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(S)-lactate + O2
acetate + CO2 + H2O
(S)-lactate + O2
pyruvate + H2O2
2-hydroxy-3-methylvalerate + O2
?
-
A95G-mutant
-
-
?
2-hydroxybutanoate + bromopyruvate + ?
bromolactate + pyruvate + ?
-
transhydrogenation reaction
-
?
2-hydroxybutyrate + O2
?
-
wild-type and A95G-mutant
-
-
?
2-hydroxycaproate + O2
2-oxocaproate + H2O2
-
-
-
?
2-hydroxycaprylate + O2
2-oxocaprylate + H2O2
-
-
-
?
2-hydroxydodecanoate + O2
2-oxododecanoate + H2O2
-
-
-
?
2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
-
-
?
2-hydroxyisovalerate + O2
?
-
A95G-mutant
-
-
?
2-hydroxyoctanoate + 2,6-dichlorophenolindophenol
2-oxo-octanoate + reduced 2,6-dichlorophenolindophenol
-
-
-
r
2-hydroxyoctanoate + O2
2-oxooctanoate + H2O2
-
substrates for isoenzymes HAOX1, HAOX2, preferred substrate for isoenzyme HAOX3
-
?
2-hydroxypalmitate + O2
2-oxopalmitate + H2O2
2-hydroxyvalerate + O2
?
-
wild-type and A95G-mutant
-
-
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
D-2 -hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
D-lactate + O2
pyruvate + H2O2
DL-2-hydroxy-3-butynoate + O2
2-oxo-3-butynoate + H2O2
-
good substrate, but inactivation after 25 turnovers
-
?
DL-2-hydroxy-3-heptynoate + O2
2-oxo-3-heptynoate + H2O2
-
86% of the activity compared to DL-2-hydroxybutyrate
-
?
DL-2-hydroxy-3-hexynoate + O2
2-oxo-3-hexynoate + H2O2
-
65% of the activity compared to DL-2-hydroxybutyrate
-
?
DL-2-hydroxy-3-octynoate + O2
2-oxo-3-octynoate + H2O2
-
70% of the activity compared to DL-2-hydroxybutyrate
-
?
DL-2-hydroxy-3-pentynoate + O2
2-oxo-3-pentynoate + H2O2
-
2fold higher activity compared to DL-2-hydroxybutyrate
-
?
DL-2-hydroxy-4-methylmercaptobutyrate + 2,6-dichlorophenolindophenol
2-oxo-4-methylmercaptobutyrate + reduced 2,6-dichlorophenolindophenol
-
good substrate for long chain oxidase, low activity for short chain oxidase
-
?
DL-2-hydroxy-4-methylthiobutanoic acid + 2,6-dichlorophenolindophenol
2-oxo-4-methylthiobutanoic acid + reduced 2,6-dichlorophenolindophenol
-
-
-
?
DL-2-hydroxybutyrate + 2,4-dinitrophenylhydrazine
2-oxobutyrate 2,4-dinitrophenylhydrazone
-
low activity
-
?
DL-2-hydroxybutyrate + 2,6-dichlorophenolindophenol
2-oxobutyrate + reduced 2,6-dichlorophenolindophenol
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
DL-2-hydroxycaproate + 2,6-dichlorophenolindophenol
2-oxocaproate + reduced 2,6-dichlorophenolindophenol
-
low activity for short chain oxidase, moderate activity for long chain oxidase
-
?
DL-2-hydroxycaproate + O2
2-oxocaproate + H2O2
DL-2-hydroxydecanoate + 2,6-dichlorophenolindophenol
2-oxodecanoate + reduced 2,6-dichlorophenolindophenol
-
good substrate for long chain oxidase, traces of activity for short chain oxidase
-
?
DL-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
DL-2-hydroxyisovalerate + 2,4-dinitrophenylhydrazine
2-oxoisovalerate 2,4-dinitrophenylhydrazone
