-
-
arginine decarboxylase
P22220
-
arginine decarboxylase
-
-
arginine decarboxylase
Q57764
-
arginine decarboxylase
-
-
arginine decarboxylase
B3Y023
-
arginine decarboxylase
-
-
arginine decarboxylase
-
-
arginine decarboxylase
Q5NT93
-
arginine decarboxylase
-
-
arginine decarboxylase2
-
-
arginine:agmatine exchange system
-
-
AtDC2
-
stress-inducible
bADC
-
-
-
-
Biosynthetic arginine decarboxylase
-
-
-
-
Biosynthetic arginine decarboxylase
Q7MK24
-
CPn1032 homolog
-
-
CPn1032 homolog
Chlamydia pneumoniae Kajaani
-
-
-
dADC
-
-
-
-
Decarboxylase, arginine
-
-
-
-
L-Arginine decarboxylase
-
-
-
-
PaADC1
-
expressed in all stages of development, up-regulated in response to chilling or salt stress in seedling stage
PaADC2
-
expressed mainly in mature plant
PBCV-1 DC
Paramecium bursaria Chlorella virus-1
-
-
PpADC
B3Y023
-
protein SSO0536
Q9UWU1
-
protein SSO0536
Q9UWU1
-
-
pyruvoyl-dependent arginine decarboxylase
-
-
pyruvoyl-dependent arginine decarboxylase
Q57764
-
pyruvoyl-dependent arginine decarboxylase
Q5JFI4
-
pyruvoyl-dependent arginine decraboxylase
-
-
SpeA
Campylobacter jejuni NCTC 11168
Q0PAC6
-
-
SpeA
P21170
-
Synthetic arginine decarboxylase
-
-
-
-
L-Arginine decarboxylase
Q5NT93
-
additional information
-
the enzyme is a decarboxylase of the AR structural family
additional information
Paramecium bursaria chlorella virus
-
the enzyme belongs to the group IV of pyridoxal 5'-phosphate-dependent decarboxylases belonging to the alpha/beta barrel structural family
additional information
-
the enzyme is a decarboxylase of the AR structural family
CAS REGISTRY NUMBER
COMMENTARY
9024-77-5
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Nossen ecotype
-
-
Manually annotated by BRENDA team
wild type and mutants spe1-1 and spe2-1 with reduced arginine decarboxylase activity
-
-
Manually annotated by BRENDA team
L. cv. Victory
-
-
Manually annotated by BRENDA team
Bacillus subtilis 168
-
-
-
Manually annotated by BRENDA team
ssp. oleifera
-
-
Manually annotated by BRENDA team
Campylobacter jejuni NCTC 11168
-
UniProt
Manually annotated by BRENDA team
strain Kajaani 6, gene CPn1032
-
-
Manually annotated by BRENDA team
Chlamydia pneumoniae Kajaani
strain Kajaani 6, gene CPn1032
-
-
Manually annotated by BRENDA team
serovar L2 and D strains
-
-
Manually annotated by BRENDA team
Clostridium difficile
-
-
-
Manually annotated by BRENDA team
gene adiA, inducible and constitutive ArgDCs
SwissProt
Manually annotated by BRENDA team
strain B
-
-
Manually annotated by BRENDA team
strain BL21(DE3)
SwissProt
Manually annotated by BRENDA team
(L) Merr cv. Williams
SwissProt
Manually annotated by BRENDA team
Heliotropium spathulatum
-
-
-
Manually annotated by BRENDA team
variant Nugget
-
-
Manually annotated by BRENDA team
(L) var. Ventus
-
-
Manually annotated by BRENDA team
(L) Mill. var. domestica (Borkh.) Mansf.
SwissProt
Manually annotated by BRENDA team
var. domestica, gene ADC
-
-
Manually annotated by BRENDA team
strain TMC 1546
-
-
Manually annotated by BRENDA team
Mycobacterium smegmatis TMC 1546
strain TMC 1546
-
-
Manually annotated by BRENDA team
cv. Wisconsin 38
-
-
Manually annotated by BRENDA team
L. cv. Petit Havana SR1
-
-
Manually annotated by BRENDA team
TMV-resistant plants
-
-
Manually annotated by BRENDA team
no activity in Trypanosoma cruzi
-
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
subsp. japonica, cv. Yukihikari, gene ADC1
SwissProt
Manually annotated by BRENDA team
Paramecium bursaria chlorella virus
-
-
-
Manually annotated by BRENDA team
Paramecium bursaria Chlorella virus-1
enzyme displays ornithine decarboxylase as well as arginine decarboxylase activity
-
-
Manually annotated by BRENDA team
clones K818 and K884
SwissProt
Manually annotated by BRENDA team
fragment; clone 884 originating from the Punkaharju clone collection in Finland
SwissProt
Manually annotated by BRENDA team
endemic in subantarctic region, high levels of polyamines and agmatine
-
-
Manually annotated by BRENDA team
Mochizuki and Akatsuki fruits
UniProt
Manually annotated by BRENDA team
male Harlan Sprague-Dawley rats
-
-
Manually annotated by BRENDA team
male Sprague-Daley rats
-
-
Manually annotated by BRENDA team
male sprague-dawley rats
-
-
Manually annotated by BRENDA team
Rhizophora apiculata Bl
Bl
-
-
Manually annotated by BRENDA team
serovar typhimurium
-
-
Manually annotated by BRENDA team
Salmonella enterica subsp. enterica serovar Typhimurium CECT 44
strain CECT 44
-
-
Manually annotated by BRENDA team
-
Q5NT93
UniProt
Manually annotated by BRENDA team
PCC 6803; strain PCC 6803, two genes encoding the enzyme
-
-
Manually annotated by BRENDA team
strain RA
-
-
Manually annotated by BRENDA team
Trypanosoma cruzi RA
strain RA
-
-
Manually annotated by BRENDA team
gene speA
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
mutants overexpressing arginine decarboxylase 2 display dwarfism and late flowering
malfunction
-
an adiA deletion strain does not show any survival at pH 2.3. Lack of AdiA does not impair systemic infection
physiological function
-
in transgenic plants expressing ADC, putrescine synthesis is enhanced even under normal conditions, stress results in the trigger level being exceeded and the accumulation of spermidine and spermine leads to the restoration of normal growth and development, even under stress
physiological function
-
high putrescine accumulation by overexpression of ADC2 results in reduced water loss
physiological function
-
the Bacillus subtilis biosynthetic aspartate aminotransferase fold arginine decarboxylase is essential for biofilm formation
physiological function
-
higher level of hexahistidine tagged human ADC transgene expression completely trigger the endogenous agmatine synthesis during H2O2 injury thus protecting NIH3T3 cells against cytotoxicity
physiological function
-
AdiA promotes survival of Salmonella at pH 2.3
physiological function
Q5JFI4, -
a gene disruptant lacking arginine decarboxylase is constructed, showing that it grows only in the medium in the presence of agmatine but not in the absence of agmatine. The results indicates that agmatine is essential for the cell growth of Thermococcus kodakaraensis
physiological function
Bacillus subtilis 168
-
the Bacillus subtilis biosynthetic aspartate aminotransferase fold arginine decarboxylase is essential for biofilm formation
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
arginine
?
show the reaction diagram
-
-
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
Q96A70
-
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
Q57764
-
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-, Q9SCF0
-
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
Paramecium bursaria Chlorella virus-1
-
-
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
Q5R145
-
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
Q39827
-
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
Q9SNN0
-
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-, P28629
-
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
Q71S28
-
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
arginine decarboxylase pathway participates in putescine biosynthesis
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
Q96A70
biosynthesis of agmatine
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
enzyme is involved in polyamine biosynthesis
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
key enzyme of polyamine biosynthesis
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
level and/or activity is posttranslationally regulated
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
the ADC2 gene is the only gene of polyamine biosynthesis involved in wounding response mediated by methyl jasmonate. A transient increase in the level of free putrescine follows the increase in the mRNA level for ADC2
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
Q9SI64
amino acids K136 and C524 of ADC1 are essential for activity and participate in separate active sites
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine and the subsequent synthesis of spermine and spermidine, plays a role in response to mechanical wounding
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, involved in chilling and salt stress response
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in abiotic stress response
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
Q5R145
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in chilling, salt, and dehydration stress response
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in salt and osmotic stress response
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in salt stress response, high temperature and glucose treatment causes an increase in the specific activity, the specific activity is reduced by iron deficiency
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in stress response
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in stress response
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
Paramecium bursaria Chlorella virus-1
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in stress response
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in stress response, mutants spe1-1 and spe2-1 have a lower salt tolerance than the wild type plant
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
Q39827
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in stress response, possible involved in the development of lateral roots
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, which is the precursor for the synthesis of spermidine and spermine, plays a role in the growth of hypocotyls
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
key enzyme in the biosynthesis of polyamines, primarily responsible for the biosynthesis of putrescine in non-dividing elongation cells, plays a role in stress response
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
rate limiting and key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, induced in response to salt stress
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
enzyme catalyzes the first step of the polyamine-biosynthetic pathway
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
Trypanosoma cruzi RA
-
-
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
Mycobacterium smegmatis TMC 1546
-
-
-
-
L-Arg
Agmatine + CO2
show the reaction diagram
Rhizophora apiculata Bl
-
-, key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, which is the precursor for the synthesis of spermidine and spermine, plays a role in the growth of hypocotyls
-
-
?
