Information on EC 3.5.3.6 - arginine deiminase

Word Map on EC 3.5.3.6
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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

EC NUMBER
COMMENTARY hide
3.5.3.6
-
RECOMMENDED NAME
GeneOntology No.
arginine deiminase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-arginine + H2O = L-citrulline + NH3
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amidine hydrolysis
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Arginine biosynthesis
-
-
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
L-arginine degradation V (arginine deiminase pathway)
-
-
L-proline biosynthesis II (from arginine)
-
-
Metabolic pathways
-
-
arginine metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
L-arginine iminohydrolase
Also acts on canavanine.
CAS REGISTRY NUMBER
COMMENTARY hide
9027-98-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
strain 250; strain EQUILAIT
-
-
Manually annotated by BRENDA team
strain 250
-
-
Manually annotated by BRENDA team
strain EQUILAIT
-
-
Manually annotated by BRENDA team
strain CUC-3
-
-
Manually annotated by BRENDA team
strain Microenos HP
-
-
Manually annotated by BRENDA team
strain Microenos HP
-
-
Manually annotated by BRENDA team
several strains, isolated from wine
-
-
Manually annotated by BRENDA team
subsp. cremonis strain MG1363
-
-
Manually annotated by BRENDA team
strain ATCC 7962
-
-
Manually annotated by BRENDA team
strain 67-166
-
-
Manually annotated by BRENDA team
strain G230
-
-
Manually annotated by BRENDA team
strain 14027
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
no activity in Lactobacillus brevis
strain ML30
-
-
Manually annotated by BRENDA team
no activity in Lactobacillus brevis ML30
strain ML30
-
-
Manually annotated by BRENDA team
no activity in Lactobacillus delbrueckii
strain CUC-1
-
-
Manually annotated by BRENDA team
no activity in Lactobacillus delbrueckii CUC-1
strain CUC-1
-
-
Manually annotated by BRENDA team
no activity in Lactobacillus plantarum
strain Viniflora LP and strain 49
-
-
Manually annotated by BRENDA team
no activity in Loktanella hongkongensis
-
-
-
Manually annotated by BRENDA team
no activity in Marinovum algicola
-
-
-
Manually annotated by BRENDA team
no activity in Marinovum algicola ATCC 51442
-
-
-
Manually annotated by BRENDA team
no activity in Oenococcus oeni
strain Microenos B3, strain ML34, strain PSU-1, strain L181 and strain Microenos B
-
-
Manually annotated by BRENDA team
no activity in Pediococcus sp.
strain 44.40, strain C5, strain CUC-4, strain 93 and strain 272
-
-
Manually annotated by BRENDA team
no activity in Phaeobacter gallaeciensis BS107
-
-
-
Manually annotated by BRENDA team
strain 1008
-
-
Manually annotated by BRENDA team
strain 122
-
-
Manually annotated by BRENDA team
strain 2035
-
-
Manually annotated by BRENDA team
strain 2043
-
-
Manually annotated by BRENDA team
strain 252
-
-
Manually annotated by BRENDA team
strain DSIR-A
-
-
Manually annotated by BRENDA team
strain DSIR-B
-
-
Manually annotated by BRENDA team
strain DSIR-C
-
-
Manually annotated by BRENDA team
strain Er1a
-
-
Manually annotated by BRENDA team
strain Ey2d
-
-
Manually annotated by BRENDA team
strain IOEB 8406 containing the arcR, A, B, C, D1, and D2 cluster
-
-
Manually annotated by BRENDA team
strain L181
-
-
Manually annotated by BRENDA team
strain MCW
-
-
Manually annotated by BRENDA team
strain Microenos B2
-
-
Manually annotated by BRENDA team
strain Microoenos B
-
-
Manually annotated by BRENDA team
strain ML34
-
-
Manually annotated by BRENDA team
strain OENO
-
-
Manually annotated by BRENDA team
strain PSU-1
-
-
Manually annotated by BRENDA team
strain Vinoflora Oenos
-
-
Manually annotated by BRENDA team
strain CGMCC 2039, isolated from soil
UniProt
Manually annotated by BRENDA team
strain CGMCC2039
UniProt
Manually annotated by BRENDA team
strain CC5A
-
-
Manually annotated by BRENDA team
strain CC5A
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain TV 10, strain MR-5 and strain MR-100
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
agmatine-L-Arg + H2O
N5-carbamoyl-N2-[4-(carbamoylamino)butyl]-L-ornithine + NH3
show the reaction diagram
-
3.2% activity compared to L-Arg
-
-
?
