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Literature summary for 1.4.3.14 extracted from

  • Kondo, H.; Kitagawa, M.; Matsumoto, Y.; Saito, M.; Amano, M.; Sugiyama, S.; Tamura, T.; Kusakabe, H.; Inagaki, K.; Imada, K.
    Structural basis of strict substrate recognition of l-lysine alpha-oxidase from Trichoderma viride (2020), Protein Sci., 29, 2213-2225 .
    View publication on PubMed
Search for more literature for 1.4.3.14

Cloned(Commentary)

Cloned (Comment) Organism
the enzyme (LysOX) is expressed in Streptomyces lividans TK24 and in Escherichia coli. The D212A, D315A, and D212A/D315A mutant variants are expressed in Escherichia coli Trichoderma viride

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting-drop vapor-diffusion method at 20°C. The structure of the enzyme in complex with L-lysine at 1.7 A resolution is determined Trichoderma viride

Protein Variants

Protein Variants Comment Organism
D212A the Km-value of the mutant enzyme for L-lysine is increased 43fold respectively, to the wild-type enzyme, the kcat-value is slightly decreased. The single mutation does not much affect substrate preference Trichoderma viride
D212A/D315A the Km value of the double mutant variant increases 585fold and kcat/Km decreasea more than 2000fold to the wild-type enzyme. The D212A/D315A double mutation increases relative activity for aromatic L-amino acids (L-phenylalanine, L-tyrosine, and L-tryptophan) and L-arginine while reduced for L-lysine Trichoderma viride
D315A the Km-value of the mutant enzyme for L-lysine is increased 22fold respectively, to the wild-type enzyme, the kcat-value is slightly decreased. The single mutation does not much affect substrate preference Trichoderma viride
M67A activity is greatly reduced and is too low to determine the kinetic parameters for L-lysine Trichoderma viride

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.013
-
 L-lysine pH 7.4, 40°C, recombinant enzyme from Escherichia coli Trichoderma viride
0.013
-
 L-lysine pH 7.4, 40°C, recombinant enzyme from Streptomyces lividans Trichoderma viride
0.28
-
 L-lysine pH 7.4, 40°C, mutant enzyme D315A Trichoderma viride
0.56
-
 L-lysine pH 7.4, 40°C, mutant enzyme D212A Trichoderma viride
7.6
-
 L-lysine pH 7.4, 40°C, mutant enzyme D212A/D315A Trichoderma viride

Organism

Organism UniProt Comment Textmining
Trichoderma viride A0A0J9X1X3 i.e. Trichoderma viride
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.7
-
 substrate: L-lysine, pH 7.4, 40°C, mutant enzyme M67A Trichoderma viride
6.4
-
 substrate: L-lysine, pH 7.4, 40°C, mutant enzyme D212A/D315A Trichoderma viride
18.5
-
 substrate: L-lysine, pH 7.4, 40°C, mutant enzyme D212A Trichoderma viride
22.2
-
 substrate: L-lysine, pH 7.4, 40°C, mutant enzyme D315A Trichoderma viride
62.5
-
 substrate: L-lysine, pH 7.4, 40°C, recombinant enzyme from Streptomyces lividans Trichoderma viride
66.1
-
 substrate: L-lysine, pH 7.4, 40°C, recombinant enzyme from Escherichia coli Trichoderma viride

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-lysine + O2 + H2O the molecular mechanism of the strict specificity for L-lysine is explained Trichoderma viride 6-amino-2-oxohexanoate + NH3 + H2O2
-
 ?

Subunits

Subunits Comment Organism
homodimer
-
 Trichoderma viride

Synonyms

Synonyms Comment Organism
LysOx
-
 Trichoderma viride

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
60
-
 the enzyme retains more than 90% of the original activity after incubation at 60°C for 30 min in 0.1 M potassium phosphate buffer Trichoderma viride

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
17
-
 L-lysine pH 7.4, 40°C, mutant enzyme D212A/D315A Trichoderma viride
24.3
-
 L-lysine pH 7.4, 40°C, mutant enzyme D315A Trichoderma viride
26.4
-
 L-lysine pH 7.4, 40°C, mutant enzyme D212A Trichoderma viride
59.1
-
 L-lysine pH 7.4, 40°C, recombinant enzyme from Streptomyces lividans Trichoderma viride
62.8
-
 L-lysine pH 7.4, 40°C, recombinant enzyme from Escherichia coli Trichoderma viride

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7 10 the activity of the enzyme does not significantly change in the pH range from 7.0 to 10.0 Trichoderma viride

Cofactor

Cofactor Comment Organism Structure
FAD FAD-dependent enzyme Trichoderma viride

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.2
-
 L-lysine pH 7.4, 40°C, mutant enzyme D212A/D315A Trichoderma viride
47
-
 L-lysine pH 7.4, 40°C, mutant enzyme D212A Trichoderma viride
87
-
 L-lysine pH 7.4, 40°C, mutant enzyme D315A Trichoderma viride
4500
-
 L-lysine pH 7.4, 40°C, recombinant enzyme from Streptomyces lividans Trichoderma viride
4800
-
 L-lysine pH 7.4, 40°C, recombinant enzyme from Escherichia coli Trichoderma viride