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Literature summary for 1.4.3.25 extracted from

  • Yano, Y.; Matsuo, S.; Ito, N.; Tamura, T.; Kusakabe, H.; Inagaki, K.; Imada, K.
    A new L-arginine oxidase engineered from L-glutamate oxidase (2021), Protein Sci., 30, 1044-1055 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.4.3.25

Application

Application Comment Organism
diagnostics the R305E mutant enzyme is suitable for the determination of L-arginine. L-Arginine can be a medical biomarker because patients with argininemia or cancer show unusual concentrations of L-arginine in the blood Streptomyces sp. X-119-6

Crystallization (Commentary)

Crystallization (Comment) Organism
structure of the L-glutamate oxidase R305E mutant enzymed is determined at 2.65 A resolution Streptomyces sp. X-119-6

Protein Variants

Protein Variants Comment Organism
R305E wild-type enzyme shows strict substrate specificity for L-glutamate. The mutant variant of L-glutamate oxidase exhibits strict specificity for L-arginine. L-Glutamate oxidase R305E mutant is a thermostable and pH stable enzyme Streptomyces sp. X-119-6

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.223
-
 L-arginine pH 8.0, 40°C, L-glutamate oxidase mutant R305E Streptomyces sp. X-119-6

Organism

Organism UniProt Comment Textmining
Streptomyces sp. X-119-6 Q8L3C7 wild-type L-glutamate oxidase enzyme shows strict substrate specificity for L-glutamate. The R305E mutant variant of L-glutamate oxidase exhibits strict specificity for L-arginine, cf. EC 1.4.3.11
-

Purification (Commentary)

Purification (Comment) Organism
L-glutamate oxidase R305E mutant enzyme Streptomyces sp. X-119-6

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-arginine + H2O + O2 wild-type L-glutamate oxidase enzyme shows strict substrate specificity for L-glutamate. The R305E mutant variant of L-glutamate oxidase exhibits strict specificity for L-arginine Streptomyces sp. X-119-6 5-guanidino-2-oxopentanoate + NH3 + H2O2
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
 L-glutamate oxidase mutant R305E Streptomyces sp. X-119-6

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
30 60 30°C: more than 90% of maximal activity, 60°C: about 75% of maximal activity, L-glutamate oxidase mutant R305E Streptomyces sp. X-119-6

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
 pH 7.4, remaining activity is 100% after 1 h incubation, L-glutamate oxidase mutant R305E Streptomyces sp. X-119-6
60
-
 pH 7.4, remaining activity is 88% after 1 h incubation, L-glutamate oxidase mutant R305E Streptomyces sp. X-119-6
70
-
 pH 7.4, remaining activity is 60% after 1 h incubation, L-glutamate oxidase mutant R305E Streptomyces sp. X-119-6
71
-
 pH 7.4, melting temperature,L-glutamate oxidase mutant R305E Streptomyces sp. X-119-6

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.42
-
 L-arginine pH 8.0, 40°C, L-glutamate oxidase mutant R305E Streptomyces sp. X-119-6

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 L-glutamate oxidase mutant R305E Streptomyces sp. X-119-6

pH Range

pH Minimum pH Maximum Comment Organism
6 10 pH 6.0: about 15% of maximal activity, pH 10: about 35% of maximal activity, L-glutamate oxidase mutant R305E Streptomyces sp. X-119-6

pH Stability

pH Stability pH Stability Maximum Comment Organism
5 11 1 h, 40°C, residual activity is over 80% in the pH range of 5.0-11.0, L-glutamate oxidase mutant R305E Streptomyces sp. X-119-6

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
15.3
-
 L-arginine pH 8.0, 40°C, L-glutamate oxidase mutant R305E Streptomyces sp. X-119-6