benzoyl-L-arginine ethyl ester + H2O
benzoyl-L-citrulline ethyl ester + NH3
show the reaction diagram
bradykinin-L-Arg + H2O
bradykinin-L-citrulline + NH3
show the reaction diagram
-
18.8% activity compared to L-Arg
-
-
?
D-Arg + H2O
?
show the reaction diagram
-
26.4% activity compared to L-Arg
-
-
?
D-Arg + H2O
D-citrulline + NH3
show the reaction diagram
-
0.38% of the activity with L-Arg
-
-
?
homoarginine + H2O
(2S)-2-amino-6-[(aminocarbonyl)amino]hexanoic acid + NH3
show the reaction diagram
-
50% activity compared to L-Arg
-
-
?
KRPPGFSPL + H2O
L-lysyl-N5-carbamoyl-L-ornithyl-L-prolyl-L-prolylglycyl-L-phenylalanyl-L-seryl-L-prolyl-L-leucine + NH3
show the reaction diagram
-
3.1% activity compared to L-Arg
-
-
?
L-alpha-amino-beta-guanidinepropionic acid + H2O
2-amino-3-carbamoylpropionic acid + NH3
show the reaction diagram
-
-
-
-
?
L-alpha-amino-gamma-guanidinobutyric acid + H2O
2-amino-4-carbamoylbutanoic acid + NH3
show the reaction diagram
-
-
-
-
?
L-Arg + H2O
citrulline + NH3
show the reaction diagram
L-Arg + H2O
L-citrulline + NH3
show the reaction diagram
L-arginine + H2O
L-citrulline + NH3
show the reaction diagram
L-arginine ethyl ester + H2O
?
show the reaction diagram
L-arginine hydroxamate + H2O
?
show the reaction diagram
-
68.2% activity compared to L-Arg
-
-
?
L-argininic acid + H2O
(2S)-5-[(aminocarbonyl)amino]-2-hydroxypentanoic acid + NH3
show the reaction diagram
-
0.032% of the activity with L-Arg
-
-
?
L-canavanine + H2O
(2S)-2-amino-4-[[(aminocarbonyl)amino]oxy]butanoic acid + NH3
show the reaction diagram
-
2.3% of the activity with L-Arg
-
-
?
L-canavanine + H2O
O-ureido-L-homoserine + NH3
show the reaction diagram
L-canavanine + H2O
O-ureidohomoserine + NH3
show the reaction diagram
-
via enzyme Cys-bound S-alkyl-thiouronium intermediate, residues Asp166 and Asp280 are involved, overview
product identification by mass spectrometry
-
?
L-canavanine-L-Arg + H2O
O-ureido-L-homoserine + NH3
show the reaction diagram
-
2.5% activity compared to L-Arg
-
-
?
L-homoarginine + H2O
(2S)-2-amino-6-[(aminocarbonyl)amino]hexanoic acid + NH3
show the reaction diagram
-
0.05% of the activity with L-Arg
-
-
?
L-nitroarginine + H2O
NH3 + nitrocitrulline
show the reaction diagram
-
-
-
-
?
L-Pro-L-Arg-L-Phe + H2O
?
show the reaction diagram
-
3.4% activity compared to L-Arg
-
-
?
L-Pro-L-Phe-L-Arg + H2O
?
show the reaction diagram
-
78.2% activity compared to L-Arg
-
-
?
N-alpha-benzoyl-L-arginine + H2O
N-alpha-benzoyl-L-citrulline + NH3
show the reaction diagram
Nalpha-benzoyl-L-arginine + H2O
?
show the reaction diagram
Nalpha-methyl-L-Arg + H2O
Nalpha-methyl-L-citrulline + NH3
show the reaction diagram
-
0.75% of the activity with L-Arg
-
-
?
Nomega-amino-Arg + H2O
L-citrulline + hydrazine
show the reaction diagram
-
-
-
?
