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Information on EC 1.4.3.14 - L-lysine oxidase
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1.4.3.14 L-lysine oxidaseIUBMB Comments
Also acts, more slowly, on L-ornithine, L-phenylalanine, L-arginine and L-histidine.
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Word Map
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
apoptosis-inducing protein, l-lysine-alpha-oxidase, l-lysine alpha-oxidase, lysox, l-lysine oxidase, l-lox/mog, lysine-oxidase, l-lysyl-alpha-oxidase, l6150, l-lysine oxidase/monooxygenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
L-lysine alpha-oxidase
L-lysine-a-oxidase
L-lysine-alpha-oxidase
L-lysyl-alpha-oxidase
-
-
-
-
LyOx
lysine-oxidase
-
-
-
-
LysOx
L-lysine alpha-oxidase
-
-
-
-
L-lysine-alpha-oxidase
Trichoderma cf. aureoviride Rifai VKM F-4268D
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-lysine + O2 + H2O = 6-amino-2-oxohexanoate + NH3 + H2O2
the substrate specificity of Trichoderma strains changes as a function of the age of the culture and its morphological condition
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L-lysine + O2 + H2O = 6-amino-2-oxohexanoate + NH3 + H2O2
the substrate specificity of Trichoderma strains changes as a function of the age of the culture and its morphological condition
-
L-lysine + O2 + H2O = 6-amino-2-oxohexanoate + NH3 + H2O2
the substrate specificity of Trichoderma strains changes as a function of the age of the culture and its morphological condition
-
L-lysine + O2 + H2O = 6-amino-2-oxohexanoate + NH3 + H2O2
the substrate specificity of Trichoderma strains changes as a function of the age of the culture and its morphological condition
-
L-lysine + O2 + H2O = 6-amino-2-oxohexanoate + NH3 + H2O2
catabolic pathway of L-lysine through the pipecolic acid pathway
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L-lysine + O2 + H2O = 6-amino-2-oxohexanoate + NH3 + H2O2
also acts, more slowly, on L-ornithine, L-phenylalanine, L-arginine and L-histidine
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
oxidative deamination
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-
-
-
redox reaction
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-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
-
,
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SYSTEMATIC NAME
IUBMB Comments
L-lysine:oxygen 2-oxidoreductase (deaminating)
Also acts, more slowly, on L-ornithine, L-phenylalanine, L-arginine and L-histidine.
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CAS REGISTRY NUMBER
COMMENTARY
70132-14-8
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,6-diaminopimelate + O2 + H2O
?
-
22% activity compared to L-lysine
-
-
?
5-hydroxy-DL-lysine + O2 + H2O
6-amino-5-hydroxy-2-oxohexanoate + NH3 + H2O2
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5% activity compared to L-lysine
-
-
?
L-tyrosine + O2 + H2O
3-(4-hydroxyphenyl)pyruvate + NH3 + H2O2
-
-
-
?
L-tyrosine + O2 + H2O
4-hydroxyphenylpyruvate + NH3 + H2O2
-
1.4% activity compared to L-lysine
-
-
?
L-arginine + O2 + H2O
5-carbamidamido-2-oxopentanoate + NH3 + H2O2
-
5.8% activity compared to L-lysine
-
-
?
L-arginine + O2 + H2O
5-carbamidamido-2-oxopentanoate + NH3 + H2O2
Trichoderma cf. aureoviride
-
8.3% activity compared to L-lysine
-
-
?
L-arginine + O2 + H2O
5-carbamidamido-2-oxopentanoate + NH3 + H2O2
Trichoderma cf. aureoviride Rifai VKM F-4268D
-
8.3% activity compared to L-lysine
-
-
?
L-arginine + O2 + H2O
5-guanidino-2-oxopentanoate + NH3 + H2O2
-
12.8% activity compared to L-lysine
-
-
?
