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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

Reaction

L-arginine
+
H2O
=
L-citrulline
 +
NH3

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 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.3 In linear amidines
                3.5.3.6 arginine deiminase

Engineering

Engineering on EC 3.5.3.6 - arginine deiminase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C265S/C336S
-
the mutant is catalytically active
F269P
the conversion rate of L-arginine to L-citrulline at 45°C is 93.2% compared to wild-type enzyme
G292C
the conversion rate of L-arginine to L-citrulline at 45°C is 96.0% compared to wild-type enzyme
G292D
the conversion rate of L-arginine to L-citrulline at 45°C is 97.5% compared to wild-type enzyme
G292P
the conversion rate of L-arginine to L-citrulline at 45°C is 96.5% compared to wild-type enzyme
R15K
the conversion rate of L-arginine to L-citrulline at 45°C is 95.8% compared to wild-type enzyme
R15K/F269Y/G292P
the triple-site mutant enzyme displays a 2.5fold higher specific enzyme activity (333 U/mg), a lower Km value of 6.4 mM, and a 6.1fold longer half-life (t1/2(45°C): 86.7 min) than wild-type enzyme. The conversion rate of L-arginine to L-citrulline at 45°C is 97.4% compared to wild-type enzyme
G292C
-
the conversion rate of L-arginine to L-citrulline at 45°C is 96.0% compared to wild-type enzyme
-
G292D
-
the conversion rate of L-arginine to L-citrulline at 45°C is 97.5% compared to wild-type enzyme
-
G292P
-
the conversion rate of L-arginine to L-citrulline at 45°C is 96.5% compared to wild-type enzyme
-
R15K
-
the conversion rate of L-arginine to L-citrulline at 45°C is 95.8% compared to wild-type enzyme
-
R15K/F269Y/G292P
-
the triple-site mutant enzyme displays a 2.5fold higher specific enzyme activity (333 U/mg), a lower Km value of 6.4 mM, and a 6.1fold longer half-life (t1/2(45°C): 86.7 min) than wild-type enzyme. The conversion rate of L-arginine to L-citrulline at 45°C is 97.4% compared to wild-type enzyme
-
C424A
D123N
2.5fold decrease in kcat/Km compared to wild-type value with N-alpha-benzoyl-L-arginine ethyl ester as substrate
D125A
2.75fold decrease in kcat/Km compared to wild-type value with N-alpha-benzoyl-L-arginine ethyl ester as substrate
D166A
85fold decrease in kcat/Km compared to wild-type value with N-alpha-benzoyl-L-arginine ethyl ester as substrate
D169A
2fold decrease in kcat/Km compared to wild-type value with N-alpha-benzoyl-L-arginine ethyl ester as substrate
D177A
15fold decrease in kcat/Km compared to wild-type value with N-alpha-benzoyl-L-arginine ethyl ester as substrate
D370A
220fold decrease in kcat/Km compared to wild-type value with N-alpha-benzoyl-L-arginine ethyl ester as substrate
D374A
145fold decrease in kcat/Km compared to wild-type value with N-alpha-benzoyl-L-arginine ethyl ester as substrate
D389A
20fold decrease in kcat/Km compared to wild-type value with N-alpha-benzoyl-L-arginine ethyl ester as substrate
E352A
1250fold decrease in kcat/Km compared to wild-type value with N-alpha-benzoyl-L-arginine ethyl ester as substrate
E412A
3300fold decrease in kcat/Km compared to wild-type value with N-alpha-benzoyl-L-arginine ethyl ester as substrate
F221A/F222A
1.1fold increase in kcat/Km compared to wild-type value with N-alpha-benzoyl-L-arginine ethyl ester as substrate
Q350A
2350fold decrease in kcat/Km compared to wild-type value with N-alpha-benzoyl-L-arginine ethyl ester as substrate
R347A
fold decrease in kcat/Km compared to wild-type value with N-alpha-benzoyl-L-arginine ethyl ester as substrate
W373A
50fold decrease in kcat/Km compared to wild-type value with N-alpha-benzoyl-L-arginine ethyl ester as substrate
D160E
-
site-directed mutagenesis, the mutant shows 70% reduced activity compared to the wild-type enzyme, the mutation impairs both the substrate binding and the substrate-induced conformational changes of ADI and interfers with the stability of the enzyme
D160E/D270E
-
site-directed mutagenesis, inactive mutant, the mutation impairs both the substrate binding and the substrate-induced conformational changes of ADI and interfers with the stability of the enzyme, the mutant loses inhibitory ability on the proliferation of mouse melanoma cells
D160E/E212D
-
site-directed mutagenesis, inactive mutant, the mutation impairs both the substrate binding and the substrate-induced conformational changes of ADI and interfers with the stability of the enzyme, the mutant loses inhibitory ability on the proliferation of mouse melanoma cells
