3.5.3.6: arginine deiminase
This is an abbreviated version!
For detailed information about arginine deiminase, go to the full flat file.
Word Map on EC 3.5.3.6
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3.5.3.6
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ornithine
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streptococcus
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argininosuccinate
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pegylated
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levan
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king
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carbamate
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reisolated
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mycoplasma
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water-soaked
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syringae
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greenhouse
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urease
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arginase
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adi-peg20
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lopat
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dna-dna
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melibiose
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pathovars
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d-sorbitol
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midi
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gordonii
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l-citrulline
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voges-proskauer
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newark
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l-rhamnose
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symptomless
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aesculin
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d-mannitol
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rep-pcr
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ncppb
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surface-sterilized
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lecithinase
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glistening
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cichorii
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amygdalin
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arginine-dependent
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supragingival
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deimination
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phytopathology
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sanguinis
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non-spore-forming
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salicin
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malolactic
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maculicola
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monterey
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dulcitol
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caries-free
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hayward
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drug development
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adonitol
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pharmacology
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synthesis
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medicine
- 3.5.3.6
- ornithine
- streptococcus
- argininosuccinate
-
pegylated
- levan
-
king
- carbamate
-
reisolated
- mycoplasma
-
water-soaked
- syringae
-
greenhouse
- urease
- arginase
-
adi-peg20
-
lopat
-
dna-dna
- melibiose
-
pathovars
- d-sorbitol
-
midi
- gordonii
- l-citrulline
-
voges-proskauer
-
newark
- l-rhamnose
-
symptomless
- aesculin
- d-mannitol
-
rep-pcr
-
ncppb
-
surface-sterilized
- lecithinase
-
glistening
- cichorii
- amygdalin
-
arginine-dependent
-
supragingival
-
deimination
-
phytopathology
- sanguinis
-
non-spore-forming
- salicin
-
malolactic
- maculicola
-
monterey
- dulcitol
-
caries-free
-
hayward
- drug development
- adonitol
- pharmacology
- synthesis
- medicine
Reaction
Synonyms
ADI, ArcA, arcA-1, arcA-2, arginine deiminase, arginine dihydrolase, arginine-degrading enzyme, citrulline iminase, deiminase, arginine, L-arginine deiminase, LADI, lymphocyte blastogenesis inhibitory factor, More, PaADI, PAD, PAD2, peptidylarginine deiminase, PpADI, Streptococcal acid glycoprotein
ECTree
3.5.3.6 arginine deiminaseAdvanced search results
results (
results (Inhibitors
Inhibitors on EC 3.5.3.6 - arginine deiminase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
3-aminoalanine
10 mM, 3% loss of activity. 200 mM, 28% loss of activity
AlCl3
-
1 mM, dextran-conjugated enzyme and native enzyme retain 47% and 48% of their initial activities
BaCl2
-
1 mM, dextran-conjugated enzyme and native enzyme retain 61.2% and 58.8% of their initial activities
CaCl2
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1 mM, dextran-conjugated enzyme and native enzyme retain 45.9% and 51.9% of their initial activities
CuSO4
-
1 mM, dextran-conjugated enzyme and native enzyme retain 33% and 43.4% of their initial activities
D-arginine
10 mM, 4% loss of activity. 200 mM, 97% loss of activity
DTNB
-
1 mM, dextran-conjugated enzyme and native enzyme retain 46.7% and 4.9% of their initial activities
FeCl3
-
1 mM, dextran-conjugated enzyme and native enzyme retain 45% and 50% of their initial activities
H2O2
-
1 mM, dextran-conjugated enzyme and native enzyme retain 25.8% and 2.9% of their initial activities
HgCl2
-
1 mM, dextran-conjugated enzyme and native enzyme retain 40% and 13.4% of their initial activities
K2CrO4
-
1 mM, dextran-conjugated enzyme and native enzyme retain 42% and 36% of their initial activities
KCl
-
1 mM, dextran-conjugated enzyme and native enzyme retain 97% and 98% of their initial activities