L-Arg
?
show the reaction diagram
-
inducible enzyme
-
-
-
L-Arg
?
show the reaction diagram
-
constitutive enzyme
-
-
-
L-Arg
?
show the reaction diagram
-
important enzyme in putrescine and polyamine biosynthesis
-
-
-
L-Arg
?
show the reaction diagram
-
agmatine production by the mitochondria could serve as a protective mechanism against cytotoxicity from excessive nitric oxide formation
-
-
-
L-Arg
?
show the reaction diagram
-
cAMP receptor protein controls arginine decarboxylase expression by inhibiting the activity of the enzyme indirectly and putrescine represses the gene at the level of transcription
-
-
-
L-Arg
?
show the reaction diagram
-
higher activity in plants cultivated on ammonium chloride than in plants grown on nitrate
-
-
-
L-Arg
?
show the reaction diagram
-
possibly active in biosynthesis of polyamines required for growth by expansion and differentiation or in synthesis of alkaloids from putrescine
-
-
-
L-Arg
?
show the reaction diagram
-
key enzyme in polyamine metabolism of plants
-
-
-
L-Arg
?
show the reaction diagram
-
2 enzyme forms: a biosynthetic arginine decarboxylase and a degradative arginine decarboxylase. The physiological role of the degradative arginine decarboxylase possibly is the regulation of the environmental pH
-
-
-
L-Arg
?
show the reaction diagram
-
regulatory role in growth and cell division
-
-
-
L-Arg
?
show the reaction diagram
-
the biosynthetic arginine decarboxylase is the first of two enzymes in a putrescine biosynthetic pathway
-
-
-
L-Arg
?
show the reaction diagram
-
enzyme is involved in synthesis of polyamines
-
-
-
L-arginine
agmatine + CO2
show the reaction diagram
-
-
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-
-
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-
-
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-
-
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-, Q71SB4
-
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-
-
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-
-
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
Clostridium difficile
-
-
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-
-
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-
-
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-
-
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-
-
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-
-
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-
-
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-
-
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
Paramecium bursaria chlorella virus
-
-
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-, Q9SNN0
-
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-
-
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
P28629
-
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-, Q71SB4
-
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
B3Y023, -
-
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
P21170
-
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-, Q0PAC6
-
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
Q7MK24
-
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-
-
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-
-
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
Q9UWU1, -
-
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
Q8ZHG8
ADC is the primary polyamine biosynthetic enzyme in the pathway
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
P28629
the AdiA enzyme is required by the AR3 arginine-dependent acid resistance system
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-, Q71SB4
the enzyme is involved in biosynthesis of the important polyamine precursor putrescine and is transcriptionally regulated, ADC gene expression and enzyme activity increase during embryogenesis
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-
the enzyme is involved in biosynthesis of the important polyamine precursor putrescine, Nicotiana species also utilize putrescine to provide the pyrollidine ring of the defensive alkaloid nicotine and its derivatives in roots playing no major role, overview
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-
the enzyme is involved in polyamine biosynthesis and plays a role in stress response, the enzyme is induced by salt stress leading to accumulation of putrescine
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-
the enzyme is involved in putrescine biosynthesis, diurnal changes in enzyme activity and polyamine contents in leaves, overview
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-
the enzyme is involved in the biosynthesis of putrescine, which is the precursor of other polyamines in animals, plants, and bacteria
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-
the enzyme is the enzyme essential for agmatine synthesis, chronic treatment with glucocorticoids alters rat hippocampal and prefrontal cortical morphology in parallel with endogenous agmatine and arginine decarboxylase levels, neuroprotective effect of agmatine on dexamethasone-induced neuronal damage in brain areas, overview
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-
the first enzyme in the alternative route to putrescine in the polyamine biosynthesis pathway in bacteria and plants, posttranslational regulation involving a putative extra domain, modelling, overview
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-, Q9SNN0
the key enzyme involved with putrescine biosynthesis in plants, the ADC gene shows essentially chilling-specific regulation that also potentially influences putrescine accumulation, a phenomenon previously noted in cold-stressed rice seedlings
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-, Q71SB4
the localization of the enzyme transcript differs in roots inoculated and non-inoculated with mycorrhizal fungus, e.g. Suillus variegatus, overview
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-
effects of various types of short-term stresses on the transcript amount and specific activity of the enzyme, overview
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
Q8ZHG8
the enzyme exists in two different conformational states, one that binds ligand and one that does not
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
Paramecium bursaria chlorella virus
-
the key specificity element is the 310-helix that contains and positions substrate-binding residues such as Glu296,mechanism, the 310-helix in Chlorella virus ADC is shifted over 2 A away from the pyridoxal 5'-phosphate cofactor, the K148 loop functions as an active site lid, overview
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-, P22220
first reaction of a putrescine synthetic pathway found in bacteria and plants
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-
rate-limiting enzyme in polyamine biosynthesis
agmatine is a neurotransmitter or neuromodulator in the brain, agmatine has neuroprotective effects in vitro and in vivo
-
?
L-arginine
agmatine + CO2
show the reaction diagram
Q5NT93, -
assay at pH 6.5, 10 min, 50C
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
Q5JFI4, -
first step of polyamine biosynthesis
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
Q5JFI4, -
no activity with ornithine and lysine
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
Q9UWU1, -
the crenarchaeal arginine decarboxylase has no S-adenosylmethionine decarboxylase activity
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
Bacillus subtilis 168, Chloroflexus aurantiacus J-10-fl
-
-
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
Chlamydia pneumoniae Kajaani
-
-
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
Campylobacter jejuni NCTC 11168
Q0PAC6
-
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-
-
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
Q9UWU1
-, the crenarchaeal arginine decarboxylase has no S-adenosylmethionine decarboxylase activity
-
-
?
L-Asp
?
show the reaction diagram
-
2.6% of the activity with L-Arg
-
-
-
L-Canavanine
?
show the reaction diagram
-
-
-
-
-
L-Canavanine
?
show the reaction diagram
-
40% of the activity with L-Arg
-
-
-
L-canavanine
N-(3-aminopropoxy)guanidine + CO2
show the reaction diagram
-
-
-
-
?
L-canavanine
N-(3-aminopropoxy)guanidine + CO2
show the reaction diagram
Q9UWU1, -
decarboxylation at 40% of the activity compared with L-arginine
-
-
?
L-canavanine
N-(3-aminopropoxy)guanidine + CO2
show the reaction diagram
Q9UWU1
decarboxylation at 40% of the activity compared with L-arginine
-
-
?
L-canavanine
gamma-guanidinoxypropylamine + CO2
show the reaction diagram
Chlamydia pneumoniae, Chlamydia pneumoniae Kajaani
-
-
-
-
?
L-Glu
?
show the reaction diagram
-
2.1% of the activity with L-Arg
-
-
-
L-lysine
1,5-diaminopentane + CO2
show the reaction diagram
-
activity is 1.9% of that with L-arginine
-
-
?
L-lysine
?
show the reaction diagram
Q5NT93, -
assay at pH 6.5, 10 min, 50C
-
-
?
L-N5-(iminoethyl)-ornithine
N1-(2-iminoethyl)-butane-1,4-diamine + CO2
show the reaction diagram
-
-
-
-
?
L-Orn
Putrescine + CO2
show the reaction diagram
-
-
-
-
?
L-Orn
?
show the reaction diagram
-
-
-
-
-
L-ornithine
putrescine + CO2
show the reaction diagram
Paramecium bursaria Chlorella virus-1
-
-
-
-
?
L-ornithine
1,4-diaminobutane + CO2
show the reaction diagram
-
very low activity
-
-
?
L-ornithine
1,4-diaminobutane + CO2
show the reaction diagram
-
activity is 1.4% of that with L-arginine
-
-
?
L-ornithine
1,4-diaminobutane + CO2
show the reaction diagram
Bacillus subtilis 168
-
very low activity
-
-
?
L-ornithine
1,4-diaminobutane + CO2
show the reaction diagram
-
activity is 1.4% of that with L-arginine
-
-
?
L-Phe
phenylethylamine + CO2
show the reaction diagram
-
1.4% of the activity with L-Arg
-
-
-
L-Pro
?
show the reaction diagram
-
3.8% of the activity with L-Arg
-
-
-
L-Ser
?
show the reaction diagram
-
4.4% of the activity with L-Arg
-
-
-
Ngamma-monomethyl-L-Arg
N-(3-aminopropyl)-N'-methylguanidine + CO2
show the reaction diagram
-
-
-
-
?
meso-diaminopimelate
?
show the reaction diagram
-
activity is less than 2% of that with L-arginine
-
-
?
additional information
?
-
-
acting together with a putative arginine-agmatine antiporter, the CPn1032 homologs may have evolved convergently to form an arginine-dependent acid resistance system, this system could reduce the host cell arginine concentration and produce inhibitors of nitric oxide synthase, obligately intracellular chlamydiae may encounter acidic conditions, overview
-
-
-
additional information
?
-
-
the enzyme is involved in the polyamine metabolism, effects of long term cadmium or copper stress, overview
-
-
-
additional information
?
-
-
the enzyme is highly substrate specific, no activity with D-arginine, L-aspartate, L-citrulline, L-glutamine, L-histidine, L-homoarginine, L-lysine, N-methyl-Larginine, and L-ornithine
-
-
-
additional information
?
-
-
arginine decarboxylase is involved in stress protection against environmental cues and pathogens
-
-
-
additional information
?
-
-
recent evidence suggests a potential involvement of agmatine in learning and memory processing
-
-
-
additional information
?
-
-
human ornithine decarboxylase paralogue (ODCp) is not an arginine decarboxylase
-
-
-
additional information
?
-
Chlamydia pneumoniae Kajaani
-
acting together with a putative arginine-agmatine antiporter, the CPn1032 homologs may have evolved convergently to form an arginine-dependent acid resistance system, this system could reduce the host cell arginine concentration and produce inhibitors of nitric oxide synthase, obligately intracellular chlamydiae may encounter acidic conditions, overview, the enzyme is highly substrate specific, no activity with D-arginine, L-aspartate, L-citrulline, L-glutamine, L-histidine, L-homoarginine, L-lysine, N-methyl-Larginine, and L-ornithine
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-Arg
Agmatine + CO2
show the reaction diagram
-
-
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
Q9SNN0
-
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-, P28629
-
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
arginine decarboxylase pathway participates in putescine biosynthesis
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
Q96A70
biosynthesis of agmatine
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
enzyme is involved in polyamine biosynthesis
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
key enzyme of polyamine biosynthesis
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
level and/or activity is posttranslationally regulated
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
the ADC2 gene is the only gene of polyamine biosynthesis involved in wounding response mediated by methyl jasmonate. A transient increase in the level of free putrescine follows the increase in the mRNA level for ADC2
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine and the subsequent synthesis of spermine and spermidine, plays a role in response to mechanical wounding
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, involved in chilling and salt stress response
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in abiotic stress response
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
Q5R145
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in chilling, salt, and dehydration stress response
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in salt and osmotic stress response
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in salt stress response, high temperature and glucose treatment causes an increase in the specific activity, the specific activity is reduced by iron deficiency
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in stress response
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in stress response
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
Paramecium bursaria Chlorella virus-1
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in stress response
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in stress response, mutants spe1-1 and spe2-1 have a lower salt tolerance than the wild type plant
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
Q39827
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, plays a role in stress response, possible involved in the development of lateral roots
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, which is the precursor for the synthesis of spermidine and spermine, plays a role in the growth of hypocotyls
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
key enzyme in the biosynthesis of polyamines, primarily responsible for the biosynthesis of putrescine in non-dividing elongation cells, plays a role in stress response
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
rate limiting and key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, induced in response to salt stress
-
-
?