Nomega-amino-L-arginine + H2O
hydrazine + L-citrulline
show the reaction diagram
Nomega-amino-L-arginine + H2O
L-citrulline + diamine
show the reaction diagram
-
-
-
?
Nomega-hydroxy-L-arginine + H2O
Nomega-hydroxy-L-citrulline + NH3
show the reaction diagram
-
2.1% activity compared to L-Arg
-
-
?
Nomega-methyl-Arg + H2O
L-citrulline + methylamine
show the reaction diagram
-
-
-
?
Nomega-methyl-L-arginine + H2O
L-citrulline + methylamine
show the reaction diagram
-
-
-
?
protein L-Arg + H2O
protein L-citrulline + NH3
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-Arg + H2O
citrulline + NH3
show the reaction diagram
L-arginine + H2O
L-citrulline + NH3
show the reaction diagram
protein L-Arg + H2O
protein L-citrulline + NH3
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
PAD does not need a cofactor for catalysis and stability
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
(NH4)2SO4
-
optimal activity in presence of 2.0 M, 48% of the activation with NaCl
CdCl2
-
optimal activity in presence of 5.0 M, 52% of the activation with NaCl
Co2+
-
required, maximal activity at 0.5 mM CoCl2
MgCl2
-
increases the activity 8fold at 20 mM
Na2HPO4
-
optimal activity in presence of 2.0 M, 77% of the activation with NaCl
Na2SO4
-
optimal activity in presence of 1.5 M, 39% of the activation with NaCl
NaBr
-
optimal activity in presence of 3.0 M, 24% of the activation with NaCl
NaCl
-
optimal activity in presence of 3.5 M
RbCl
-
optimal activity in presence of 5.0 M, 53% of the activation with NaCl
additional information
-
PAD is not a metalloenzyme
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2S)-2-amino-5-(N''-cyanocarbamimidamido)pentanoic acid
-
-
5,5'-dithiobis(2-nitrobenzoic acid)
agmatine
aminoguanidine
beta-amyloid peptide(1-28)
-
not-containing arginine
-
beta-amyloid peptide(1-42)
-
containing arginine
-
beta-amyloid peptide(22-35)
-
not-containing arginine
Cd2+
-
53% inhibition at 1 mM Cd2+
Ethylguanidine
-
-
Formamidinium ion
-
1 mM, irreversible inhibition within 1 min
formylguanidine
-
-
gamma-guanidinobutyrate
-
-
guanidine
L-Alpha-amino-beta-guanidinopropionic acid
L-Alpha-amino-gamma-guanidinobutyric acid
-
competitive
L-alpha-aminobutyrate
-
-
L-canavanine
L-citrulline
-
-
L-glutamate
-
-
L-homoarginine
L-norvaline
-
noncompetitive
L-ornithine
Mersalyl
-
-
Methylguanidine
-
-
nitroguanidine
-
-
p-hydroxymercuribenzoate
-
-
PEG
-
modifiying ADI with PEG leads to reduced activity of the complex of 400 kDa MW
Polyethylene glycol
-
binding of 12 kDa and of 20 kDa MW inhibits the enzyme activity, but does not alter the pH-dependence of the enzyme and increases the enzyme stability during storage slightly, with PEG 12k showing the higher effect
putrescine
-
-
S-nitroso-L-homocysteine
-
active site directed, irreversible inhibitor
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
imidazole
-
0.2 M, accelerates 5fold
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
31
agmatine-L-Arg
-
-
18
benzoyl-L-arginine ethyl ester
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37C
0.033
bradykinin antagonist-L-Arg
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37C
0.021
bradykinin-L-Arg
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37C
1.9 - 10
D-Arg
11
guanidine
-
-
4.7
homoarginine
-
-
2.38
L-Alpha-amino-beta-guanidinopropionic acid
-
-
3.03
L-Alpha-amino-gamma-guanidinobutyric acid
-
-
0.004 - 38
L-Arg
0.09 - 38
L-arginine
2.1
L-arginine ethyl ester
-
in 50 mM K+-HEPES (pH 7.5), at 25C
6.9
L-Arginine hydroxamate
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37C
16
L-Argininic acid
-
-
0.044 - 2.3
L-canavanine
6
L-canavanine-L-Arg
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37C
4.7
L-homoarginine
-
-
3.38
L-nitroarginine
-
-
0.07
L-Pro-L-Arg-L-Phe
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37C
0.089
L-Pro-L-Phe-L-Arg
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37C
0.01 - 0.02
N-alpha-benzoyl-L-arginine
