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
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results (General Stability
General Stability on EC 3.5.3.6 - arginine deiminase
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GENERAL STABILITY 
ORGANISM
UNIPROT
LITERATURE
dextran-enzyme conjugates exhibit a higher thermal stability by about 2folds for all the tested temperatures, ensuring the acquired structural and catalytic stability upon dextran conjugation
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the resistance of the enzyme conjugated with dextran to proteolysis is increased by 2.5folds to proteinase K and trypsin
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upon proteolysis for 30 min, the residual activity of the soluble enzyme, the PEGylated enzyme, and the enzyme covalently immobilized on dextran is 8.0%, 32.0%, and 20.0% for proteinase K and 10.0%, 52.0%, and 90.0% for acid protease, respectively
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urea-induced unfolding, quantitative stability analysis of recombinant wild-type and mutant enzymes, kinetics, overview
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