L-Arg
Agmatine + CO2
show the reaction diagram
-
enzyme catalyzes the first step of the polyamine-biosynthetic pathway
-
-
?
L-Arg
?
show the reaction diagram
-
inducible enzyme
-
-
-
L-Arg
?
show the reaction diagram
-
constitutive enzyme
-
-
-
L-Arg
?
show the reaction diagram
-
important enzyme in putrescine and polyamine biosynthesis
-
-
-
L-Arg
?
show the reaction diagram
-
agmatine production by the mitochondria could serve as a protective mechanism against cytotoxicity from excessive nitric oxide formation
-
-
-
L-Arg
?
show the reaction diagram
-
cAMP receptor protein controls arginine decarboxylase expression by inhibiting the activity of the enzyme indirectly and putrescine represses the gene at the level of transcription
-
-
-
L-Arg
?
show the reaction diagram
-
higher activity in plants cultivated on ammonium chloride than in plants grown on nitrate
-
-
-
L-Arg
?
show the reaction diagram
-
possibly active in biosynthesis of polyamines required for growth by expansion and differentiation or in synthesis of alkaloids from putrescine
-
-
-
L-Arg
?
show the reaction diagram
-
key enzyme in polyamine metabolism of plants
-
-
-
L-Arg
?
show the reaction diagram
-
2 enzyme forms: a biosynthetic arginine decarboxylase and a degradative arginine decarboxylase. The physiological role of the degradative arginine decarboxylase possibly is the regulation of the environmental pH
-
-
-
L-Arg
?
show the reaction diagram
-
regulatory role in growth and cell division
-
-
-
L-Arg
?
show the reaction diagram
-
the biosynthetic arginine decarboxylase is the first of two enzymes in a putrescine biosynthetic pathway
-
-
-
L-Arg
?
show the reaction diagram
-
enzyme is involved in synthesis of polyamines
-
-
-
L-Arg
Agmatine + CO2
show the reaction diagram
Rhizophora apiculata Bl
-
key enzyme in the biosynthesis of polyamines, key enzyme in the biosynthesis of putrescine, which is the precursor for the synthesis of spermidine and spermine, plays a role in the growth of hypocotyls
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-
-
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-
-
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-
-
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-
-
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-
-
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
Paramecium bursaria chlorella virus
-
-
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
B3Y023, -
-
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
Q9UWU1, -
-
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
Q8ZHG8
ADC is the primary polyamine biosynthetic enzyme in the pathway
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
P28629
the AdiA enzyme is required by the AR3 arginine-dependent acid resistance system
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-, Q71SB4
the enzyme is involved in biosynthesis of the important polyamine precursor putrescine and is transcriptionally regulated, ADC gene expression and enzyme activity increase during embryogenesis
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-
the enzyme is involved in biosynthesis of the important polyamine precursor putrescine, Nicotiana species also utilize putrescine to provide the pyrollidine ring of the defensive alkaloid nicotine and its derivatives in roots playing no major role, overview
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-
the enzyme is involved in polyamine biosynthesis and plays a role in stress response, the enzyme is induced by salt stress leading to accumulation of putrescine
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-
the enzyme is involved in putrescine biosynthesis, diurnal changes in enzyme activity and polyamine contents in leaves, overview
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-
the enzyme is involved in the biosynthesis of putrescine, which is the precursor of other polyamines in animals, plants, and bacteria
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-
the enzyme is the enzyme essential for agmatine synthesis, chronic treatment with glucocorticoids alters rat hippocampal and prefrontal cortical morphology in parallel with endogenous agmatine and arginine decarboxylase levels, neuroprotective effect of agmatine on dexamethasone-induced neuronal damage in brain areas, overview
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-
the first enzyme in the alternative route to putrescine in the polyamine biosynthesis pathway in bacteria and plants, posttranslational regulation involving a putative extra domain, modelling, overview
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-, Q9SNN0
the key enzyme involved with putrescine biosynthesis in plants, the ADC gene shows essentially chilling-specific regulation that also potentially influences putrescine accumulation, a phenomenon previously noted in cold-stressed rice seedlings
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-, Q71SB4
the localization of the enzyme transcript differs in roots inoculated and non-inoculated with mycorrhizal fungus, e.g. Suillus variegatus, overview
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-, P22220
first reaction of a putrescine synthetic pathway found in bacteria and plants
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
-
rate-limiting enzyme in polyamine biosynthesis
agmatine is a neurotransmitter or neuromodulator in the brain, agmatine has neuroprotective effects in vitro and in vivo
-
?
L-arginine
agmatine + CO2
show the reaction diagram
Q5JFI4, -
first step of polyamine biosynthesis
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
Chlamydia pneumoniae Kajaani
-
-
-
-
?
L-arginine
agmatine + CO2
show the reaction diagram
Q9UWU1
-
-
-
?
L-ornithine
putrescine + CO2
show the reaction diagram
Paramecium bursaria Chlorella virus-1
-
-
-
-
?
additional information
?
-
-
acting together with a putative arginine-agmatine antiporter, the CPn1032 homologs may have evolved convergently to form an arginine-dependent acid resistance system, this system could reduce the host cell arginine concentration and produce inhibitors of nitric oxide synthase, obligately intracellular chlamydiae may encounter acidic conditions, overview
-
-
-
additional information
?
-
-
the enzyme is involved in the polyamine metabolism, effects of long term cadmium or copper stress, overview
-
-
-
additional information
?
-
-
arginine decarboxylase is involved in stress protection against environmental cues and pathogens
-
-
-
additional information
?
-
-
recent evidence suggests a potential involvement of agmatine in learning and memory processing
-
-
-
additional information
?
-
Chlamydia pneumoniae Kajaani
-
acting together with a putative arginine-agmatine antiporter, the CPn1032 homologs may have evolved convergently to form an arginine-dependent acid resistance system, this system could reduce the host cell arginine concentration and produce inhibitors of nitric oxide synthase, obligately intracellular chlamydiae may encounter acidic conditions, overview
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
stimulates
pyridoxal 5'-phosphate
-
stimulates
pyridoxal 5'-phosphate
-
cofactor
pyridoxal 5'-phosphate
-
0.8 mM, stimulates by about 30%; stimulates
pyridoxal 5'-phosphate
-
required
pyridoxal 5'-phosphate
-
a formyl group of pyridoxal 5'-phosphate is bound to the 6-amino group of a Lys residue. Binds 10 mol of pyridoxal 5'-phosphate per mol of enzyme
pyridoxal 5'-phosphate
-
structure of the pyridoxal 5'-phosphate binding site: Ala-Thr-His-Ser-Thr-His-(pyridoxal 5'-phosphate)Lys-Leu-Leu-Asn-Ala-Leu-Ser-Gln-Ala-Ser-Tyr
pyridoxal 5'-phosphate
-
dependent on; required for tetramer formation
pyridoxal 5'-phosphate
-
absolute requirement
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
conserved binding site structure
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
Paramecium bursaria chlorella virus
-
dependent on, the cofactor forms an interaction with K48 via Schiff base
pyridoxal 5'-phosphate
Q8ZHG8
a fold III, pyridoxal 5'-phosphate-dependent enzyme
pyridoxal 5'-phosphate
P28629
dependent on
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
Q5NT93, -
-
pyridoxal 5'-phosphate
P22220
ADC belongs to the group IV pyridoxal 5'-phosphate-dependent decarboxylases
pyridoxal 5'-phosphate
B3Y023, -
enzyme contains the motif characteristics of the pyridoxal 5'-phosphate-attachment site at amino acid position 149-167
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-, Q0PAC6
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
Q7MK24
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
Pyruvoyl group
Q9UWU1, -
pyruvoyl-dependent decarboxylase, synthesised as zymogen. The pyruvoyl cofactor results from the self-modification of an internal serine (Ser82) residue of the proenzyme, the pyruvoyl group functions through the formation of a Schiff base with the substrate to promote decarboxylation
additional information
-
the enzyme contains a reactive pyruvoyl group
-
additional information
-
the pyruvoyl group of the enzyme is generated by an autocatalytic internal serinolysis reaction at Ser53 in the proenzyme resulting in two polypeptide chains
-
additional information
-
The serine residue at N terminus of the {alpha} subunit forms a reactive pyruvoyl group that functions analogously to pyridoxal 5'-phosphate
-
additional information
-
the enzyme contains a reactive pyruvoyl group, the proenzyme undergoes autocatalytic serinolysis, resulting in the formation of two chains and the creation of a pyruvoyl group, which is the cofactor for the decarboxylation reaction
-
additional information
Q5JFI4, -
pyruvoyl-dependent decarboxylase, synthesised as zymogen. The pyruvoyl cofactor results from the self-modification of an internal serine (Ser44) residue of the proenzyme, the pyruvoyl group functions through the formation of a Schiff base with the substrate to promote decarboxylation
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Cd2+
-
activates at 1 mM, overview
Cd2+
B3Y023, -
transcripts of ADC in peach leaves are quickly induced in response to treatment with 0.15 mM CdCl2
Cu2+
-
activates at 1 mM, overview
Mg2+
-
required
Mg2+
-
absolute requirement
Mg2+
-
required
Mg2+
Q8ZHG8
required for activity
Mn2+
-
0.1 mM increases activity by 35%. 0.01-0.1 mM, enhances activity. Inhibition at higher concentrations
additional information
Q9UWU1, -
no stimulation by KCl
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(E)-alpha-Monofluoromethyl-3-4-dehydroarginine