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37C
1.2
Nalpha-methyl-L-Arg
-
-
50
Nomega-amino-Arg
-
pH 5.6, 25C, wild-type enzyme
0.002 - 50
Nomega-amino-L-arginine
1.5
Nomega-hydroxy-L-arginine
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37C
21
Nomega-methyl-Arg
-
pH 5.6, 25C, wild-type enzyme
21
Nomega-methyl-L-arginine
-
pH 5.6, 25C, wild-type enzyme
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.007
agmatine-L-Arg
Porphyromonas gingivalis
-
-
0.019
benzoyl-L-arginine ethyl ester
Porphyromonas gingivalis
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37C
0.0068
bradykinin antagonist-L-Arg
Porphyromonas gingivalis
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37C
0.043
bradykinin-L-Arg
Porphyromonas gingivalis
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37C
0.058
D-Arg
Porphyromonas gingivalis
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37C
0.11
homoarginine
Porphyromonas gingivalis
-
-
0.00036 - 29
L-Arg
0.013 - 22.5
L-arginine
2.3
L-arginine ethyl ester
Giardia intestinalis
-
in 50 mM K+-HEPES (pH 7.5), at 25C
0.15
L-Arginine hydroxamate
Porphyromonas gingivalis
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37C
0.09 - 0.62
L-canavanine
0.0052
L-canavanine-L-Arg
Porphyromonas gingivalis
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37C
0.0075
L-Pro-L-Arg-L-Phe
Porphyromonas gingivalis
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37C
0.17
L-Pro-L-Phe-L-Arg
Porphyromonas gingivalis
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37C
0.12
N-alpha-benzoyl-L-arginine
Porphyromonas gingivalis
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37C
2.5
Nalpha-benzoyl-L-arginine
Giardia intestinalis
-
in 50 mM K+-HEPES (pH 7.5), at 25C
7
Nomega-amino-Arg
Pseudomonas aeruginosa
-
pH 5.6, 25C, wild-type enzyme
0.58 - 7
Nomega-amino-L-arginine
0.0046
Nomega-hydroxy-L-arginine
Porphyromonas gingivalis
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37C
0.01
Nomega-methyl-Arg
Pseudomonas aeruginosa
-
pH 5.6, 25C, wild-type enzyme
1
Nomega-methyl-L-arginine
Pseudomonas aeruginosa
-
pH 5.6, 25C, wild-type enzyme
additional information
additional information
Mycoplasma arthritidis
-
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00023
agmatine-L-Arg
Porphyromonas gingivalis
-
-
41376
0.00099
benzoyl-L-arginine ethyl ester
Porphyromonas gingivalis
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37C
12436
0.21
bradykinin antagonist-L-Arg
Porphyromonas gingivalis
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37C
41373
2.1
bradykinin-L-Arg
Porphyromonas gingivalis
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37C
41372
0.031
D-Arg
Porphyromonas gingivalis
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37C
1349
0.024
homoarginine
Porphyromonas gingivalis
-
-
4255
0.19
L-Arg
Porphyromonas gingivalis
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37C
178
6.73 - 16
L-arginine
123
0.022
L-Arginine hydroxamate
Porphyromonas gingivalis
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37C
12578
0.00093
L-canavanine-L-Arg
Porphyromonas gingivalis
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37C
41375
0.11
L-Pro-L-Arg-L-Phe
Porphyromonas gingivalis
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37C
41374
1.9
L-Pro-L-Phe-L-Arg
Porphyromonas gingivalis
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37C
24234
6 - 12
N-alpha-benzoyl-L-arginine
Porphyromonas gingivalis
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37C
7600
2.3
Nalpha-benzoyl-L-arginine
Giardia intestinalis
-
in 50 mM K+-HEPES (pH 7.5), at 25C
21186
0.29
Nomega-amino-L-arginine
Giardia intestinalis
-
in 50 mM K+-HEPES (pH 7.5), at 25C
11513
0.003
Nomega-hydroxy-L-arginine
Porphyromonas gingivalis
-
in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37C
2523
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.7
L-canavanine
40
S-nitroso-L-homocysteine
-
