Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.5.3.1 extracted from

  • Stone, E.M.; Chantranupong, L.; Georgiou, G.
    The second-shell metal ligands of human arginase affect coordination of the nucleophile and substrate (2010), Biochemistry, 49, 10582-10588.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.5.3.1

Application

Application Comment Organism
analysis development of a high-throughput semiquantitative assay system using a colorimetric 96-well plate assay to monitor the formation of urea. The assay has a dynamic range of about 5-300 microM for the ureido product Homo sapiens

Protein Variants

Protein Variants Comment Organism
D181E with Co2+, rate similar to wild-type Homo sapiens
D181E/S230A with Co2+, rate similar to wild-type Homo sapiens
D181N with Co2+, rate similar to wild-type Homo sapiens
D181N/S230G with Co2+, rate similar to wild-type Homo sapiens
D181S with Co2+, rate similar to wild-type Homo sapiens
D181S/S230G with Co2+, rate similar to wild-type Homo sapiens
additional information pairwise saturation mutagenesis of the first- and second-shell metal ligands in human arginase I. Certain second-shell mutations can modulate the binding of both the nucleophilic water/hydroxide molecule and substrate or product ligands, resulting in activity greater than that of the wild-type enzyme. The strict conservation of the second-shell metal binding residues in eukaryotic arginases does not reflect kinetic optimization of the enzyme during the course of evolution Homo sapiens
S230C with Co2+, about 2fold increase in rate, compared to wild-type Homo sapiens
S230D with Co2+, rate similar to wild-type Homo sapiens
S230G with Co2+, 2fold increase in rate, compared to wild-type Homo sapiens
S230T with Co2+, about 1.5fold increase in rate, compared to wild-type Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
L-ornithine
-
 Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.08
-
 L-arginine mutant S230G, activated by Co2+, pH 7.4, 37°C Homo sapiens
0.15
-
 L-arginine mutant D181E/S230A, activated by Co2+, pH 7.4, 37°C Homo sapiens
0.15
-
 L-arginine mutant S230C, activated by Co2+, pH 7.4, 37°C Homo sapiens
0.15
-
 L-arginine mutant S230D, activated by Co2+, pH 7.4, 37°C Homo sapiens
0.16
-
 L-arginine mutant S230T, activated by Co2+, pH 7.4, 37°C Homo sapiens
0.19
-
 L-arginine mutant D181S/S230G, activated by Co2+, pH 7.4, 37°C Homo sapiens
0.21
-
 L-arginine mutant D181N/S230G, activated by Co2+, pH 7.4, 37°C Homo sapiens
0.27
-
 L-arginine mutant D181E, activated by Co2+, pH 7.4, 37°C Homo sapiens
0.28
-
 L-arginine mutant D181S, activated by Co2+, pH 7.4, 37°C Homo sapiens
0.3
-
 L-arginine mutant D181N, activated by Co2+, pH 7.4, 37°C Homo sapiens
0.8
-
 L-arginine mutant S230G, activated by Mn2+, pH 7.4, 37°C Homo sapiens
2.1
-
 L-arginine mutant S230C, activated by Mn2+, pH 7.4, 37°C Homo sapiens
2.8
-
 L-arginine mutant D181N/S230G, activated by Mn2+, pH 7.4, 37°C Homo sapiens
3
-
 L-arginine mutant D181N, activated by Mn2+, pH 7.4, 37°C Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
additional information pairwise saturation mutagenesis of the first- and second-shell metal ligands in human arginase I shows that several metal binding ligands are actually quite tolerant to amino acid substitutions. The strict conservation of the second-shell metal binding residues in eukaryotic arginases does not reflect kinetic optimization of the enzyme during the course of evolution Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P05089
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-arginine + H2O
-
 Homo sapiens L-ornithine + urea
-
 ?