-
irreversible inhibitor may have a potential application in chemotherapy against Trypanosoma cruzi infection
2-Nor-2-butylpyridoxal phosphate
-
-
4-Bromo-3-hydroxybenzoyloxyamine dihydrogen phosphate
-
-
4-Bromo-3-hydroxybenzoyloxyamine dihydrogen phosphate
-
NSD 1055
4-Bromo-3-hydroxybenzoyloxyamine dihydrogen phosphate
-
-
4-Guanidinobutyrate
-
-
5-Deoxypyridoxal
-
-
agmatine
-
10 mM, 57% inhibition
agmatine
-
-
agmatine
-
1.4 mM, 50% inhibition
alpha-Difluoromethylarginine
-
-
alpha-Difluoromethylarginine
Paramecium bursaria Chlorella virus-1
-
1 mM causes almost complete inhibition after 30 min incubation, irreversible
alpha-Difluoromethylarginine
-
-
alpha-difluoromethylornithine
Q5R145
-
alpha-difluoromethylornithine
Paramecium bursaria Chlorella virus-1
-
10 mM causes 74% inhibition after 30 min incubation, irreversible
beta-(2-Methyl-3-hydroxy-4-formylpyridine-5)-propionic acid
-
-
Ca2+
-
100 mM, 90% decrease of activity
Ca2+
-
IC50: 0.8 mM
canavanine
-
-
canavanine
-
L-canavanine
canavanine
-
L-canavanine
canavanine
-
-
canavanine
-
L-canavanine
citrulline
-
-
citrulline
-
L-citrulline
citrulline
-
-
Co2+
-
0.1 mM, 70% loss of activity
Cu2+
-
1 mM, 25% inhibition. 5 mM, 94% inhibition
Cu2+
-
0.1 mM, 70% loss of activity
D-Arg
-
1 mM, 60% inhibition
D-Arginine
Q5R145
decreases enzyme activity and inhibits growth of apple callus
D-Arginine
-
causes further damage to callus under salt stress, reversible by addition of putrescine
D-Arginine
Q9SNN0
-
difluoromethyl-L-arginine
Q9UWU1, -
1 mM, 80 C, 15 min, 64% loss of activity, irreversible inhibition
-
difluoromethyl-L-ornithine
Q9UWU1, -
1 mM, reduces activity by 20%
-
DL-alpha-Difluoromethylarginine
-
irreversible inhibitor may have a potential application in chemotherapy against Trypanosoma cruzi infection
DL-alpha-Difluoromethylarginine
-
-
DL-alpha-Difluoromethylarginine
Q5NT93, -
-
DL-alpha-Difluoromethylarginine
-
In the absence of phenanthrene, treatment with 1.5 mM DL-alpha-difluoromethylarginine with reduces ADC activity by 61%
Fluorescein isothiocyanate
-
0.09 mM, 40% inhibition
guanidine
-
-
guanidine
-
5-10 mM, 50% inhibition
Guanidinoacetic acid
-
-
Homoarginine
-
-
Homoarginine
-
-
hydroxylamine
-
-
iodoacetamide
-
-
K+
-
100 mM, 50% decrease of activity
L-2-Amino-3-guanidinopropanoate
-
-
L-2-Amino-4-guanidinobutyrate
-
-
L-2-amino-5-guanidinopentanoate
-
-
L-2-Amino-6-guanidinohexanoate
-
-
L-2-Chloro-5-guanidinopentanoate
-
-
L-2-Hydroxy-5-guanidinopentanoate
-
-
L-argininamide
-
5 mM, complete inhibition
L-argininamide
-
33% inhibition at 2 mM
L-argininamide
Q9UWU1, -
1 mM, almost completely abolished arginine decarboxylase activity
L-arginine methyl ester
-
-
L-arginine methyl ester
-
5 mM, complete inhibition
L-arginine methyl ester
Q9UWU1, -
1 mM, 70% loss of activity
L-arginineamide
-
-
L-Argininic acid
-
-
L-canavanine
-
-
L-canavanine
Q9UWU1, -
1 mM, 46% inhibition
L-histidine
Q9UWU1, -
1 mM, 20-30% inhibition
L-Homoarginine
-
-
L-Homoarginine
Q9UWU1, -
1 mM, 20-30% inhibition
Methyl bis-[guanylhydrazone]
-
-
-
methylglyoxal bisguanylhydrazone
-
-
Methylguanidine
-
-
Methylguanidine
-
-
Methylguanidine
-
5-10 mM, 50% inhibition
Mg2+
-
100 mM, 90% decrease of activity
Mn2+
-
0.01-0.1 mM, enhances activity. Inhibition at higher concentrations
Mn2+
-
100 mM, 90% decrease of activity
N-benzylguanidine
-
-
N-Carbamoylputrescine
-
-
n-propylguanidine
-
-
N5-Hydroxy-DL-Arg
-
-
Na+
-
10 mM, 20% decrease of activity
Nalpha-acetyl-L-arginine
Q9UWU1, -
1 mM, 20-30% inhibition
NEM
-
3 mM, 65% inhibition
NG-methylarginine
-
-
NG-Nitroarginine
-
-
Ngamma-methyl-D-arginine
-
-
O-(4-nitrobenzyl)hydroxylamine
Q9UWU1, -
1 mM, 50% inhibition, pyruvoyl group modification
-
O-methyl hydroxylamine
-
69% inhibition at 2 mM
O-Methylhydroxylamine
Q9UWU1, -
1 mM, 50% inhibition, pyruvoyl group modification
O-nitrobenzylhydroxylamine
-
75% inhibition at 2 mM
p-hydroxymercuribenzoate
-
-
PCMB
-
dithiothreitol prevents inhibition
phenanthrene
-
concentrations above 0.5 microM cause either no change or a significant reduction in ADC activity irrespective of treatment with or without DL-alpha-difluoromethylarginine
phenylhydrazine
-
-
Polyamines
-
-
-
Polyamines
-
-
-
putrescine
-
-
-
putrescine
-
-
-
putrescine
-
-
-
putrescine
-
-
-
putrescine
-
-
-
putrescine
-
-
-
pyridoxal
-
-
Pyridoxine-HCl
-
-
Semicarbazide
-
-
spermidine
-
-
spermidine
-
-
spermidine
-
-
spermidine
-
-
spermidine
-
-
spermine
-
1 mM, 5% inhibition of the enzyme from fully developed fruit, 65% inhibition of the enzyme from the seed coat of 4-week-old fruitlets
spermine
-
-
spermine
-
-
spermine
-
1 mM, 30% loss of activity
Urea
-
4 M, 80% inhibition
urethane
-
-
Monofluoromethylagmatine
-
irreversible inhibitor may have a potential application in chemotherapy against Trypanosoma cruzi infection
additional information
-
no inhibition by 1 mM alpha-difluoromethylornithine
-
additional information
-
no inhibition by DL-alpha-difluoromethylornithine
-
additional information
-
profiles of the steady-state accumulation of Synechocystis ADC transcripts and ADC specific activities under various environmental conditions, e.g. darkness and cold reduce enzyme expression, overview
-
additional information
-
activity not affected by Mg2+ or Ca2+ at 0.1 mM
-
additional information
-
the mRNA level of adiA is 4fold lower in the mutants deficient in both alpha-subunit and beta-subunit of major histon-like protein HU
-
additional information
-
inhibition of ADC results in much greater levels of oxidative damage than seen in plants treated with 0.5 microM phenanthrene; treatment with DL-alpha-difluoromethylarginine suppresses the large increase in ADC activity observed when the plants are exposed to 0.1 or 0.5 microM phenanthrene in the absence of DL-alpha-difluoromethylarginine; treatment with methylglyoxal-bis(guanylhydrazone) does not significantly influence ADC activity
-
additional information
Q9UWU1, -
1 mM phenylhydrazine does not inactivate the enzyme. No inhibition with D-arginine, L-citrulline, L-lysine, Nalpha-methyl-L-arginine, L-methionine, Nalpha-nitro-L-arginine methyl ester, or L-ornithine
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-Norpyridoxal phosphate
-
reactivation of the apoenzyme
6-Methylpyridoxal phosphate
-
reactivation of the apoenzyme
abscisic acid
B3Y023, -
mRNA level of ADC is induced in the shoots subjected to the concentration of 0.2 mM abscisic acid. After treatment of peach shoots with 0.1 mM abscisic acid to study time-course change of ADC expression over 2 days, are markable increase of the expression level is observed 1 h after the treatment, followed by quick decline until the end of treatment.
alpha-difluoromethylornithine
-
-
arsenic
-
ADC is analyzed in plants treated with arsenic and compared with untreated plants and with positive (TMV-inoculated or DL-beta-aminobutyric acid-treated) controls. ADC transcripts are significantly increased, at both the local and systemic levels, relative to untreated controls.
dithiothreitol
-
stimulates
dithiothreitol
-
absolute requirement
DL-alpha-Difluoromethylarginine
-
plants exposed to 0.1 or 0.5 microM phenanthrene plus DL-alpha-difluoromethylarginine have significantly greater ADC activities when compared with plants treated with DL-alpha-difluoromethylarginine in the absence of phenanthrene
DL-alpha-difluoromethylornithine
-
activates
DL-alpha-difluoromethylornithine
-
ADC activity increases by 21% in plants exposed to DL-alpha-difluoromethylornithine in the absence of phenanthrene
EDTA
-
stimulates
gibberellic acid
-
stimulates
indoleacetic acid
-
stimulates
kinetin
-
stimulates
mercaptoethanol
-
stimulates
phenanthrene
-
concentrations of phenanthrene up to 0.5 microM cause significant increases in the activity of ADC, with a resultant increase in tissue polyamine levels
putrescine
B3Y023, -
treatment of peach shoots from Mochizuki with exogenous putrescine (indirect product of ADC) remarkably induces accumulation of ADC mRNA, incubation of shoots in 1 and 5 mM exogenous putrescine for 2 days leads to obvious and significant increase in endogenous putrescine
-
pyridoxal 5'-phosphate
-
recombinant enzyme, extracts from Trypanosoma cruzi have an about six times higher activity in the presence of pyridoxal 5-phosphate
pyridoxal 5'-phosphate
Paramecium bursaria Chlorella virus-1
-
included in enzyme assay
spermidine
-
ADC is analyzed in plants treated with spermidine and compared with untreated plants and with positive (TMV-inoculated or DL-beta-aminobutyric acid-treated) controls. ADC transcripts are significantly increased, at both the local and systemic levels, relative to untreated controls.
MG-132
P22220
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.
additional information
-
profiles of the steady-state accumulation of Synechocystis ADC transcripts and ADC specific activities under various environmental conditions, e.g. photoheterotrophy, high temperature and high light conditions activate enzyme expression, overview
-
additional information
-
no photoinduction of arginine decarboxylase activity
-
additional information
-
the enzyme is induced by 200 mM NaCl salt stress leading to accumulation of putrescine, during recovery the enzyme expression decreases
-
additional information
Q71SB4
inoculation with the mycorrhizal fungus Suillus variegatus leads to 3.0fold induction of the nezyme in roots and 1.4fold induction in shoots
-
additional information
-
chronic treatment, over 21 days, with glucocorticoids, via dexamethasone, alters endogenous agmatine and arginine decarboxylase levels in the brain, reversible by exogenous agmatine, overview
-
additional information
Q9SNN0
the gene encoding the enzyme is up-regulated by chilling stress in rice seedling leaves, effects of environmental stress, overview, the enzyme is induced by cold stress at 5C and 12C, by drought and by methyljasmonic acid and abscisic acid treatment
-
additional information
-, Q71SB4
ADC gene expression and enzyme activity increase during embryogenesis
-
additional information
B3Y023, -
transcripts of ADC in peach leaves are quickly induced, either transiently or continuously, in response to dehydration, high salinity (200 mM NaCl), low temperature (4C) and heavy metal (0.15 mM CdCl2), but represses by high temperature (37C) during a 2-day treatment, which changes in an opposite direction when the stresses are otherwise removed with the exception of CdCl2 treatment.
