1.4.3.14: L-lysine oxidase
This is an abbreviated version!
For detailed information about L-lysine oxidase, go to the full flat file.
Reaction
Synonyms
AIP, apoptosis-inducing protein, L-LOX/MOG, L-lysine alpha-oxidase, L-lysine oxidase/monooxygenase, L-lysine-a-oxidase, L-lysine-alpha-oxidase, L-lysyl-alpha-oxidase, L6150, LyOx, lysine-oxidase, LysOx
ECTree
Advanced search results
Inhibitors
Inhibitors on EC 1.4.3.14 - L-lysine oxidase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
-
EDTA, iodoacetamide and iodoacetate show no substantial effects on the enzyme activity
-
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
-
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
-