-
very low activity
-
?
DL-2-hydroxyisovalerate + 2,6-dichlorophenolindophenol
2-oxoisovalerate + reduced 2,6-dichlorophenolindophenol
-
no activity for short chain oxidase, moderate activity for long chain oxidase
-
?
DL-2-hydroxyisovalerate + O2
2-oxoisovalerate + H2O2
DL-2-hydroxyoctanoate + 2,6-dichlorophenolindophenol
2-oxooctanoate + reduced 2,6-dichlorophenolindophenol
-
good substrate for long chain oxidase, no activity for short chain oxidase
-
?
DL-2-hydroxyvalerate + 2,6-dichlorophenolindophenol
2-oxovalerate + reduced 2,6-dichlorophenolindophenol
-
low activity for short chain oxidase, moderate activity for long chain oxidase
-
?
DL-2-hydroxyvalerate + O2
2-oxovalerate + H2O2
DL-3-chlorolactate + O2
3-chloropyruvate + H2O2
DL-3-indolelactate + 2,6-dichlorophenolindophenol
3-indolepyruvate + reduced 2,6-dichlorophenolindophenol
-
good substrate for long chain oxidase, no activity for short chain oxidase
-
?
DL-3-indolelactate + O2
3-indolepyruvate + H2O2
-
-
-
?
DL-3-methoxy-4-hydroxymandelate + 2,6-dichlorophenolindophenol
(3-methoxy-4-hydroxyphenyl)pyruvate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
DL-beta-phenyllactate + 2,6-dichlorophenolindophenol
phenylpyruvate + reduced 2,6-dichlorophenolindophenol
-
no activity for short chain oxidase
-
?
DL-glycerate + O2
? + H2O2
-
-
-
?
DL-lactate + O2
pyruvate + H2O2
-
-
-
?
DL-mandelate + 2,6-dichlorophenolindophenol
oxo(phenyl)acetic acid + reduced 2,6-dichlorophenolindophenol
-
low activity
-
?
DL-mandelate + O2
phenylglyoxylic acid + H2O2
-
the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
-
-
?
DL-methionine + O2
? + H2O2
-
-
-
?
DL-p-hydroxy-beta-phenyllactate + 2,6-dichlorophenolindophenol
(4-hydroxyphenyl)pyruvate + reduced 2,6-dichlorophenolindophenol
-
no activity for short chain oxidase
-
?
DL-p-hydroxymandelate + O2
?
-
the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
-
-
?
DL-phenyllactate + O2
phenylpyruvate + H2O2
DL-vinylglycolate + O2
2-oxo-3-butenoic acid + H2O2
-
90% of the activity compared to DL-2-hydroxybutyrate
-
?
glycerate + O2
? + H2O2
-
-
-
-
?
glycolate + 2,4-dinitrophenylhydrazine
glyoxylate 2,4-dinitrophenylhydrazone
-
best substrate tested
-
?
glycolate + 2,6-dichlorophenolindophenol
glyoxylate + reduced 2,6-dichlorophenolindophenol
glycolate + acceptor
glyoxylate + reduced acceptor
B7FUG8
-
-
-
?
glycolate + ferricyanide
glyoxylate + ferrocyanide
glycolate + O2
glyoxylate + H2O2
glycolate + phenazine methosulfate
glyoxylate + reduced phenazine methosulfate
B7FUG8
-
-
-
?
glyoxalate + O2
oxalate + H2O2
-
-
-
-
?
glyoxylate + 2,4-dinitrophenylhydrazine
oxalate 2,4-dinitrophenylhydrazone
-
25% of the activity compared to glycolate
-
?
glyoxylate + 2,6-dichlorophenolindophenol
?
-
-
-
-
?
glyoxylate + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
glyoxylate + ferricyanide
? + ferrocyanide
-
-