-
additional information
-
ADC protein levels and endogenous agmatine levels are significantly increased in the prefrontal cortex, hippocampus, striatum and hypothalamus by immobilization stress. As one element of self-protection mechanisms in the brain, agmatine synthesis is triggered by repeated immobilization through activation of ADC expression, which in turn increases endogenous agmatine levels as an initial protective response to stress.
-
additional information
-
DL-alpha-difluoromethylornithine does not influence the general trend of increased ADC activitiy observed in plants exposed to 0.1 or 0.5 microM phenanthrene
-
additional information
-
increased enzyme activity after wounding of the potatoe
-
additional information
-, P28629
arginine decarboxylase activity is modulated by external pH and active at acidic pH
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.028
-
L-Arg
-
66000 Da enzyme form
0.029
-
L-Arg
-
38000 Da enzyme form
0.03
-
L-Arg
-
-
0.0461
-
L-Arg
-
-
0.049
-
L-Arg
-
23000 Da enzyme form
0.2
-
L-Arg
-
pH 7.5, 37C
0.23
-
L-Arg
-
pH 7.2
0.26
-
L-Arg
-
pH 8.1
0.28
-
L-Arg
-
-
0.45
-
L-Arg
Paramecium bursaria Chlorella virus-1
-
pH 8.2, 37C
0.48
-
L-Arg
-
115000 Da enzyme form
0.48
-
L-Arg
Paramecium bursaria Chlorella virus-1
-
pH 9.0, 40C
0.51
-
L-Arg
-
195000 Da enzyme form
0.65
-
L-Arg
-
-
0.75
-
L-Arg
-
-
0.75
-
L-Arg
-
pH 8.0, 30C
1.73
-
L-Arg
-
-
1.85
-
L-Arg
-
enzyme from seed coat of 4-week-old fruitlets
2.85
-
L-Arg
-
enzyme from fully developed fruit
4.7
-
L-Arg
-
pH 6.0, 70C
5
-
L-Arg
-
double reciprocal plot is biphasic with a Km-value of 10 mM at higher concentrations of L-Arg
5
-
L-Arg
-
wild type enzyme
5.4
-
L-Arg
-
mutant enzyme X128W
7.1
-
L-Arg
-
pH 6.0, 83C
0.03
-
L-arginine
P28629
pH 8.4, 37C, constitutive ArgDC
0.11
-
L-arginine
P22220
untagged ADC
0.2
-
L-arginine
Q9UWU1, -
pH 6.5, 70C
0.31
-
L-arginine
P22220
His-tagged ADC
0.59
-
L-arginine
-
at pH 6.5, 70C
0.63
-
L-arginine
-
at pH 7.5, 37C
0.65
-
L-arginine
P28629
pH 5.2, 37C, inducible ArgDC
0.73
-
L-arginine
Clostridium difficile
-
at pH 7.5, 60C
1.1
-
L-arginine
-
at pH 7.5, 70C
2.2
-
L-arginine
-
at pH 8.5, 30C
5
-
L-arginine
-
pH 3.5, 37C
5.6
-
L-arginine
Q5NT93, -
-
0.233
-
L-canavanine
-
pH 7.5, 37C
1.2
-
L-canavanine
-
-
50
-
L-lysine
Q5NT93, -
-
9.53
-
L-N5-(iminoethyl)-ornithine
-
pH 7.5, 37C
7.5
-
L-ornithine
-
at pH 7.5, 70C
46
-
L-ornithine
Paramecium bursaria Chlorella virus-1
-
pH 9.0, 40C
0.163
-
Ngamma-methyl-L-arginine
-
pH 7.5, 37C
180
-
L-ornithine
Paramecium bursaria Chlorella virus-1
-
pH 8.2, 37C
additional information
-
additional information
-
-
-
additional information
-
additional information
Q8ZHG8
pre-steady-state kinetics of substrate, product, and inhibitor with ADC by single-wavelength stopped-flow spectroscopy, overview
-
additional information
-
additional information
-
steady-state kinetics
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2.3
-
L-Arg
-
mutant enzyme X128W
2.7
-
L-Arg
-
pH 6.0, 83C
5.46
-
L-Arg
-
pH 7.5, 37C
6.9
-
L-Arg
-
wild type enzyme
0.025
-
L-arginine
Clostridium difficile
-
at pH 7.5, 60C
0.21
-
L-arginine
-
at pH 7.5, 37C
0.48
-
L-arginine
-
at pH 8.5, 30C
0.9
-
L-arginine
P22220
untagged ADC
1.4
-
L-arginine
-
at pH 7.5, 70C
2.6
-
L-arginine
Q9UWU1, -
pH 6.5, 70C
6.9
-
L-arginine
-
pH 3.5, 37C
9.9
-
L-arginine
P22220
His-tagged ADC
11
-
L-arginine
-
at pH 6.5, 70C
0.11
-
L-canavanine
-
pH 7.5, 37C
0.419
-
L-N5-(iminoethyl)-ornithine
-
pH 7.5, 37C
1.22
-
Ngamma-methyl-L-arginine
-
pH 7.5, 37C
0.04
-
L-ornithine
-
at pH 7.5, 70C
additional information
-
additional information
-
-
-
additional information
-
additional information
P22220
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.
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.035
-
L-arginine
Clostridium difficile
-
at pH 7.5, 60C
12093
0.22
-
L-arginine
-
at pH 8.5, 30C
12093
0.34
-
L-arginine
-
at pH 7.5, 37C
12093
1.3
-
L-arginine
-
at pH 7.5, 70C
12093
13
-
L-arginine
Q9UWU1, -
pH 6.5, 70C
12093
18
-
L-arginine
-
at pH 6.5, 70C
12093
0.0056
-
L-ornithine
-
at pH 7.5, 70C
12348
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2.77
-
agmatine
-
pH 7.5, 37C
0.0206
-
D-Arg
-
pH 7.5, 37C
0.8
-
DL-alpha-Difluoromethylarginine
Q5NT93, -
-
3.39
-
guanidine
-
pH 7.5, 37C
0.897
-
L-argininamide
-
pH 7.5, 37C
0.189
-
L-arginine methyl ester
-
pH 7.5, 37C
0.327
-
L-Argininic acid
-
pH 7.5, 37C
0.427
-
L-canavanine
-
pH 7.5, 37C
1.53
-
L-Homoarginine
-
pH 7.5, 37C
3.09
-
Methylguanidine
-
pH 7.5, 37C
1.4
-
N-benzylguanidine
-
pH 7.5, 37C
1.93
-
n-propylguanidine
-
pH 7.5, 37C
0.168
-
NG-methyl-D-arginine
-
pH 7.5, 37C
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.8
-
Ca2+
-
IC50: 0.8 mM
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0012
-
P22220
untagged ADC
0.002
-
-
murtant N47A, assay is carried out in 50 mM 2-(N-morpholino)ethanesulfonic acid/NaOH buffer, 50 mM KCl, 1 mM DTT with 4 mM L-arginine and 2 microl [14C] L-arginine
0.0023
-
-
-
0.00738
-
Q5NT93, -
crude extract
0.0096
-
-
-
0.01104
-
Q5NT93, -
heat treatment
0.02394
-
Q5NT93, -
after purification with DEAE-Toyopearl 650M
0.0331
-
P22220
His-tagged ADC
0.0381
-
Q5NT93, -
after purification with DEAE-5PW
0.113
-
-
-
0.132
-
-
mutant E109Q, assay is carried out in 50 mM 2-(N-morpholino)ethanesulfonic acid/NaOH buffer, 50 mM KCl, 1 mM DTT with 4 mM L-arginine and 2 microl [14C] L-arginine
0.151
-
-
crude extract, in 67 mM Tris-HCl (pH 7.5), 3.3 mM EDTA, 3.3 mM dithiothreitol, 0.04 mM pyridoxal 5'-phosphate
0.28
-
Q5JFI4, -
pH 6.0, 70-90C
0.39
-
-
at pH 7.5, 37C
1.014
-
-
wild type enzyme, assay is carried out in 50 mM 2-(N-morpholino)ethanesulfonic acid/NaOH buffer, 50 mM KCl, 1 mM DTT with 4 mM L-arginine and 2 microl [14C] L-arginine
1.026
-
Q5NT93, -
at the semi-final step of purification with HA-1000 column chromatography
1.495
-
-
-
1.5
-
-
at pH 7.5, 37C
2.8
-
-
purified enzyme, in 67 mM Tris-HCl (pH 7.5), 3.3 mM EDTA, 3.3 mM dithiothreitol, 0.04 mM pyridoxal 5'-phosphate
8.1
-
-
purified recombinant enzyme
14.94
-
Q5NT93, -
final step of purification with MonoQ HR 5/5
16.4
-
-
biosynthetic arginine decarboxylase
350
370
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
profiles of the steady-state accumulation of Synechocystis ADC transcripts and ADC specific activities under various environmental conditions, overview
additional information
-
-
arginine-dependent acid resistance assay, overview
additional information
-
-
quantitative determination of polyamine contents in leaves, diurnal changes in polyamine content, arginine and ornithine decarboxylase, and diamine oxidase in tobacco leaves, overview
additional information
-
-
quantitative determination of polyamine contents, overview
additional information
-
-
quantitative determination of agmatine levels in the brain
additional information
-
Q9SNN0
quantitative determination of polyamine and putrescine contents under chilling stress, overview
additional information
-
-
alkaloid profile of cultured hairy roots and in leaves of transgenic and of wild-type plants, overview
additional information
-
-, Q71SB4
quantitative analysis of polyamine contents during zygotic embryo development, polyamine levels correlate with the developmental stage, overview
additional information
-
P22220
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
additional information
-
-
no ADC transcript is detectable on day 5 following TMV inoculation in tobacco plants
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.2
-
-
degradative arginine decarboxylase
5.2
-
P28629
inducible ArgDC
5.2
-
-, P28629
-
6
-
Q5JFI4, -
assay at
6.5
-
Q5NT93, -
assay at pH 6.5, 10 min, 50C
6.5
-
Q9UWU1, -
assay at
7
7.5
-
-
7
-
-
-
7
-
-
-
7.2
7.4
-
-
7.2
-
-
-
7.5
-
Q8ZHG8
assay at
7.8
-
-
assay at
8
9
-
at 60C
8
-
-
-
8
-
-
Tris-HCl buffer
8
-
-
assay at
8.1
-
-
-
8.4
-
-
biosynthetic arginine decarboxylase
8.4
-
P28629
constitutive ArgDC
8.5
-
-
assay at
8.5
-
-
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1.5
5.5
-
activity range
3.5
7
-
pH 3.5: about 50% of maximal activity, pH 7.0: 23% of maximal activity
4
6
Q9UWU1, -
pH 4.0: about 65% of maximal activity, pH 6.0: optimum
4
9
-
about 50% of maximal activity at pH 4 and 9
5
8
-
pH 5.0: about 60% of maximal activity, pH 8.0: about 60% of maximal activity
6.5
9
Q5NT93, -
80% enzyme activity at pH 7.0, 70% enzyme activity at pH 8.0, 50% enzyme activity at pH 9.0
7
11
-
pH 7: about 25% of maximal activity, pH 11: 80% of maximal activity
7.2
8.8
-
pH 7.2: about 45% of maximal activity, pH 8.8: about 35% of maximal activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
50
-
-
30
-
-
assay at
30
-
-
assay at
37
-
-
assay at
37
-
P28629
assay at
37
-
-
assay at
37
-
P22220
assay at
45
-
-
-
50
-
-
around 50C
60
-
-
2fold increase in activity after preincubation at 55C for 10 min
70
90
Q5JFI4, -
assay at
70
-
Q9UWU1, -
assay at
75
-
-
optimum temperature at above 75C
80
-
-
ADC is most active at temperatures above 80C
90
-
-
activity increases up to