L-arginine + O2 + H2O
5-guanidino-2-oxopentanoate + NH3 + H2O2
-
-
-
?
L-arginine + O2 + H2O
5-guanidino-2-oxopentanoate + NH3 + H2O2
-
-
-
?
L-arginine + O2 + H2O
5-guanidino-2-oxopentanoate + NH3 + H2O2
-
-
-
?
L-arginine + O2 + H2O
5-guanidino-2-oxopentanoate + NH3 + H2O2
-
-
-
?
L-arginine + O2 + H2O
5-guanidino-2-oxopentanoate + NH3 + H2O2
-
6.3% activity compared to L-lysine
-
-
?
L-arginine + O2 + H2O
5-guanidino-2-oxopentanoate + NH3 + H2O2
-
-
-
?
L-arginine + O2 + H2O
5-guanidino-2-oxopentanoate + NH3 + H2O2
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6.3% activity compared to L-lysine
-
-
?
L-histidine + O2 + H2O
3-(1H-imidazol-4-yl)-2-oxopropanoate + NH3 + H2O2
-
-
-
?
L-histidine + O2 + H2O
3-(1H-imidazol-4-yl)-2-oxopropanoate + NH3 + H2O2
-
-
-
?
L-histidine + O2 + H2O
3-(1H-imidazol-4-yl)-2-oxopropanoate + NH3 + H2O2
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only 1% in comparison with L-lysine
-
?
L-lysine + O2 + H2O
6-amino-2-oxohexanoate + NH3 + H2O2
enzymes with dual activities in a single active site: L-lysine oxidase and L-lysine monooxygenase
-
-
?
L-lysine + O2 + H2O
6-amino-2-oxohexanoate + NH3 + H2O2
the mechanistic features are reported that are important for allowing the single active site of L-LOX/MOG to catalyze the two reactions of apparent monooxygenation and the oxidation of the flavoprotein oxidase
-
-
?
L-lysine + O2 + H2O
6-amino-2-oxohexanoate + NH3 + H2O2
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100% activity
-
-
?
L-lysine + O2 + H2O
6-amino-2-oxohexanoate + NH3 + H2O2
-
-
-
-
?
L-lysine + O2 + H2O
6-amino-2-oxohexanoate + NH3 + H2O2
-
100% activity
-
-
?
L-lysine + O2 + H2O
6-amino-2-oxohexanoate + NH3 + H2O2
Trichoderma aureoviride Rifai VKM F-4268D
-
-
-
-
?
L-lysine + O2 + H2O
6-amino-2-oxohexanoate + NH3 + H2O2
Trichoderma cf. aureoviride
-
-
-
-
?
L-lysine + O2 + H2O
6-amino-2-oxohexanoate + NH3 + H2O2
Trichoderma cf. aureoviride
-
the stereospecific enzyme oxidizes almost exclusively L-lysine
-
-
?
L-lysine + O2 + H2O
6-amino-2-oxohexanoate + NH3 + H2O2
Trichoderma cf. aureoviride Rifai VKM F-4268D
-
the stereospecific enzyme oxidizes almost exclusively L-lysine
-
-
?
L-lysine + O2 + H2O
6-amino-2-oxohexanoate + NH3 + H2O2
Trichoderma cf. aureoviride Rifai VKM F-4268D
-
-
-
-
?
L-lysine + O2 + H2O
6-amino-2-oxohexanoate + NH3 + H2O2
-
-
-
?
L-lysine + O2 + H2O
6-amino-2-oxohexanoate + NH3 + H2O2
-
-
-
-
?
L-lysine + O2 + H2O
6-amino-2-oxohexanoate + NH3 + H2O2
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most favored substrate
-
?
L-lysine + O2 + H2O
6-amino-2-oxohexanoate + NH3 + H2O2
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-
-
-
?
L-lysine + O2 + H2O
6-amino-2-oxohexanoate + NH3 + H2O2
-
-
-
?