-
?
glyoxylate thiohemiacetals + O2
? + H2O2
-
possible natural substrates, i.e. glyoxylate thiohemiacetals of coemzyme A, D-phosphopantetheine, D-pantetheine, N-acetylcysteamine, 2-mercaptoethanol, DL-dihydrolipoate, propane-1,3-dithiol
-
?
homoserine + O2
? + H2O2
-
traces of activity
-
?
isoleucic acid + O2
? + H2O2
-
-
-
?
L-2-hydroxy octanoate + O2
2-oxo-octanoate + H2O2
-
-
-
?
L-2-hydroxy palmitate + O2
2-oxo-palmitate + H2O2
-
-
-
?
L-2-hydroxy-4-methylthiobutanoic acid + O2
3-(methylthio)propanoate + HCO3-
-
oxidative decarboxylation
-
?
L-2-hydroxy-beta-methylvalerate + 2,6-dichlorophenolindophenol
3-methyl-2-oxopentanoate + reduced 2,6-dichlorophenolindophenol
L-2-hydroxyisocaproate + 2,4-dinitrophenylhydrazine
2-oxoisocaproate 2,4-dinitrophenylhydrazone
-
-
-
?
L-2-hydroxyisocaproate + 2,6-dichlorophenolindophenol
2-oxoisocaproate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
L-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
L-2-hydroxyphenyllactate + O2
? + H2O2
L-4-chloromandelate + O2
?
-
the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
-
-
?
L-4-fluoromandelate + O2
?
-
the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
-
-
?
L-4-methoxymandelate + O2
?
-
the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
-
-
?
L-4-methylmandelate + O2
?
-
the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
-
-
?
L-4-nitromandelate + O2
?
-
the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
-
-
?
L-4-trifluoromethylmandelate + O2
?
-
the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
-
-
?
L-alanine + O2
? + H2O2
-
low activity
-
?
L-isoleucine + O2
? + H2O2
-
low activity
-
?
L-lactate + 2,4-dinitrophenylhydrazine
pyruvate 2,4-dinitrophenylhydrazone
-
very low activity
-
?
L-lactate + 2,6-dichlorophenolindophenol
pyruvate + reduced 2,6-dichlorophenolindophenol
L-lactate + O2
pyruvate + H2O2
L-lactate + phenazine methosulfate
? + reduced phenazine methosulfate
B7FUG8
-
-
-
?
L-leucine + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
?
L-lysine + O2
? + H2O2
-
-
-
?
L-mandelate + 2,6-dichlorophenolindophenol
?
-
-
-
-
?
L-mandelate + 2,6-dichlorophenolindophenol
oxo(phenyl)acetic acid + reduced 2,6-dichlorophenolindophenol
L-mandelate + O2
? + H2O2
-
-
-
?
L-methionine + O2
? + H2O2
L-phenylalanine + O2
? + H2O2
-
-
-
?
L-phenyllactate + 2,6-dichlorophenolindophenol
phenylpyruvate + reduced 2,6-dichlorophenolindophenol
L-tryptophan + O2
? + H2O2
L-tyrosine + O2
? + H2O2
-
-
-
?
L-valine + O2
? + H2O2
-
low activity
-
?
lactate + O2
pyruvate + H2O2
mandelate + O2
phenylpyruvate + H2O2
oxidation of an L-2-hydroxy acid to a 2-oxoacid, model for the binding of L-mandelate into the active site, overview
-
-
?
thiol-glyoxylate adducts + O2
an oxalyl thioester + H2O2
-
may be the physiological substrates
-
?
valic acid + O2
? + H2O2
-
-
-
?
additional information
?
-
(S)-lactate + O2