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
50
-
20C: about 40% of maximal activity, 50C: about 70% of maximal activity
20
80
-
about 50% of maximal activity at 20C and 80C
30
37
-
30C: maximal activity, 37C: about 35% of maximal activity
37
45
-
37C: about 50% of maximal activity, 45C: maximal activity
40
70
Q5NT93, -
after 10 min incubation at 50C 4fold higher enzyme activity than at 40C, after 10 min incubation at 55C 7fold higher enzyme activity than at 40C, after 10 min incubation at 60C 10fold higher enzyme activity than at 40C, after 10 min incubation at 70C 1.2fold higher enzyme activity than at 40C
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.9
-
Q9SNN0
sequence calculation, ADC1
5.1
-
-
calculated from amino acid sequence
5.2
-
B3Y023, -
predicted from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
about 5% of the activity in aorta
Manually annotated by BRENDA team
-
highest activity of all tissues tested
Manually annotated by BRENDA team
-
about 40% of the activity in aorta
Manually annotated by BRENDA team
-
activity is not affected by hormone deprivation
Manually annotated by BRENDA team
Q5R145
derived from young fruits
Manually annotated by BRENDA team
Q39827
low activity
Manually annotated by BRENDA team
-, Q71SB4
protein and mRNA transcript are present at different phases of mitosis in Scots pine zygotic embryogenesis, ADC gene expression and enzyme activity increase during embryogenesis, overview, localization of ADC gene expression in the cells of primary shoot and root meristem of late embryo and in the mitotic cells of shoot meristem in the late embryo at the cotyledonary stage, in situ immunohistochemic detection, overview
Manually annotated by BRENDA team
-
significantly increased agmatine levels in the prefrontal, entorhinal, and perirhinal cortices in a T-maze training group relative to the control group
Manually annotated by BRENDA team
-
enzyme activity is only present in the early stage of the parasite exponential growth, between 4 and 23 h of cultivation in presence of Arg, with a maximum at 14 h and disappears completely at the mid logarithmic phase. It is never detected during the stationary phase
Manually annotated by BRENDA team
Trypanosoma cruzi RA
-
enzyme activity is only present in the early stage of the parasite exponential growth, between 4 and 23 h of cultivation in presence of Arg, with a maximum at 14 h and disappears completely at the mid logarithmic phase. It is never detected during the stationary phase
-
Manually annotated by BRENDA team
Q5R145
highest activity
Manually annotated by BRENDA team
Q5R145
young fruit, almost no activity in ripe fruit
Manually annotated by BRENDA team
B3Y023, -
the fruit collected at 107 days after full bloom shows stronger expression than that at 23 days after full bloom
Manually annotated by BRENDA team
-
increasing activity during developmental stages, high activity in final stage
Manually annotated by BRENDA team
Rhizophora apiculata Bl
-
increasing activity during developmental stages, high activity in final stage
-
Manually annotated by BRENDA team
-
about 40% of the activity in aorta
Manually annotated by BRENDA team
-
about 85% of the activity in aorta
Manually annotated by BRENDA team
Q5R145
young leaves have higher activity than mature leaves
Manually annotated by BRENDA team
-
vascular tissue
Manually annotated by BRENDA team
-
no significant effect of sorbitol or NaCl treatment
Manually annotated by BRENDA team
-
increased activity after mechanical wounding, highest activity 1-2 h after wounding
Manually annotated by BRENDA team
-
diurnal changes in enzyme activity and polyamine contents, overview
Manually annotated by BRENDA team
B3Y023, -
young leaves have higher ADC expression levels
Manually annotated by BRENDA team
Q9SNN0
Adc1 is expressed in leaf, root and stem
Manually annotated by BRENDA team
-
about 75% of the activity in aorta
Manually annotated by BRENDA team
-
significantly increased agmatine levels in the prefrontal, entorhinal, and perirhinal cortices in a T-maze training group relative to the control group
Manually annotated by BRENDA team
-
significantly increased agmatine levels in the prefrontal, entorhinal, and perirhinal cortices in a T-maze training group relative to the control group
Manually annotated by BRENDA team
-
tips, junction between hypocotyls and roots, vascular tissue
Manually annotated by BRENDA team
-
great increase of ADC2 mRNA level at low temperature cultivation and after salt exposure, ADC1 and ADC2 in mature plants
Manually annotated by BRENDA team
-
significantly increased activity in roots grown for 24 h in the presence of 260 mM NaCl or 360 mM sorbitol
Manually annotated by BRENDA team
Q39827
tips
Manually annotated by BRENDA team
Q71SB4
localization in specific root parenchyma cells adjacent to tracheids and in mitotic cells of the root apical meristem, difference in ADC transcript localization between roots inoculated and non-inoculated with mycorrhizal fungus
Manually annotated by BRENDA team
Q9SNN0
Adc1 is expressed in leaf, root and stem
Manually annotated by BRENDA team
-
developing seed
Manually annotated by BRENDA team
-
of both 4-week-old avocado fruitlet and fully developed fruit
Manually annotated by BRENDA team
-
shotts of seedlings
Manually annotated by BRENDA team
-
ADC2 mRNA hardly detectable when cultivated at 22C
Manually annotated by BRENDA team
Q39827
high level in sieve tubes of main root in 6-8 days old seedlings
Manually annotated by BRENDA team
-
great increase of ADC2 mRNA level at low temperature cultivation and after salt exposure, ADC1 but not ADC2 accumulated in shoots of mature plants
Manually annotated by BRENDA team
-
germinating
Manually annotated by BRENDA team
Q9SNN0
Adc2 expression is restricted to stem tissue, Adc1 is expressed in leaf, root and stem
Manually annotated by BRENDA team
-
about 60% of the activity in aorta
Manually annotated by BRENDA team
-
about 15% of the activity in aorta
Manually annotated by BRENDA team
additional information
-
profiles of the steady-state accumulation of Synechocystis ADC transcripts and ADC specific activities under various environmental conditions
Manually annotated by BRENDA team
additional information
Q39827
no activity detectable in lateral roots emergence region
Manually annotated by BRENDA team
additional information
Q71SB4
Pinus sylvestris forms a symbiosis with ectomycorrhizal fungi, e.g. Suillus variegatus, that entirely cover short roots with a hyphal mantle, inducing effects in different tissues, overview
Manually annotated by BRENDA team
additional information
B3Y023, -
expression levels of PpADC in different tissues of peach are spatially and developmentally regulated
Manually annotated by BRENDA team
additional information
-
not detected in roots
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
in photosynthetic tissues mainly located in
Manually annotated by BRENDA team
Q9SNN0
the enzyme sequence contains a putative N-terminal chloroplastic signal peptide
Manually annotated by BRENDA team
-
most activity is associated with
Manually annotated by BRENDA team
-
in non-photosynthetic tissues mainly located in
Manually annotated by BRENDA team
-
the activity is equally divided between the soluble and pellet fractions
-
Manually annotated by BRENDA team
-
the activity is equally divided between the soluble and pellet fractions
-
Manually annotated by BRENDA team
-
highly if not exclusively associated with mitochondrial membrane
Manually annotated by BRENDA team
additional information
-
no activity in cytosol
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Vibrio vulnificus (strain YJ016)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
17940
-
Q9UWU1, -
inactive proenzyme, mass spectrometry
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
25000
-
-
His-tagged-AaxB protein from strain D/UW-3, SDS-PAGE
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
55900
-
-
gel filtration
58000
-
Q5NT93, -
SDS-PAGE
58000
-
-
SDS-PAGE
63000
-
-
SDS-PAGE
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
66000
-
P22220
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
68000
-
Q9SNN0
ADC2, predicted from amino acid sequence
74000
-
Q9SNN0
ADC1, predicted from amino acid sequence
77700
-
B3Y023, -
predicted from amino acid sequence
80000
-
Q9UWU1, -
His10-tagged enzyme, gel filtration
88000
-
-
recombinant enzyme, gel filtration
99400
-
Q5JFI4, -
gel filtration
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
120000
-
Q5NT93, -
gel filtration
163100
-
-
apo-ADC, light-scattering analysis
176000
-
-
gel filtration
178000
-
-
holo-ADC, light-scattering analysis
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
220000
-
-
gel filtration
232000
-
-
gel filtration
240000
-
-
gel filtration
240000
-
-
gel filtration
327000
-
-
gel filtration
800000
-
-, P28629
gel filtration
820000
-
-
-
additional information
-
-
-
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
Q5R145
x * 78000, calculated from the deduced amino acid sequence
?