L-lysine + O2 + H2O
6-amino-2-oxohexanoate + NH3 + H2O2
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preferred substrate
-
?
L-lysine + O2 + H2O
6-amino-2-oxohexanoate + NH3 + H2O2
-
preferred substrate
-
?
L-lysine + O2 + H2O
6-amino-2-oxohexanoate + NH3 + H2O2
-
also other alpha,omega-diaminomonocarboxylates and L-lysine hydroxamate are oxidized
-
?
L-lysine + O2 + H2O
6-amino-2-oxohexanoate + NH3 + H2O2
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lysine metabolism
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?
L-lysine + O2 + H2O
6-amino-2-oxohexanoate + NH3 + H2O2
-
lysine metabolism
-
?
L-lysine + O2 + H2O
6-amino-2-oxohexanoate + NH3 + H2O2
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100% activity
-
-
?
L-lysine + O2 + H2O
6-amino-2-oxohexanoate + NH3 + H2O2
the molecular mechanism of the strict specificity for L-lysine is explained
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-
?
L-lysine + O2 + H2O
6-amino-2-oxohexanoate + NH3 + H2O2
-
preferred substrate
-
?
L-lysine + O2 + H2O
6-amino-2-oxohexanoate + NH3 + H2O2
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100% activity
-
-
?
L-ornithine + O2 + H2O
5-amino-2-oxopentanoate + NH3 + H2O2
enzymes with dual activities in a single active site: L-lysine oxidase and L-lysine monooxygenase
-
-
?
L-ornithine + O2 + H2O
5-amino-2-oxopentanoate + NH3 + H2O2
Trichoderma cf. aureoviride
-
5.8% activity compared to L-lysine
-
-
?
L-ornithine + O2 + H2O
5-amino-2-oxopentanoate + NH3 + H2O2
Trichoderma cf. aureoviride Rifai VKM F-4268D
-
5.8% activity compared to L-lysine
-
-
?
L-ornithine + O2 + H2O
5-amino-2-oxopentanoic acid + NH3 + H2O2
the mechanistic features are reported that are important for allowing the single active site of L-LOX/MOG to catalyze the two reactions of apparent monooxygenation and the oxidation of the flavoprotein oxidase
-
-
?
L-ornithine + O2 + H2O
5-amino-2-oxopentanoic acid + NH3 + H2O2
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6% activity compared to L-lysine
-
-
?
L-ornithine + O2 + H2O
5-amino-2-oxopentanoic acid + NH3 + H2O2
-
8.3% activity compared to L-lysine
-
-
?
L-ornithine + O2 + H2O
5-amino-2-oxopentanoic acid + NH3 + H2O2
-
-
-
?
L-ornithine + O2 + H2O
5-amino-2-oxopentanoic acid + NH3 + H2O2
-
-
-
?
L-ornithine + O2 + H2O
5-amino-2-oxopentanoic acid + NH3 + H2O2
-
-
-
?
L-ornithine + O2 + H2O
5-amino-2-oxopentanoic acid + NH3 + H2O2
-
-
-
?
L-ornithine + O2 + H2O
5-amino-2-oxopentanoic acid + NH3 + H2O2
-
18.3% activity compared to L-lysine
-
-
?
L-ornithine + O2 + H2O
5-amino-2-oxopentanoic acid + NH3 + H2O2
-
-
-
?
L-ornithine + O2 + H2O
5-amino-2-oxopentanoic acid + NH3 + H2O2
-
18.3% activity compared to L-lysine
-
-
?
L-phenylalanine + O2 + H2O
phenylpyruvate + NH3 + H2O2
-
-
-
?
L-phenylalanine + O2 + H2O
phenylpyruvate + NH3 + H2O2
-
16% in comparison to L-lysine
-
?
L-phenylalanine + O2 + H2O
phenylpyruvate + NH3 + H2O2
-
1.7% activity compared to L-lysine
-
-
?