in 50 mM K+-HEPES (pH 7.5), at 25C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000345
-
crude extract, pH 9.5, at 37C
0.115
-
purifed recombinant enzyme
0.175
-
after purification, pH 9.5, at 37C
0.476
crude enzyme extract, IU/mg dry cell weight
1.5
purified enzyme, at pH 6.5 and 37C
4.76
at pH 6.0 and 37C
5.4
-
purified enzyme
25.5
-
PEG-modified enzyme
27
-
free enzyme
32.7 - 37
-
purified recombinant enzyme
35
-
purified enzyme
40
-
purifed recombinant ADI mutant
41
-
purified native enzyme
44.5
-
purified native enzyme
50
-
purified rcombinant enzyme
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 7.75
-
a series of in vitro batch fermentations using reconstituted Man-Rogosa-Sharpe (MRS) medium at different constant pH values (pH 4.50 - pH 7.75) is performed. Arginine conversion through the ADI pathway, which is activated from the stationary growth phase on, results in the production of both citrulline and ornithine for all pH conditions tested. The pattern and the ratio of the end-products of the ADI pathway are influenced by pH
4.5 - 7
5 - 6.5
-
for certain pH values (between pH 5.0 and 6.5), a further conversion of citrulline into ornithine is found when all arginine is depleted
5 - 7
-
deviations from the optimal pH (pH 5.0 and pH 7.0) results in an overall decline of the relative expression level of arginine deiminase
5 - 7.5
-
maximal activity at pH 6.0, 50% of maximal activity at pH 7.0, 10% at pH 7.5
5 - 8.6
-
pH profiles of wild-type and mutant enzymes
5 - 7.5
5.5 - 9
-
the kcat value is maximal from pH 5.5 to pH 9.0
6 - 8
-
the kcat_Km value is maximal between pH 6.0 and 8.0
6 - 11
-
38.5% activity remaining at pH 6.0 and 3.4% activity remaining at pH 11.0
6 - 7.4
-
pH 6.0: maximal activity, pH 7.4: 13% of maximal activity
6.5 - 7.5
-
a pH shift from 6.5 to 7.5 results in an approximately 80% drop in activity
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 50
-
10C: about 70% of maximal activity, 50C: about 60% of maximal activity
35 - 53
-
35C: about 55% of maximal activity, 53C: about 50% of maximal activity
additional information
-
no activity at 45C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
lymphatic
Manually annotated by BRENDA team
-
retinoblastoma cell line
Manually annotated by BRENDA team
-
retinoblastoma cell line
Manually annotated by BRENDA team
additional information
-
isolated from human U-937 cells
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Helicobacter pylori (strain ATCC 700392 / 26695)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
44000
-
2 * 44000, the subunits differ in conformation, SDS-PAGE
45900
-
calculated from amino acid sequence; electrospray mass spectrometry
45920
-
electrospray mass spectrometry
46050
-
calculated from amino acid sequence
46500
deduced ADI protein sequence
46940
-
calculated from amino acid sequence; electrospray mass spectrometry
47000
-
2 * 47000, SDS-PAGE
47200
x * 47200, SDS-PAGE
48000
-
2 * 48000, SDS-PAGE
51000
-
purified recombinant truncated PAD (missing 43 N-terminal amino acid residues but including Xpress and poly-His tags), SDS-PAGE
53000
-
active enzyme, gel filtration
54000
-
2 * 54000, SDS-PAGE
55000
-
2 * 55000, cetyl trimethylammonium bromide
60880
-
truncated PAD with its poly-His and Xpress epitope tags, calculated from amino acid sequence
60890
-
MALDI-TOF mass spectrometry
64189
-
2 * 64189, calculated from amino acid sequence
64190
-
2 * 64190, ESI-MS analysis
66000
-
2 * 66000, SDS-PAGE
80000
-
gel filtration
87000
-
gel filtration
87300
-
equilibrium sedimentation
100000
-
gel filtration
105000
120000
127000
-
gel filtration
130000
-
gel filtration
140000
199000
-
gel filtration
additional information
-
genetic structure and transcriptional analysis of the arginine deiminase (ADI) cluster
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
tetramer
trimer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