Q9SNN0
x * 74000, about, sequence calculation, ADC1
?
-
x * 24000, two bands with a molecular mass of approximately 24000 Da and 54000 D corresponding to ADC protein are detected by SDS-PAGE; x * 54000, two bands with a molecular mass of approximately 24000 Da and 54000 D corresponding to ADC protein are detected by SDS-PAGE
decamer
-
10 * or 1 * 82000, degradative arginine decarboxylase
decamer
-
10 * 82000-96000, SDS-PAGE
decamer
-
decamer dissociates in stages rather than all at once to a dimer
decamer
-
decamer-dimer transition is sequential, occuring in five steps, two protons must ionize and two Na+ ions bind at each step
decamer
-, P28629
pentamer of homodimers, X-ray crystallography
dimer
-
2 * or 10 * 82000, degradative arginine decarboxylase
dimer
-
decamer dissociates in stages rather than all at once to a dimer
dimer
-
decamer-dimer transition is sequential, occuring in five steps, two protons must ionize and two Na+ ions bind at each step
dimer
Q9SI64
the enzyme is a head-to-tail homodimer with two active sites acting in trans across the interface of the dimer
dimer
-
in solution at pH 8.0, light-scattering analysis
dimer
-
stabilized by two inter-subunit disulfide bonds, structural modeling
dimer
Q5NT93, -
-
heterodimer
P22220
1 * 42000 + 1 * 24000, determined by SDS-polyacrylamide gel electrophoresis
hexamer
-
6 * 36000-36500, SDS-PAGE
hexamer
-
3 * alpha 11000-13000 + 3 * beta 5000-7000, SDS-PAGE
hexamer
-
3 * 16000, alpha subunit, + 3 * 9000, beta-subunit, trimeric dimer, (alpha/beta)3, SDS-PAGE
hexamer
Q5JFI4, -
6 * 12600 + 6 * 4500, (alphabeta)6 complex, denaturant gel electrophoresis
octamer
Q9UWU1, -
4 * 6123 + 4 * 11759, mass spectrometry, SDS-PAGE
octamer
-
4 * 6123 + 4 * 11759, mass spectrometry, SDS-PAGE
-
tetramer
-
4 * 74000, biosynthetic arginine decarboxylase
tetramer
-
4 * 58900, SDS-PAGE
tetramer
-
4 * 74000, crystal structure analysis
tetramer
-
4 * 78000, subunit mass calculated from the deduced amino acid sequence, SDS-PAGE
tetramer
-, Q0PAC6
x-ray crystallography
tetramer
P21170
x-ray crystallography
tetramer
Q7MK24
x-ray crystallography
tetramer
Campylobacter jejuni NCTC 11168
-
x-ray crystallography
-
tetramer
Mycobacterium smegmatis TMC 1546
-
4 * 58900, SDS-PAGE
-
trimer
-
3 * 74000, SDS-PAGE
trimer
-
3 * 63000, SDS-PAGE
trimer
-
Mutant E109Q, the structure contains 2 complete trimers in the asymmetric unit, the active sites of each trimer are located between adjacent protomers. All 6 protomers are fully processed and contain the product agmatine at the active site. The presence of the product agmatine confirms that the mutant is active because the substrate arginine is added to the protein during crystallization.; Mutant N47A, the structure contains 2 complete trimers in the asymmetric unit, the active sites of each trimer are located between adjacent protomers. The mutant protein does not show complete processing in all protomers. The first protomer of N47A is processed showing clear cleavage of the protomer to form the beta-chain (residues 1-52) and the alpha-chain (residues 53-165). A second protomer is unprocessed, showing clear density connecting residues Ser52 and Ser53. The final protomer in the first trimer can not easily be classified as either processed or unprocessed and is likely to be a mixture of the two states. The density between Ser52 and Ser53 is weak, density is also present corresponding to the pyruvoyl group and the product agmatine.
hexamer
Chlamydia pneumoniae Kajaani
-
3 * 16000, alpha subunit, + 3 * 9000, beta-subunit, trimeric dimer, (alpha/beta)3, SDS-PAGE
-
additional information
-
effects of substrate, coenzyme, and positive and negative effectors on the enzyme structure
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
additional information
-
Synechocystis ADCs have a putative extra domain, which might be involved in the posttranslational regulation of ADC activity, structural modeling, overview
additional information
Paramecium bursaria chlorella virus
-
the mobile loop, the K148-loop, is observed in a closed, substrate-bound conformation, this loop adopts different conformations throughout the catalytic cycle, overview
additional information
Q8ZHG8
the enzyme exists in two different conformational states, one that binds ligand and one that does not, overview
additional information
-
the recombinant enzyme self-cleaved to form a reactive pyruvoyl group, and the subunits assembled into a thermostable (alpha/beta)3 complex
additional information
-
structural modelling
additional information
Chlamydia pneumoniae Kajaani
-
the recombinant enzyme self-cleaved to form a reactive pyruvoyl group, and the subunits assembled into a thermostable (alpha/beta)3 complex
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
proteolytic modification
Q9SI64
maximal activity of ADC1 in yeast requires the presence of general protease genes, and it is likely that dimer formation precedes proteolytic processing of the ADC pre-protein monomer
proteolytic modification
-
the protein is synthesized as a 66000 Da precursor that is proteolytically processed into two polypeptides of 42000 and 24000 da
proteolytic modification
P22220
post-translational proteolysis of ADC depends on the presence of a protease-sensitive loop in the structure of the protein
proteolytic modification
-
the recombinant enzyme self-cleaved to form a reactive pyruvoyl group, and the subunits assembled into a thermostable (alpha/beta)3 complex
proteolytic modification
Chlamydia pneumoniae Kajaani
-
the recombinant enzyme self-cleaved to form a reactive pyruvoyl group, and the subunits assembled into a thermostable (alpha/beta)3 complex
-
proteolytic modification
-
the enzyme is formed by self-cleavage of a proenzyme into a 5000 Da subunit and a 12000 Da subunit that contains a reactive pyruvoyl group
proteolytic modification
-
the pyruvoyl group of the enzyme is generated by an autocatalytic internal serinolysis reaction at Ser53 in the proenzyme resulting in two polypeptide chains. Asn47, Ser52, Ser53, Ile54, and Glu109 are proposed to play roles in the self-processing reaction
proteolytic modification
Q9UWU1, -
synthesized as an inactive proenzyme
pyruvoyl group formation
Q9UWU1, -
the enzyme is synthesized as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue (Ser82) via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme
proteolytic modification
-
synthesized as an inactive proenzyme
-
pyruvoyl group formation
-
the enzyme is synthesized as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue (Ser82) via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme
-
proteolytic modification
Q5JFI4, -
synthesized as an inactive proenzyme
pyruvoyl group formation
Q5JFI4, -
the enzyme is synthesized as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue (Ser44) via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme
proteolytic modification
-
existence of an autocatalytic proteolytic property of ADC protein, which possibly regulates posttranslationally the levels and/or the activity of ADC enzyme
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hanging drop vapor diffusion method, at 16C using 50 mM calcium chloride, 100 mM bis-tris pH 6.5, 30% (w/v) polyethylene glycol monomethyl ether 550, 10 mM putrescine
-
in complex with pyridoxal 5'-phosphate, microbatch method, using 100 mM bis-Tris propane pH 7.0 and 1.88 M sodium sulfate
-, Q0PAC6
hanging drop vapor diffusion method, using 1 M lithium sulfate monohydrate, 0.1 M Na citrate tribasic dihydrate pH 5.6, and 0.5 M ammonium sulfate
-
in complex with a sulfate ion, microbatch method, using 100 mM HEPES pH 8.5 and 1.6 M ammonium sulfate
P21170
sparse matrix method, using 100 mM MES, pH 6.5, 13% PEG 8000, and 400 mM sodium acetate, at 20C
-, P28629
crystallization of enzyme labeled with selenomethionine, enzyme-agmatine complex and S53A mutant structure, hanging drop method, determination of structure at 1.4 A, crystals belong to space group P2, with cell dimensions a = 56.77 A, b = 92.99 A, c = 87.23 A, and beta = 94.84
-
the N47A and E109Q mutant proteins are co-crystallized at 22C with 1-2 mM arginine, the hanging-drop vapor-diffusion method is used. Crystals are grown in 17-20% PEG 2000, 10% 2-methyl-2,4-pentanediol, 2.5% glycerol, 100 mM HEPES pH 6.7-7.3, 0.5 mM beta-octylglucoside, 0.5 mM ethylenediaminetetraacetic acid and 10 mM dithiothreitol.
