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Literature summary for 1.4.3.11 extracted from

  • Zhang, X.; Xu, N.; Li, J.; Ma, Z.; Wei, L.; Liu, Q.; Liu, J.
    Engineering of L-glutamate oxidase as the whole-cell biocatalyst for the improvement of alpha-ketoglutarate production (2020), Enzyme Microb. Technol., 136, 109530 .
    View publication on PubMed
Search for more literature for 1.4.3.11

Application

Application Comment Organism
biotechnology engineering of L-glutamate oxidase has great potentials to enhance the industrial production of 2-oxoglutarate. A whole-cell biocatalyst for 2-oxoglutarate production is developed by co-expression of both S280T/H533L mutant and KatE catalase. S280T/H533L mutant has high maximal velocity (Vmax: 0.2313 mM/mg/min) and the low Km-value of 2.7 mM. Randomized ribosome binding site (RBS) sequences are introduced to generate vectors with varying expression levels of S280T/H533L and KatE, and two optimized coexpression strains are obtained after screening. The 2-oxoglutarate production reaches a maximum titer of 181.9 g/l after 12 h conversation using the optimized whole-cell biocatalyst, with a molar conversion rate of substrate higher than 86.3% in the absence of exogenous catalase, while the molar conversion rate of substrate using the wild-type biocatalyst is less than 30% Streptomyces mobaraensis
synthesis engineering of L-glutamate oxidase has great potentials to enhance the industrial production of 2-oxoglutarate. A whole-cell biocatalyst for 2-oxoglutarate production is developed by co-expression of both S280T/H533L mutant and KatE catalase Streptomyces mobaraensis

Protein Variants

Protein Variants Comment Organism
F94L single point mutant with improved enzymatic activity Streptomyces mobaraensis
H533R single point mutant with improved enzymatic activity Streptomyces mobaraensis
I282M single point mutant with improved enzymatic activity Streptomyces mobaraensis
S280T single point mutant with improved enzymatic activity Streptomyces mobaraensis
S280T/H533L mutant shows 90% higher enzymatic activity than the wild-type control Streptomyces mobaraensis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7
-
 L-glutamate pH 7.4, 37°C, mutant enzyme S280T/H533L Streptomyces mobaraensis
3.1
-
 L-glutamate pH 7.4, 37°C, mutant enzyme H533L Streptomyces mobaraensis
3.2
-
 L-glutamate pH 7.4, 37°C, mutant enzyme S280T Streptomyces mobaraensis
11.7
-
 L-glutamate pH 7.4, 37°C, wild-type enzyme Streptomyces mobaraensis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-glutamate + O2 + H2O Streptomyces mobaraensis
-
 2-oxoglutarate + NH3 + H2O2
-
 ?

Organism

Organism UniProt Comment Textmining
Streptomyces mobaraensis A0A1S6XWY4
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamate + O2 + H2O
-
 Streptomyces mobaraensis 2-oxoglutarate + NH3 + H2O2
-
 ?

Synonyms

Synonyms Comment Organism
LGOX
-
 Streptomyces mobaraensis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.164
-
 L-glutamate pH 7.4, 37°C, wild-type enzyme Streptomyces mobaraensis
0.187
-
 L-glutamate pH 7.4, 37°C, mutant enzyme S280T Streptomyces mobaraensis
0.201
-
 L-glutamate pH 7.4, 37°C, mutant enzyme H533L Streptomyces mobaraensis
0.204
-
 L-glutamate pH 7.4, 37°C, mutant enzyme S280T/H533L Streptomyces mobaraensis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.014
-
 L-glutamate pH 7.4, 37°C, wild-type enzyme Streptomyces mobaraensis
0.0584
-
 L-glutamate pH 7.4, 37°C, mutant enzyme S280T Streptomyces mobaraensis
0.0648
-
 L-glutamate pH 7.4, 37°C, mutant enzyme H533L Streptomyces mobaraensis
0.0756
-
 L-glutamate pH 7.4, 37°C, mutant enzyme S280T/H533L Streptomyces mobaraensis