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Literature summary for 3.5.3.1 extracted from

  • Shishova, E.Y.; Di Costanzo, L.; Emig, F.A.; Ash, D.E.; Christianson, D.W.
    Probing the specificity determinants of amino acid recognition by arginase (2009), Biochemistry, 48, 121-131.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.5.3.1

Application

Application Comment Organism
medicine enzyme serves as a therapeutic target for the treatment of asthma, erectile dysfunction, and atherosclerosis Homo sapiens
medicine enzyme serves as a therapeutic target for the treatment of asthma, erectile dysfunction, and atherosclerosis Rattus norvegicus

Cloned(Commentary)

Cloned (Comment) Organism
mutants are overexpressed and purified from Escherichia coli BL21(DE3) cells using a pBS(KS) vector Homo sapiens
mutants are overexpressed and purified from Escherichia coli BL21(DE3) cells using a pET29b expression vector Rattus norvegicus

Crystallization (Commentary)

Crystallization (Comment) Organism
D183A and D183N mutants of human arginase I complexed with 2(S)-amino-6-boronohexanoic acid are crystallized by the sitting drop vapor diffusion method at 21°C Homo sapiens
T135A rat arginase I-BEC complex and unliganded N130A rat arginase I are crystallized by the hanging drop vapor diffusion method at 4°C Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
D183A site-directed mutagenesis. D183A substitution completely abolishes the hydrogen bond with the alpha-amino group of the inhibitor, resulting in 1400fold diminished affinity as well as a diminished occupancy of 0.5 for inhibitor binding in the crystal structure Homo sapiens
D183A site-directed mutagenesis. KM is increased 14fold, whereas the value of kcat is reduced 24fold, relative to values measured for the wild-type enzyme Rattus norvegicus
D183N site-directed mutagenesis. D183N substitution results solely from the altered electrostatics of the interaction with the alpha-amino group of the inhibitor Homo sapiens
N130A site-directed mutagenesis. The value of KM is increased 50fold, whereas the value of kcat is reduced only 37%, relative to values measured for the wild-type enzyme Rattus norvegicus
N130F site-directed mutagenesis Rattus norvegicus
N130Y site-directed mutagenesis Rattus norvegicus
T135A site-directed mutagenesis, substitution of T135 with Ala destroys hydrogen-bonding potential Rattus norvegicus
T135S site-directed mutagenesis, substitution of T135 with serine conserves hydrogen-bonding potential Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
2(S)-amino-6-boronohexanoic acid
-
 Homo sapiens
2(S)-amino-6-boronohexanoic acid
-
 Rattus norvegicus
S-(2-boronoethyl)-L-cysteine
-
 Homo sapiens
S-(2-boronoethyl)-L-cysteine
-
 Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1
-
 L-arginine wild type Rattus norvegicus
1.5
-
 L-arginine wild type Homo sapiens
2.5
-
 L-arginine T135S mutant, KM increases 2.5fold relatively to values measured for the wild-type enzyme Rattus norvegicus
13
-
 L-arginine T135A mutant, KM is increased 13fold relatively to values measured for the wild-type enzyme Rattus norvegicus
13.9
-
 L-arginine D183A mutant Rattus norvegicus
19.3
-
 L-arginine N130F mutant Rattus norvegicus
21.4
-
 L-arginine N130Y mutant Rattus norvegicus
40
-
 L-arginine D183N mutant Homo sapiens
50
-
 L-arginine N130A mutant Rattus norvegicus
136
-
 L-arginine D183A mutant Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ binuclear manganese metalloenzyme Homo sapiens
Mn2+ binuclear manganese metalloenzyme Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Rattus norvegicus P07824
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Homo sapiens
-
 Rattus norvegicus

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
arginase
-
 Homo sapiens
arginase
-
 Rattus norvegicus
arginase I
-
 Homo sapiens
arginase I
-
 Rattus norvegicus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
additional information
-
 enzyme activity assay at room temperature Homo sapiens
additional information
-
 enzyme activity assay at room temperature Rattus norvegicus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.8
-
 L-arginine N130F mutant Rattus norvegicus
14.7
-
 L-arginine D183A mutant Rattus norvegicus
17
-
 L-arginine N130Y mutant Rattus norvegicus
68
-
 L-arginine D183A mutant Homo sapiens
167
-
 L-arginine D183N mutant Homo sapiens
190
-
 L-arginine wild type Homo sapiens
220
-
 L-arginine N130A mutant Rattus norvegicus
260
-
 L-arginine T135A mutant, is reduced 26% relative to values measured for the wild-type enzyme Rattus norvegicus
350
-
 L-arginine wild type Rattus norvegicus
350
-
 L-arginine T135S mutant, kcat is unchanged relatively to values measured for the wild-type enzyme Rattus norvegicus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.000125
-
 S-(2-boronoethyl)-L-cysteine T135S mutant Rattus norvegicus
0.0004
-
 S-(2-boronoethyl)-L-cysteine wild type Rattus norvegicus
0.0045
-
 S-(2-boronoethyl)-L-cysteine T135A mutant Rattus norvegicus
0.013
-
 S-(2-boronoethyl)-L-cysteine N130A mutant Rattus norvegicus