D270E
-
site-directed mutagenesis, inactive mutant, the mutation impairs both the substrate binding and the substrate-induced conformational changes of ADI and interfers with the stability of the enzyme, the mutant loses inhibitory ability on the proliferation of mouse melanoma cells
E212D
-
site-directed mutagenesis, almost inactive mutant, the mutation impairs both the substrate binding and the substrate-induced conformational changes of ADI and interfers with the stability of the enzyme, the mutant loses inhibitory ability on the proliferation of mouse melanoma cells
E212D/D270E
-
site-directed mutagenesis, inactive mutant, the mutation impairs both the substrate binding and the substrate-induced conformational changes of ADI and interfers with the stability of the enzyme, the mutant loses inhibitory ability on the proliferation of mouse melanoma cells
H268F
-
site-directed mutagenesis, inactive mutant, the mutation impairs both the substrate binding and the substrate-induced conformational changes of ADI and interfers with the stability of the enzyme, the mutant loses inhibitory ability on the proliferation of mouse melanoma cells
H268Y
-
site-directed mutagenesis, inactive mutant, the mutation impairs both the substrate binding and the substrate-induced conformational changes of ADI and interfers with the stability of the enzyme, the mutant loses inhibitory ability on the proliferation of mouse melanoma cells
C406A
C406S
D166A
D280A
E224A
E224D
H278A
H278N
H278V
N160A
R185A
R185K
site-directed mutagenesis, unstable mutant enzyme that precipitates
R185L
R243A
R243K
R243L
R401A
R401L
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
A128T/H404R/I410L
-
in contrast to wild-type mutant shows very high activity activity at pH 7.4 and pH 6.0, Km (L-Arg) 0.43 at pH 6.0, Km (L-Arg) 0.65 at pH 7.4, pH optimum: 6.5
D38H/A128T/E296K/H404R/I410L/A276W
compared with mutant enzyme D38H/A128T/E296K/H404R/I410L, the mutant enzyme D38H/A128T/E296K/H404R/I410L/A276W displays tremendous pH and thermal stability
D38H/A128T/E296K/H404R/I410L/R243L
compared with mutant enzyme D38H/A128T/E296K/H404R/I410L, the mutant enzyme D38H/A128T/E296K/H404R/I410L/R243L exhibits significantly enhanced specific activity and substrate binding affinity, as illustrated by the dramatically reduced Km value (0.16 mmol/l) and a more favorable free energy of L-arginine binding at physiological conditions
D38H/A128T/E296K/H404R/I410L/S245D
compared with mutant enzyme D38H/A128T/E296K/H404R/I410L, mutant enzyme D38H/A128T/E296K/H404R/I410L/S245D shows a significantly increased specific activity and a similar Km value at physiological conditions
H404R
-
the mutant shows higher activity (1.8fold) and improved activity ratio at pH 7.4 to 6.4 (4.7fold) compared to the wild type ADI
K30R/C37R/G129S/L148P/V291L
91fold increase in kcat as compared to wild-type enzyme. More than two times reduced S0.5 value compared to mutant K5T/D38H/D44E/A128T/E296K/H404R
K30R/C37R/L148P/V291L
105fold increase in kcat as compared to wild-type enzyme, the mutant is a highly attractive candidate to be used as therapeutic protein for the treatment of arginine-auxotrophic melanomas
K5T/D38H/D44E/A128T/E296K/H404R
58fold increase in kcat as compared to wild-type enzyme
K5T/D44E/H404R
-
at pH 7.4, the mutant has a 4times higher kcat value than the wild type ADI and retains about 50% of its activity relative to its pH optimum (pH 7.0), compared to about 10% in the case of the wild type ADI
R18L
-
mutant shows higher activity than wild-type at pH 7.4 and pH 6.0
V10F
-
mutant shows higher activity than wild-type at pH 7.4 and pH 6.0
D38H/A128T/E296K/H404R/I410L/A276W
-
compared with mutant enzyme D38H/A128T/E296K/H404R/I410L, the mutant enzyme D38H/A128T/E296K/H404R/I410L/A276W displays tremendous pH and thermal stability
-
D38H/A128T/E296K/H404R/I410L/R243L
-
compared with mutant enzyme D38H/A128T/E296K/H404R/I410L, the mutant enzyme D38H/A128T/E296K/H404R/I410L/R243L exhibits significantly enhanced specific activity and substrate binding affinity, as illustrated by the dramatically reduced Km value (0.16 mmol/l) and a more favorable free energy of L-arginine binding at physiological conditions
-
D38H/A128T/E296K/H404R/I410L/S245D
-
compared with mutant enzyme D38H/A128T/E296K/H404R/I410L, mutant enzyme D38H/A128T/E296K/H404R/I410L/S245D shows a significantly increased specific activity and a similar Km value at physiological conditions
-
additional information