MBTH
-
1 mM, dextran-conjugated enzyme and native enzyme retain 20.5% and 2.6% of their initial activities
MgCl2
-
1 mM, dextran-conjugated enzyme and native enzyme retain 49% and 14.3% of their initial activities
N-[(1S)-1-(2-tert-butyl-2H-tetrazol-5-yl)-4-[(2-fluoroethanimidoyl)amino]butyl]benzamide
preferentially inhibits protein-arginine deiminase 2 by 3fold with the highest selectivity being observed for PAD2 over PAD4. Highly selective protein-arginine deiminase 2 inhibitor relative to the other protein-arginine deiminases
N-[(1S)-1-(2-tert-butyl-2H-tetrazol-5-yl)-4-[(2-fluoroethanimidoyl)amino]butyl][1,1'-biphenyl]-4-carboxamide
preferentially inhibits protein-arginine deiminase 2 by 25fold with the highest selectivity being observed for PAD2 over PAD4. Highly selective protein-arginine deiminase 2 inhibitor relative to the other protein-arginine deiminases
Na2WO4
-
1 mM, dextran-conjugated enzyme and native enzyme retain 30% and 26.9% of their initial activities
NaCl
-
1 mM, dextran-conjugated enzyme and native enzyme retain 13% and 11% of their initial activities
NaIO3
-
1 mM, dextran-conjugated enzyme and native enzyme retain 41% and 34% of their initial activities
PEG
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modifiying ADI with PEG leads to reduced activity of the complex of 400 kDa MW
PMSF
-
1 mM, dextran-conjugated enzyme and native enzyme retain 1.1% and 1.2% of their initial activities
Polyethylene glycol
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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
S-nitroso-L-homocysteine
active site directed, irreversible inhibitor
ZnCl2
-
1 mM, dextran-conjugated enzyme and native enzyme retain 12% and 10% of their initial activities
5,5'-dithiobis(2-nitrobenzoic acid)
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the reaction of 1 sulfhydryl group with 0.3 mM 5,5'-dithiobis-(2-nitrobenzoic acid) has a half-life of about 50 min at pH 8
6-diazo-5-oxo-norleucine
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1 mM, dextran-conjugated enzyme and native enzyme retain 10.1% and 1.5% of their initial activities
hydroxylamine
-
1 mM, dextran-conjugated enzyme and native enzyme retain 24.5% and 2.3% of their initial activities
iodoacetate
-
1 mM, dextran-conjugated enzyme and native enzyme retain 23.9% and 2.6% of their initial activities
L-canavanine
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two competing pathways, slow substrate inhibition or irreversible inhibition, branch at the Cys-alkylthiouronium ion intermediate: one pathway leads to direct formation of O-ureido-L-homoserine via a reactive thiouronium intermediate. The other pathway leads to an inactive form of the enzyme, a Cys-alkylisothiourea adduct, mechanism and structure, overview
L-canavanine
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two competing pathways, slow substrate inhibition or irreversible inhibition, branch at the Cys-alkylthiouronium ion intermediate: one pathway leads to direct formation of O-ureido-L-homoserine via a reactive thiouronium intermediate. The other pathway leads to an inactive form of the enzyme, a Cys-alkylisothiourea adduct, mechanism and structure, overview
L-canavanine
-
two competing pathways, slow substrate inhibition or irreversible inhibition, branch at the Cys-alkylthiouronium ion intermediate: one pathway leads to direct formation of O-ureido-L-homoserine via a reactive thiouronium intermediate. The other pathway leads to an inactive form of the enzyme, a Cys-alkylisothiourea adduct, mechanism and structure, overview
L-canavanine
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two competing pathways, slow substrate inhibition or irreversible inhibition, branch at the Cys-alkylthiouronium ion intermediate: one pathway leads to direct formation of O-ureido-L-homoserine via a reactive thiouronium intermediate. The other pathway leads to an inactive form of the enzyme, a Cys-alkylisothiourea adduct, mechanism and structure, overview
L-canavanine
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a time-controlled, competitive, mechanism-based inhibitor, the close structural similarity between L-arginine and L-canavanine suggests that an analogous pathway is responsible for the inactivation-reactivation cycle; slow substrate inhibitor that functions by covalent modification of the active-site Cys406 residue in the form of a thiouranoim salt
L-canavanine
competitive; two competing pathways, slow substrate inhibition or irreversible inhibition, branch at the Cys-alkylthiouronium ion intermediate: one pathway leads to direct formation of O-ureido-L-homoserine via a reactive thiouronium intermediate. The other pathway leads to an inactive form of the enzyme, a Cys-alkylisothiourea adduct, mechanism and structure, overview
L-canavanine
10 mM, 45% loss of activity. 60 mM, 99% loss of activity
L-homoarginine
10 mM, 2% loss of activity. 200 mM, 25% loss of activity
L-ornithine
10 mM, 12% loss of activity. 200 mM, 24% loss of activity
putrescine
10 mM, 6% loss of activity. 200 mM, 11% loss of activity
Urea
-
1 mM, dextran-conjugated enzyme and native enzyme retain 46.5% and 36% of their initial activities
additional information
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dextran conjugation slightly protects the reactive amino and thiols groups of surface amino acids of the enzyme from amino acids suicide inhibitors
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additional information
Nomega-cyano-L-arginine does not inhibit Giardia lamblia arginine deiminase
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additional information
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Nomega-cyano-L-arginine does not inhibit Giardia lamblia arginine deiminase
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additional information
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PEG binding does not affect the enzyme activity, but does improve pharmocodynamics and pharmacokinetics
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