L-phenylalanine + O2 + H2O
phenylpyruvate + NH3 + H2O2
-
16% in comparison to L-lysine
-
?
L-phenylalanine + O2 + H2O
phenylpyruvate + NH3 + H2O2
-
1.7% activity compared to L-lysine
-
-
?
additional information
?
-
-
the enzyme shows no activity with L-histidine, L-aspartic acid, glycine, L-phenylalanine, L-alanine, L-arginine, L-glutamic acid, L-isoleucine, L-leucine, L-serine, L-proline, L-threonine, L-glutamine, L-asparagine, L-threonine, L-tryptophan, L-tyrosine, L-valine, L-methionine, L-cysteine and D-lysine
-
-
?
additional information
?
-
-
very low activity with DL-phenylalanine, L-histidine, L-arginine, DL-methionine and L-glycine
-
-
?
additional information
?
-
-
no activity with L-cysteine, L-asparagine-NH2, DL-serine, DL-asparagine and DL-glutamic acid
-
-
?
additional information
?
-
-
no activity with N-2-trifluoroacetyl-L-lysine, 6-aminocaproic acid, 1,4-diaminobutane, L-alanine, L-leucine, L-glutamic acid, L-2,7-diamino heptanoic acid, L-glutamine, and D-lysine
-
-
?
additional information
?
-
Trichoderma cf. aureoviride
-
no activity with The L-isomers of leucine, phenylalanine, citrulline, alanine, asparagine, histidine, ornithine, glutamine, threonine, tyrosine, isoleucine, valine, as well as glycine and D-lysine
-
-
?
additional information
?
-
Trichoderma cf. aureoviride Rifai VKM F-4268D
-
no activity with The L-isomers of leucine, phenylalanine, citrulline, alanine, asparagine, histidine, ornithine, glutamine, threonine, tyrosine, isoleucine, valine, as well as glycine and D-lysine
-
-
?
additional information
?
-
-
very low activity with DL-phenylalanine and DL-methionine
-
-
?
additional information
?
-
-
no activity with L-cysteine, L-asparagine-NH2, DL-serine, DL-asparagine and DL-glutamic acid
-
-
?
additional information
?
-
-
no activity with L-cysteine, L-asparagine-NH2, DL-serine, DL-asparagine and DL-glutamic acid
-
-
?
additional information
?
-
-
very low activity with several other amino acids
-
-
?
additional information
?
-
-
several amino acids, amino acid derivatives and other substances that are assumed to be possible substrates are tested
-
-
?
additional information
?
-
-
no activity with L-cysteine, L-asparagine-NH2, DL-serine, DL-asparagine and DL-glutamic acid
-
-
?
additional information
?
-
-
commercially manufactured LyOx is generally not highly selective for L-Lys among amino acids
-
-
?
additional information
?
-
-
several amino acids, amino acid derivatives and other substances that are assumed to be possible substrates are tested
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-arginine + O2 + H2O
5-carbamidamido-2-oxopentanoate + NH3 + H2O2
Trichoderma cf. aureoviride
-
8.3% activity compared to L-lysine
-
-
?
L-arginine + O2 + H2O
5-carbamidamido-2-oxopentanoate + NH3 + H2O2
Trichoderma cf. aureoviride Rifai VKM F-4268D
-
8.3% activity compared to L-lysine
-
-
?
L-lysine + O2 + H2O
6-amino-2-oxohexanoate + NH3 + H2O2
-
-
-
-
?
L-lysine + O2 + H2O
6-amino-2-oxohexanoate + NH3 + H2O2
Trichoderma cf. aureoviride
-
-
-
-
?
L-lysine + O2 + H2O
6-amino-2-oxohexanoate + NH3 + H2O2
Trichoderma cf. aureoviride
-
the stereospecific enzyme oxidizes almost exclusively L-lysine
-
-
?