identical to the previously characterized streptococcal acid glycoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure determination and analysis of purified recombinant enzyme at 1.6 and 2.0 A resolution, respectively
-
in complex with substrate
apo-enzyme, sitting drop vapor diffusion method, using 0.9 M trisodium citrate, 0.1M sodium cacodylate pH 6.5
catalytically important residues are C406 and H278
-
crystal structure determination and analysis of purified recombinant enzyme at 2.45 A resolution, recombinant selenomethionine-labeled enzyme by sitting drop vaour diffusion method
-
mutants C406A, H287A, D280A, and D166A in complex with L-arginine, protein solutions containing 20 mM arginine are mixed with an equal volume of mother liquor containing 34-38% 2-methyl-2,4-pentanediol, 6.0-7.0% PEG 3350, 0.1 M Tris-HCl, pH 7.6, and 20 mM arginine, equilibration against the mother liquor reservoir, 2-8 weeks, X-ray diffraction structure determination and anaylsis at 2.3-2.9 A resolution, modeling
-
X-ray crystallographic coordinates for the structure of the C406A ADI -L-arginine complex, overview
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.5
-
immediate loss of activity
209452
4 - 8
about 25% relative activity at pH 4.0, about 50% relative activity at pH 5.0, about 25% relative activity at pH 7.0, less than 10% relative activity at pH 8.0
697511
6
-
rapid loss of activity
209446
7
-
4C, stable for more than 1 months
209466
7 - 9.5
-
the enzyme at 13 mg/ml remains active at pH 7.0, 8.0 and 9.5 for several days at 25C
711003
8 - 11
-
15 min, 40C, stable
209455
8
-
4C, stable for 1 week
209446
9.5
-
8 h, stable
209452
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
PAD is cold sensitive, it aggregates within 30 min at 4C, but aggregated PAD displays variable activity for up to one week after re-suspension with storage buffer
5 - 60
about 20% relative activity at 5C, about 35% relative activity at 20C, about 20% relative activity at 5C, about 98% relative activity at 53C, about 40% relative activity at 50C, about 10% relative activity at 60C
35
-
optimal stability
50
-
15 min, enzyme retains 61.2% of its activity
55
-
3 min, 50% loss of activity
60
-
loss of activity above
100
-
no product formation is observed in reaction mixtures containing the PAD sample that have been boiled
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
not stable in glycerol, poly(ethyleneglycol) and glycine buffers
-
urea-induced unfolding, quantitative stability analysis of recombinant wild-type and mutant enzymes, kinetics, overview
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, stable for at least 1 year
-
25C or -80C, in the presence of 0.5 mM 2-mercaptoethanol or 1 mM dithiothreitol and 0.1% (w/v) sodium azide in 50 mM potassium phosphate buffer (pH 7.8), 2 weeks, no appreciable loss of activity
-
4C or -20C, in the presence of 0.5 mM 2-mercaptoethanol or 1 mM dithiothreitol and 0.1% (w/v) sodium azide in 50 mM potassium phosphate buffer (pH 7.8), 2 weeks, aggregation of the protein occurs
-
4C, pH 7.0, stable for more than 1 month
-
4C, pH 8.0, stable for 1 week
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DEAE-cellulose column chromatography and butyl-Sepharose column chromatography
-
DEAE-cellulose column chromatography, butyl-Sepharose column chromatography, and ammonium sulfate precipitation
DEAE-Sepharose column chromatography, butyl-Sepharose column chromatography, and ammonium sulfate precipitation
-
DEAE-Sepharose column chromatography, butyl-Sepharose column chromatography, hydroxyapatite column chromatography, and ammonium sulfate precipitation
-
deiminase I and II
-
Hi-Trap chelating Sepharose column chromatography and Superdex 200 gel filtration
native enzyme by protamine sulfate treatment, and gel filtration
-
native enzyme, and recombinant enzyme from Escherichia coli
-
native enzyme, and recombinant enzyme from Escherichia coli strain BL21(DE3), recombinant selenomethionine-labeled enzyme
-