Synonyms

Synonyms Comment Organism
ARG1
-
 Homo sapiens
arginase I
-
 Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
140
-
 L-arginine mutant S230D, activated by Co2+, pH 7.4, 37°C Homo sapiens
180
-
 L-arginine mutant D181S/S230G, activated by Co2+, pH 7.4, 37°C Homo sapiens
200
-
 L-arginine mutant S230G, activated by Co2+, pH 7.4, 37°C Homo sapiens
220
-
 L-arginine mutant D181E/S230A, activated by Co2+, pH 7.4, 37°C Homo sapiens
247
-
 L-arginine mutant D181N/S230G, activated by Co2+, pH 7.4, 37°C Homo sapiens
266
-
 L-arginine mutant S230G, activated by Mn2+, pH 7.4, 37°C Homo sapiens
285
-
 L-arginine mutant S230C, activated by Mn2+, pH 7.4, 37°C Homo sapiens
315
-
 L-arginine mutant S230T, activated by Co2+, pH 7.4, 37°C Homo sapiens
327
-
 L-arginine mutant S230C, activated by Co2+, pH 7.4, 37°C Homo sapiens
344
-
 L-arginine mutant D181E, activated by Co2+, pH 7.4, 37°C Homo sapiens
360
-
 L-arginine mutant D181N, activated by Mn2+, pH 7.4, 37°C Homo sapiens
387
-
 L-arginine mutant D181N, activated by Co2+, pH 7.4, 37°C Homo sapiens
388
-
 L-arginine mutant D181S, activated by Co2+, pH 7.4, 37°C Homo sapiens
517
-
 L-arginine mutant D181N/S230G, activated by Mn2+, pH 7.4, 37°C Homo sapiens

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.05
-
 L-ornithine product inhibition constant, Co2+-activated mutant S230G, pH 7.4, 37°C Homo sapiens
0.09
-
 L-ornithine product inhibition constant, Co2+-activated mutant D181N/S230G, pH 7.4, 37°C Homo sapiens
0.11
-
 L-ornithine product inhibition constant, Co2+-activated mutant D181N, pH 7.4, 37°C Homo sapiens
0.7
-
 L-ornithine product inhibition constant, Mn2+-activated mutant S230G, pH 7.4, 37°C Homo sapiens
1
-
 L-ornithine product inhibition constant, Mn2+-activated mutant D181N/S230G, pH 7.4, 37°C Homo sapiens
2.4
-
 L-ornithine product inhibition constant, Mn2+-activated mutant D181N, pH 7.4, 37°C Homo sapiens

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
120
-
 L-arginine mutant D181N, activated by Mn2+, pH 7.4, 37°C Homo sapiens
136
-
 L-arginine mutant S230C, activated by Mn2+, pH 7.4, 37°C Homo sapiens
185
-
 L-arginine mutant D181N/S230G, activated by Mn2+, pH 7.4, 37°C Homo sapiens
330
-
 L-arginine mutant S230G, activated by Mn2+, pH 7.4, 37°C Homo sapiens
930
-
 L-arginine mutant S230D, activated by Co2+, pH 7.4, 37°C Homo sapiens
950
-
 L-arginine mutant D181S/S230G, activated by Co2+, pH 7.4, 37°C Homo sapiens
1180
-
 L-arginine mutant D181N/S230G, activated by Co2+, pH 7.4, 37°C Homo sapiens
1270
-
 L-arginine mutant D181E, activated by Co2+, pH 7.4, 37°C Homo sapiens
1290
-
 L-arginine mutant D181N, activated by Co2+, pH 7.4, 37°C Homo sapiens
1390
-
 L-arginine mutant D181S, activated by Co2+, pH 7.4, 37°C Homo sapiens
1470
-
 L-arginine mutant D181E/S230A, activated by Co2+, pH 7.4, 37°C Homo sapiens
1970
-
 L-arginine mutant S230T, activated by Co2+, pH 7.4, 37°C Homo sapiens
2180
-
 L-arginine mutant S230C, activated by Co2+, pH 7.4, 37°C Homo sapiens
2600
-
 L-arginine mutant S230G, activated by Co2+, pH 7.4, 37°C Homo sapiens