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 (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 (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 | 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 | 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 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 | Comment | Organism | Structure |
---|---|---|---|
Mn2+ | binuclear manganese metalloenzyme | Homo sapiens | |
Mn2+ | binuclear manganese metalloenzyme | Rattus norvegicus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Rattus norvegicus | P07824 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Homo sapiens |
- |
Rattus norvegicus |
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 | Comment | Organism |
---|---|---|
arginase | - |
Homo sapiens |
arginase | - |
Rattus norvegicus |
arginase I | - |
Homo sapiens |
arginase I | - |
Rattus norvegicus |
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 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 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 |