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Literature summary for 1.4.3.14 extracted from

  • Kitagawa, M.; Ito, N.; Matsumoto, Y.; Saito, M.; Tamura, T.; Kusakabe, H.; Inagaki, K.; Imada, K.
    Structural basis of enzyme activity regulation by the propeptide of l-lysine alpha-oxidase precursor from Trichoderma viride (2021), J. Struct. Biol., 5, 100044 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.4.3.14

Cloned(Commentary)

Cloned (Comment) Organism
the L-lysine oxidase precursor prLysOX is overexpressed in Escherichia coli SoluBL21 Trichoderma viride

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting-drop vapor-diffusion method, structure determination of L-lysine oxidase precursor prLysOX and its complex with L-lysine. The crystals belong to the space group C2221 with unit cell dimensions of a: 95.2, b: 130.9, and c: 94.1 A. The prLysOX-Lys crystals are prepared by the soaking method Trichoderma viride

Inhibitors

Inhibitors Comment Organism Structure
additional information the L-lysine oxidase (LysOX) precursor (prLysOX) has a long N-terminal propeptide composed of 77 residues. The propeptide of prLysOX indirectly changes the active site structure to inhibit the enzyme activity. prLysOX can adopt two conformations. One is the inhibitory form, and the other is very similar to mature LysOX. The propeptide region of the latter form is disordered, and L-lysine is bound to the latter form. prLysOX can be activated quickly in response to the environmental change without proteolytic processing. The propeptide region of prLysOX does not cover the entrance nor the tunnel to the active site. In addition, the propeptide region does not directly interact with the residues involved in substrate binding or reaction. The propeptide region of prLysOX forms a positively-charged amphiphilic helix, which is inserted between the helical domain and the FAD-binding domain, and changes the structure of the helical domain. The structural change moves the active site residues, D289, F293, A552, and W553, which are important for reaction and the substrate binding. Moreover, the structural change shits T276 resulting in the removal of the water mediating the interaction between L-lysine and D392. As a result, the propeptide region of prLysOX indirectly changes the active site structure to inhibit the enzyme activity Trichoderma viride

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.013
-
 L-lysine pH 7.4, 50°C, mature L-lysine oxidase Trichoderma viride
0.28
-
 L-lysine pH 4.0, 50°C, L-lysine oxidase precursor prLysOX Trichoderma viride

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-lysine + O2 + H2O Trichoderma viride
-
 6-amino-2-oxohexanoate + NH3 + H2O2
-
 ?

Organism

Organism UniProt Comment Textmining
Trichoderma viride A0A0G4DCU0 i.e. Trichoderma viride
-

Purification (Commentary)

Purification (Comment) Organism
L-lysine oxidase precursor prLysOX Trichoderma viride

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-lysine + O2 + H2O
-
 Trichoderma viride 6-amino-2-oxohexanoate + NH3 + H2O2
-
 ?

Synonyms

Synonyms Comment Organism
LysOx
-
 Trichoderma viride

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.1
-
 L-lysine pH 4.0, 50°C, L-lysine oxidase precursor prLysOX Trichoderma viride
65.5
-
 L-lysine pH 7.4, 50°C, mature L-lysine oxidase Trichoderma viride

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
22
-
 L-lysine pH 4.0, 50°C, L-lysine oxidase precursor prLysOX Trichoderma viride
5000
-
 L-lysine pH 7.4, 50°C, mature L-lysine oxidase Trichoderma viride