L-lysine + O2 + H2O
6-amino-2-oxohexanoate + NH3 + H2O2
Trichoderma cf. aureoviride Rifai VKM F-4268D
-
the stereospecific enzyme oxidizes almost exclusively L-lysine
-
-
?
L-lysine + O2 + H2O
6-amino-2-oxohexanoate + NH3 + H2O2
Trichoderma cf. aureoviride Rifai VKM F-4268D
-
-
-
-
?
L-lysine + O2 + H2O
6-amino-2-oxohexanoate + NH3 + H2O2
-
-
-
?
L-lysine + O2 + H2O
6-amino-2-oxohexanoate + NH3 + H2O2
-
-
-
-
?
L-lysine + O2 + H2O
6-amino-2-oxohexanoate + NH3 + H2O2
-
most favored substrate
-
?
L-lysine + O2 + H2O
6-amino-2-oxohexanoate + NH3 + H2O2
-
-
-
?
L-lysine + O2 + H2O
6-amino-2-oxohexanoate + NH3 + H2O2
-
preferred substrate
-
?
L-lysine + O2 + H2O
6-amino-2-oxohexanoate + NH3 + H2O2
-
preferred substrate
-
?
L-lysine + O2 + H2O
6-amino-2-oxohexanoate + NH3 + H2O2
-
also other alpha,omega-diaminomonocarboxylates and L-lysine hydroxamate are oxidized
-
?
L-lysine + O2 + H2O
6-amino-2-oxohexanoate + NH3 + H2O2
-
lysine metabolism
-
?
L-lysine + O2 + H2O
6-amino-2-oxohexanoate + NH3 + H2O2
-
lysine metabolism
-
?
L-lysine + O2 + H2O
6-amino-2-oxohexanoate + NH3 + H2O2
-
preferred substrate
-
?
L-ornithine + O2 + H2O
5-amino-2-oxopentanoate + NH3 + H2O2
Trichoderma cf. aureoviride
-
5.8% activity compared to L-lysine
-
-
?
L-ornithine + O2 + H2O
5-amino-2-oxopentanoate + NH3 + H2O2
Trichoderma cf. aureoviride Rifai VKM F-4268D
-
5.8% activity compared to L-lysine
-
-
?
additional information
?
-
Trichoderma cf. aureoviride
-
no activity with The L-isomers of leucine, phenylalanine, citrulline, alanine, asparagine, histidine, ornithine, glutamine, threonine, tyrosine, isoleucine, valine, as well as glycine and D-lysine
-
-
?
additional information
?
-
Trichoderma cf. aureoviride Rifai VKM F-4268D
-
no activity with The L-isomers of leucine, phenylalanine, citrulline, alanine, asparagine, histidine, ornithine, glutamine, threonine, tyrosine, isoleucine, valine, as well as glycine and D-lysine
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
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
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Anisakiasis
Purification and cloning of an apoptosis-inducing protein derived from fish infected with Anisakis simplex, a causative nematode of human anisakiasis.
Autoimmune Diseases
Synthesis and structure-activity relationship studies of 2-(1,3,4-oxadiazole-2(3H)-thione)-3-amino-5-arylthieno[2,3-b]pyridines as inhibitors of DRAK2.
Breast Neoplasms
Overexpression of Tumor Protein p53-regulated Apoptosis-inducing Protein 1 Regulates Proliferation and Apoptosis of Breast Cancer Cells through the PI3K/Akt Pathway.
Burkitt Lymphoma
[Effect of L-lysine-alpha-oxidase on the cell cycle kinetics of cultured Burkitt's lymphoma cells]
Carcinoma
[Comparative study of the effect of L-lysine-L-oxidase from Trichoderma harzianum Rifai and Trichoderma viride on nucleic acid synthesis in human tumor cells in vitro]
Carcinoma
[Cytostatic effect of L-lysine-alpha-oxidase from Trichoderma harzianum Rifai and Trichoderma viride]
Carcinoma
[Effect of L-lysine-alpha-oxidase on skin carcinoma induced by methylcholanthrene in mice]
Carcinoma, Hepatocellular
TT virus-derived apoptosis-inducing protein induces apoptosis preferentially in hepatocellular carcinoma-derived cells.