-
purified recombinant His6-tagged wild-type and mutant enzymes, 0.005 ml of 20 mg/ml protein in 10 mM HEPES, pH 7.2, 50 mM NaCl, 1 mM DTT, 0.5 mM EDTA, pH 8.0, and 0.03% v/v Brij-35, with or without 5 mM agmatine, are mixed with an equal volume of the crystallization solution containing 6% PEG 8000, 100 mM imidazole, pH 7.5, 200 mM calcium acetate, sitting drop vapour diffusion, 16C, crystals generally grow within 24 h, cryoprotection with a solution containing the mother liquor and 25-30% 2-methyl-2,4-pentanediol, X-ray diffraction structure determination and analysis at 1.95 A and 1.8 A resolution for the free and agmatine-bound enzyme, molecular modeling
Paramecium bursaria chlorella virus
-
in complex with L-Arg, sitting drop vapor diffusion method, using 0.1 M HEPES, pH 7.0, 0.2 M MgCl2, 12% (w/v) PEG-4000
Q7MK24
hanging drop vapor diffusion method, in the presence and absence of Mg2+ and pyridoxal 5-phosphate
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
7.5
Q5NT93, -
more than 80% enzyme activity, decreased enzyme activity at higher pH
7.9
-
-
maximal activity
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
-
-
4 h, 80% loss of activity in mitochondrial/synaptosomal membranes of brain
35
-
Q5NT93, -
without pyridoxal 5'-phosphate, 50% redsidual enzyme activity
50
-
-
30 min, stable
50
-
-
10 min, the purified enzyme retains 48% of maximal activity
60
-
-
10 min, 50% loss of activity
60
-
Q5NT93, -
with pyridoxal 5'-phosphate, 54% residual enzyme activity
70
80
-
at 70C, full enzyme activity is retained, even after 30 min of incubation. Enzyme activity is almost completely abolished within 5 min by incubating the enzyme at 80C
70
-
-
5 min, 95% loss of activity
90
-
Q9UWU1, -
pH 6.0, 10 min, enzyme retains 80% of ist original activity
100
-
-
10 min, the purified enzyme retains 13% of maximal activity
121
-
-
20 min, 50% loss of activity
125
-
-
30 min, 84% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
halt life in vivo is 150 min
-
dialysis against Cys causes irreversible inactivation
-
freeze-thawing or lyophilization inactivates
-
enzyme resists proteolytic cleavage by trypsin, pepsin, carboxypeptidase A, or papain
-
enzyme retains full activity in presence of 1% w/v SDS at 70C
-
freeze-thawing or lyophilization completely inactivates
-
at 50C in absence of PALP lost of 90% enzyme activity within 10 min, no enzyme activity after heating at 70C for 60 min in presence of PALP
Q5NT93, -
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-15C, 50% loss of activity after 1 week
-
-80C, stable for at least several weeks
-
-20C, labile, even in presence of 20% glycerol
-
0-2C, 70% loss of activity after 5 days
-
-20C, about 30% loss of activity after 60 d
-
4C, 50% loss of activity after overnight storage of membrane suspension
-
4C, 1 month, no lost of enzyme activity, pH 6.0-7.5
Q5NT93, -
50C, absence of PALP, 10 min, only 10% residual activity
Q5NT93, -
70C, presence of PALP, 60 min, no residual activity
Q5NT93, -
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
P22220
HiTrap Chelating HP column chromatography
-
Ni2+-chelating affinity column chromatography and Superdex 200 gel filtration
-
HisTrap column chromatography and Superdex 75 gel filtration
-, Q0PAC6
recombinant His10-tagged enzyme from Escherichia coli strain Bl21(DE3) by nickel affinity chromatography, recombinant untagged enzyme from Escherichia coli strain Bl21(DE3) by anion exchange chromatography, most of the protein is found in the insoluble portion of cell lysate
-
HiTrap Chelating HP column chromatography
Chloroflexus aurantiacus, Clostridium difficile
-
recombinant protein using GST-tag
-
biosynthetic arginine decarboxylase and synthetic arginine decarboxylase
-
HisTrap column chromatography and Superdex 75 gel filtration
P21170
Ni-NTA column chromatography, HiTrap Q column chromatography, and DEAE Sepharose column chromatography
-
nickel chelating column chromatography and Superdex 200 gel filtration
-, P28629
HiTrap Chelating HP column chromatography
-
purification and cleavage of the N-terminal His-tag are performed
-
partially by subcellular fractionation
-
recombinant protein using His-tag
Paramecium bursaria Chlorella virus-1
-
2024fold after final purification step with MonoQ HR 5/5
Q5NT93, -
recombinant enzyme
Q5JFI4, -
Ni2+-affinity column chromatography and gel filtration
Q7MK24
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
Q8ZHG8
recombinant protein using His-tag
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
construction of negative mutant
-
expressed in hairy roots of Lotus corniculatus
-
expressed in Trypanosoma cruzi, which lacks arginine decarboxylase in wild type
-
expression in Escherichia coli
-
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.
P22220
expressed in Escherichia coli BL21(DE3) cells
-
gene ADC, phylogenetic analysis and phylogeny reconstruction, overview
-
expressed in Escherichia coli BL21(DE3) cells
-, Q0PAC6
gene CPn1032, expression of untagged and N-terminally His10-tagged enzyme in Escherichia coli strain Bl21(DE3), CPn1032 expression complements the adiA null mutation in Escherichia coli strain DEG0121, which shows low arginine decarboxylase enzyme activity and is deficient in AdiC transporter
-
expressed in Escherichia coli BL21(DE3) cells
Chloroflexus aurantiacus, Clostridium difficile
-
gene ADC, phylogenetic analysis and phylogeny reconstruction, overview
-
expressed in Arabidopsis thaliana ecotype Col-0
-
expressed in Oryza sativa
-, Q9SCF0
gene ADC, phylogenetic analysis and phylogeny reconstruction, overview
-
expressed in Escherichia coli BL21 as GST-fusion protein
-
expressed in Escherichia coli BL21(DE3) cells
P21170
expressed in the T7 expression system as a cleavable poly-Histagged fusion construct in Escherichia coli strain Rosetta (DE3) pLysS
-
gene adiA, expression of untagged and N-terminally His10-tagged wild-type enzyme and inactivated mutant in strain BW25113
P28629
expressed in Escherichia coli BL21(DE3) cells
-
expression in COS-7 cells
-
the hexahistidine tagged human ADC gene is delivered into mouse fibroblast cell line (NIH3T3) using retroviral vector and transfected into the PT-67 cell line
-
gene ADC, expression analysis under salt stress in calli, overview
-
Escherichia coli strain MachI is used as a recipient for transformations during plasmid construction and for plasmid propagation and storage. Site-directed mutagenesis is performed on pPRDC.19. The mutant plasmids are transformed into Escherichia coli B834 (DE3) competent cells.
-
expression in Escherichia coli
-
expressed in Arabidopsis thaliana
Q71S28
expression of the enzyme in transformed hairy root lines in sense and antisense orientation, expression analysis
-
overexpression in Escherichia coli
-
gene ADC1, cloning from genomic DNA, DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic analysis, expression analysis
Q9SNN0
expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
Paramecium bursaria chlorella virus
-
expression as His-tag fusion protein in Escherichia coli
Paramecium bursaria Chlorella virus-1
-
expression of sense and anti-sense constructs
Q71SB4
gene ADC, phylogenetic analysis and phylogeny reconstruction, overview
-
rapid amplification of cDNA ends (RACE) give rise to a full-length ADC cDNA (PpADC) with a complete open reading frame of 2178 bp, encoding a 725 amino acid polypeptide.
B3Y023, -
expression in Escherichia coli strain DE3
Q5NT93, -
expression in Escherichia coli. The phylogeny of the crenarchaeal homologs suggests that the arginine decarboxylase gene evolves from a single duplication of an ancestral S-adenosylmethionine decarboxylase gene early in the crenarchaeota
Q9UWU1, -
profiles of the steady-state accumulation of Synechocystis ADC transcripts and ADC specific activities under various environmental conditions, overview
-
expressed in Escherichia coli
Q5JFI4, -
gene ADC, phylogenetic analysis and phylogeny reconstruction, overview
-
expressed in Escherichia coli BL21(DE3) cells
Q7MK24
gene ADC, phylogenetic analysis and phylogeny reconstruction, overview
-
expression in Escherichia coli
-
expressed as His-tag fusion protein in Escherichia coli BL21(DE3)pLysE
-
gene speA, expression of His-tagged enzyme in Escherichia coli
Q8ZHG8
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ADC is active early during pollen hydration and germination in vitro, ADC activity is activated during pollen germination
-
after exposure to 0.2 mM methyl jasmonate for 6 h, the intensity of the Adc mRNA signal fell by approximately 90%, and after 24 h of treatment it returns to near the original level
-
ADC protein and transcript are increasingly expressed at early stages of hop internode culture (12 h). Protein and transcript continue accumulating until organogenic nodule formation after 28 days, decreasing thereafter
-
salicylic acid treatment results in a significant increase in the expression of ADC after 3 h
Q71S28
relative expression level for arginine decarboxylase related gene is significantly higher for acid adapted cells
-
relative expression level for arginine decarboxylase related gene is significantly higher for acid adapted cells
Salmonella enterica subsp. enterica serovar Typhimurium CECT 44, Salmonella enterica subsp. enterica serovar Typhimurium CECT 443
-
-
in enteroinvasive strains the presence of CadC reduces the expression of the arginine decarboxylase encoding gene adiA
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C524A
Q9SI64
91.8% reduction of activity compared to wild-type enzyme. When the k136A/pYES2 and C524A/pYX243 ADC1 plasmids are coexpressed in the same yeast cells, there is about 25% functional rescue of ADC activity
K136A
Q9SI64
97.7% reduction of activity compared to wild-type enzyme. When the k136A/pYES2 and C524A/pYX243 ADC1 plasmids are coexpressed in the same yeast cells, there is about 25% functional rescue of ADC activity
T52S
-
site-directed mutagenesis, the mutant enzyme is significantly impaired in proteolytic self-cleavage
T52S
Chlamydia pneumoniae Kajaani
-
site-directed mutagenesis, the mutant enzyme is significantly impaired in proteolytic self-cleavage
-
E109Q
-
E109Q mutation reduces the activity by 7.7fold compared to the wild type enzyme, reduced decarboxylation activity results in part from incomplete pyruvoyl-group formation
N47A
-
The activity of N47A is reduced by 500fold compared with the wild type protein
T142A
Paramecium bursaria chlorella virus
-
site-directed mutagenesis, structural comparison to the wild-type enzyme, overview
D296E
Paramecium bursaria Chlorella virus-1
-
responsible for changes in substrate specificity
X128W
-
the purified X128W variant protein catalyzes the decarboxylation of L-arginine with a pH optimum near 3.4 with increased Km and decreased kcat values compared to the wild type enzyme
additional information
P28629
construction of an enzyme deletion null mutant, complementation by expression of the enzyme from Chlamydophila pneumoniae
S53A
-
nonprocessing mutant enzyme
additional information
-
downregulation of nicotine biosynthesis via antisense approach, diminishing of ADC activity in transformed roots, alkaloid profile of cultured hairy roots and regenerated transgenic plants, growth of transformed roots is unaltered, overview
E296D
Paramecium bursaria Chlorella virus-1
-
increased Km and decreased turnover with L-Arg, minor effect on Km with L-ornithine, decreased turnover with L-ornithine
additional information
Q9UWU1, -
modeling and activity of a chimeric arginine decarboxylase/S-adenosylmethionine decarboxylase proteins. A chimeric protein containing the beta subunit of arginine decarboxylase (SSO0536) and the alpha subunit of S-adenosylmethionine decarboxylase (SSO0585) has arginine decarboxylase activity and no S-adenosylmethionine decarboxylase activity, implicating residues responsible for substrate specificity in the beta subunit
additional information
-
modeling and activity of a chimeric arginine decarboxylase/S-adenosylmethionine decarboxylase proteins. A chimeric protein containing the beta subunit of arginine decarboxylase (SSO0536) and the alpha subunit of S-adenosylmethionine decarboxylase (SSO0585) has arginine decarboxylase activity and no S-adenosylmethionine decarboxylase activity, implicating residues responsible for substrate specificity in the beta subunit
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
agriculture
B3Y023, -
generation of stress-resistent plants
drug development
Q8ZHG8
the enzyme is an attractive target for drug design