acetate + CO2 + H2O
-
-
-
-
?
(S)-lactate + O2
acetate + CO2 + H2O
-
-
-
-
?
(S)-lactate + O2
acetate + CO2 + H2O
-
-
-
-
?
(S)-lactate + O2
acetate + CO2 + H2O
-
glucose-repressible lactate oxidase is likely responsible for H2O2 production
-
-
?
(S)-lactate + O2

pyruvate + H2O2
-
no decarboxylation
-
?
(S)-lactate + O2
pyruvate + H2O2
-
no decarboxylation
-
?
(S)-lactate + O2
pyruvate + H2O2
-
-
-
?
(S)-lactate + O2
pyruvate + H2O2
-
-
-
-
?
(S)-lactate + O2
pyruvate + H2O2
-
-
-
-
?
2-hydroxypalmitate + O2

2-oxopalmitate + H2O2
-
-
-
?
2-hydroxypalmitate + O2
2-oxopalmitate + H2O2
-
substrates for isoenzymes HAOX1, HAOX2
-
?
an (S)-2-hydroxy carboxylate + O2

a 2-oxo carboxylate + H2O2
-
-
-
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
-
-
-
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
-
-
-
-
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
-
-
-
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
-
-
-
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
-
-
-
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
-
-
-
-
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
-
-
-
?
D-2 -hydroxyisocaproate + O2

2-oxoisocaproate + H2O2
-
48% of the activity compared to glycolate
-
?
D-2 -hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
liver enzyme is much less active with C4 or C5 alpha-hydroxy acids but as active as with glycolate
-
?
D-lactate + O2

pyruvate + H2O2
-
traces of activity
-
?
D-lactate + O2
pyruvate + H2O2
-
traces of activity
-
?
D-lactate + O2
pyruvate + H2O2
-
traces of activity
-
?
DL-2-hydroxybutyrate + 2,6-dichlorophenolindophenol

2-oxobutyrate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
DL-2-hydroxybutyrate + 2,6-dichlorophenolindophenol
2-oxobutyrate + reduced 2,6-dichlorophenolindophenol
-
low activity for long chain oxidase, no activity for short chain oxidase
-
?
DL-2-hydroxybutyrate + O2

2-oxobutyrate + H2O2
-
68% of the activity compared to glycolate
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
-
-
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
-
-
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
-
-
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
-
-
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
-
-
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
-
-
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
-
-
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
-
best substrate tested
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
-
higher affinity with C5 and C6 hydroxy acids
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
-
best substrate tested
-
?
DL-2-hydroxycaproate + O2

2-oxocaproate + H2O2
-
-
-
?
DL-2-hydroxycaproate + O2
2-oxocaproate + H2O2
-
-
-
?
DL-2-hydroxycaproate + O2
2-oxocaproate + H2O2
-
-
-
?
DL-2-hydroxycaproate + O2
2-oxocaproate + H2O2
-
-
-
?
DL-2-hydroxycaproate + O2
2-oxocaproate + H2O2
-
-
-
?
DL-2-hydroxycaproate + O2
2-oxocaproate + H2O2
-
low activity
-
?
DL-2-hydroxyisocaproate + O2

2-oxoisocaproate + H2O2
-
-
-
?
DL-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
-
-
?
DL-2-hydroxyisovalerate + O2

2-oxoisovalerate + H2O2
-
-
-
?
DL-2-hydroxyisovalerate + O2
2-oxoisovalerate + H2O2
-
low activity
-
?
DL-2-hydroxyisovalerate + O2
2-oxoisovalerate + H2O2
-
low activity
-
?
DL-2-hydroxyisovalerate + O2
2-oxoisovalerate + H2O2
-
low activity
-
?
DL-2-hydroxyisovalerate + O2
2-oxoisovalerate + H2O2
-
low activity
-
?
DL-2-hydroxyvalerate + O2

2-oxovalerate + H2O2
-
39% of the activity compared to glycolate
-
?
DL-2-hydroxyvalerate + O2
2-oxovalerate + H2O2
-
-
-
?
DL-2-hydroxyvalerate + O2
2-oxovalerate + H2O2
-
-
-
?
DL-2-hydroxyvalerate + O2
2-oxovalerate + H2O2
-
-
-
?
DL-2-hydroxyvalerate + O2
2-oxovalerate + H2O2
-
-
-
?
DL-2-hydroxyvalerate + O2
2-oxovalerate + H2O2
-
-
-
?
DL-2-hydroxyvalerate + O2
2-oxovalerate + H2O2
-
low activity
-
?
DL-3-chlorolactate + O2