Diabetic Retinopathy
Elevation of the vitreous body concentrations of oxidative stress-responsive apoptosis-inducing protein (ORAIP) in proliferative diabetic retinopathy.
Glioma
Soluble Fas-ligand (sFasL) in human astrocytoma cyst fluid is cytotoxic to T-cells: another potential means of immune evasion.
Hearing Loss
The DFNA5 gene, responsible for hearing loss and involved in cancer, encodes a novel apoptosis-inducing protein.
Herpes Simplex
[Effect of L-lysine-a-oxidase on reproduction of herpes simplex type I virus in vitro]
Herpes Simplex
[Effect of L-lysine-alpha-oxidase gel on development of ophthalmic herpes and herpetic skin lesions in rabbit]
HIV Infections
[Effect of L-lysine-alpha-oxidase on the synthesis of cell proteins, targets of autoimmune pathology in HIV infection]
Hyperlipoproteinemia Type II
Oxidative stress-responsive apoptosis-inducing protein in patients with heterozygous familial hypercholesterolemia.
Hypertension
Haemodynamic and endocrinological changes during anti-hypertensive treatment with a new vasodilator substance (L6150) and propranolol.
Infections
[Effect of L-lysine-A-oxidase on development of herpetic genital infection in guinea pigs]
Leukemia
The use of an enzyme single fiber reactor in the study of leukemic cell proliferation: in vitro experiments and computer simulation.
Leukemia, Lymphocytic, Chronic, B-Cell
DAP Kinase-Related Apoptosis-Inducing Protein Kinase 2 (DRAK2) Is a Key Regulator and Molecular Marker in Chronic Lymphocytic Leukemia.
Neoplasms
AAV-mediated TRAIL gene expression driven by hTERT promoter suppressed human hepatocellular carcinoma growth in mice.
Neoplasms
Apoptin specifically causes apoptosis in tumor cells and after UV-treatment in untransformed cells from cancer-prone individuals: a review.
Neoplasms
Combination of apoptin with photodynamic therapy induces nasopharyngeal carcinoma cell death in vitro and in vivo.
Neoplasms
Combination therapy with PEG-IFN-alpha and 5-FU inhibits HepG2 tumour cell growth in nude mice by apoptosis of p53.
Neoplasms
Defective apoptosis due to a point mutation in the death domain of CD95 associated with autoimmune lymphoproliferative syndrome, T-cell lymphoma, and Hodgkin's disease.
Neoplasms
Engineering of double recombinant vaccinia virus with enhanced oncolytic potential for solid tumor virotherapy.
Neoplasms
Hepatitis C Virus Core Protein Subverts the Anti-Viral Activities of Human Kupffer Cells.
Neoplasms
Histone deacetylase inhibitors modulate the sensitivity of tumor necrosis factor-related apoptosis-inducing ligand-resistant bladder tumor cells.
Neoplasms
Induction of Cancer Cell Death by Hyaluronic Acid-Mediated Uptake of Cytochrome C.
Neoplasms
Overexpression of Tumor Protein p53-regulated Apoptosis-inducing Protein 1 Regulates Proliferation and Apoptosis of Breast Cancer Cells through the PI3K/Akt Pathway.
Neoplasms
Recombinant expression, molecular characterization and crystal structure of antitumor enzyme, l-Lysine ?-oxidase from Trichoderma viride.
Neoplasms
Targeted knockdown of Bcl2 in tumor cells using a synthetic TRAIL 3'-UTR microRNA.
Neoplasms
The DFNA5 gene, responsible for hearing loss and involved in cancer, encodes a novel apoptosis-inducing protein.
Neoplasms
Truncating