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Ligand Nomega-amino-L-arginine Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Basic Ligand Information Molecular Structure
C6 H1 5 N5 O2
Nomega-amino-L-arginine
NCHSYZVVWKVWFQ-BYPYZUCNSA-N
NG-Amino-L-arginine, Nomega-amino-Arg
Roles as Enzyme Ligand
Substrate in Enzyme-catalyzed Reactions (4 results)
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NG-amino-L-arginine + H2O = ?
-
Nomega-amino-Arg + H2O = L-citrulline + hydrazine
-
Nomega-amino-L-arginine + H2O = hydrazine + L-citrulline
-
Nomega-amino-L-arginine + H2O = L-citrulline + hydrazine
-
Inhibitor in Enzyme-catalyzed Reactions (1 result)
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Enzyme Kinetic Parameters
kcat Value (Turnover Number) (4 results)
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0.58
-
in 50 mM K+-HEPES (pH 7.5), at 25°C
7
-
pH 5.6, 25°C, wild-type enzyme
7
-
pH 5.6, 25°C, wild-type enzyme
KM Value (4 results)
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0.002
-
in 50 mM K+-HEPES (pH 7.5), at 25°C
50
-
pH 5.6, 25°C, wild-type enzyme
50
-
pH 5.6, 25°C, wild-type enzyme
References & Links Literature References (4)
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Classical and slow-binding inhibitors of human type II arginase
2001
Colleluori, D.M.; Ash, D.E.
Biochemistry
40
9356-9362
Kinetic analysis of Pseudomonas aeruginosa arginine deiminase mutants and alternate substrates provides insight into structural determinants of function
2006
Lu, X.; Li, L.; Wu, R.; Feng, X.; Li, Z.; Yang, H.; Wang, C.; Guo, H.; Galkin, A.; Herzberg, O.; Mariano, P.S.; Martin, B.M.; Dunaway-Mariano, D.
Biochemistry
45
1162-1172
Characterization of a transient covalent adduct formed during dimethylarginine dimethylaminohydrolase catalysis
2005
Stone, E.M.; Person, M.D.; Costello, N.J.; Fast, W.
Biochemistry
44
7069 - 7078
Mechanisms of catalysis and inhibition operative in the arginine deiminase from the human pathogen Giardia lamblia
2009
Li, Z.; Kulakova, L.; Li, L.; Galkin, A.; Zhao, Z.; Nash, T.E.; Mariano, P.S.; Herzberg, O.; Dunaway-Mariano, D.
Bioorg. Chem.
37
149-161
Links to other databases for Nomega-amino-L-arginine
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