3-chloropyruvate + H2O2
-
-
-
?
DL-3-chlorolactate + O2
3-chloropyruvate + H2O2
-
-
-
?
DL-3-chlorolactate + O2
3-chloropyruvate + H2O2
-
best substrate tested
-
?
DL-phenyllactate + O2

phenylpyruvate + H2O2
-
-
-
?
DL-phenyllactate + O2
phenylpyruvate + H2O2
-
-
-
?
DL-phenyllactate + O2
phenylpyruvate + H2O2
-
-
-
?
glycolate + 2,6-dichlorophenolindophenol

glyoxylate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
glycolate + 2,6-dichlorophenolindophenol
glyoxylate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
glycolate + 2,6-dichlorophenolindophenol
glyoxylate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
glycolate + 2,6-dichlorophenolindophenol
glyoxylate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
glycolate + 2,6-dichlorophenolindophenol
glyoxylate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
glycolate + 2,6-dichlorophenolindophenol
glyoxylate + reduced 2,6-dichlorophenolindophenol
-
highest activity for short chain oxidase, no activity for long chain oxidase
-
?
glycolate + ferricyanide

glyoxylate + ferrocyanide
-
-
-
?
glycolate + ferricyanide
glyoxylate + ferrocyanide
-
-
-
?
glycolate + O2

glyoxylate + H2O2
-
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
-
-
glycolate + O2
glyoxylate + H2O2
-
-
-
-
-
glycolate + O2
glyoxylate + H2O2
-
-
-
-
-
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
highest activity for isoenzyme HAOX1, no activity for isoenzymes HAOX2, HAOX3
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
substrate for isoenzyme A
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
the catalytic adduct is formed by hydrogen abstraction from the re-face of glycolate
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
-
-
glycolate + O2
glyoxylate + H2O2
-
-
-
-
-
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
plant
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
substrate for isoenzyme A
-
?
glycolate + O2
glyoxylate + H2O2
-
isoenzyme A utilizes short chain aliphatic hydroxy acids, isoenzyme B utilizes long-chain and aromatic hydroxyacids, that may also utilize L-amino acids
-
?
glycolate + O2
glyoxylate + H2O2
-
preference for long chain substrates, more efficient hydroxy acid oxidase than an amino acid oxidase
-
-
-
glycolate + O2
glyoxylate + H2O2
-
-
-
-
-
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
-
-
glycolate + O2
glyoxylate + H2O2
-
-
-
-
-
glycolate + O2
glyoxylate + H2O2
-
-
-
-
-
glycolate + O2
glyoxylate + H2O2
-
-
-
-
?
glyoxylate + 2,6-dichlorophenolindophenol

? + reduced 2,6-dichlorophenolindophenol
-
-
-
?
glyoxylate + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
?
glyoxylate + O2

? + H2O2
-
substrate for isoenzyme HAOX1
-
?
glyoxylate + O2
? + H2O2
-
26% of the activity compared to glycolate
-
?
glyoxylate + O2
? + H2O2
-
-
-
?
glyoxylate + O2
? + H2O2
-
in the absence of any nucleophile less than 2% of the activity compared to glycolate
-
?
glyoxylate + O2
? + H2O2
-
40% of the activity compared to glycolate
-
?
glyoxylate + O2
? + H2O2
-
-
-
?
L-2-hydroxy-beta-methylvalerate + 2,6-dichlorophenolindophenol

3-methyl-2-oxopentanoate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
-
L-2-hydroxy-beta-methylvalerate + 2,6-dichlorophenolindophenol
3-methyl-2-oxopentanoate + reduced 2,6-dichlorophenolindophenol
-
no activity for short chain oxidase
-
?
L-2-hydroxyisocaproate + O2

2-oxoisocaproate + H2O2
-
substrate for isoenzyme B
-
?
L-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
-
-
?
L-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
-
-
?
L-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
-
-
?
L-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
best substrate tested
-
?
L-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
substrate for isoenzyme B
-
?
L-2-hydroxyphenyllactate + O2

? + H2O2
-
-
-
?
L-2-hydroxyphenyllactate + O2
? + H2O2
-
-
-
?
L-lactate + 2,6-dichlorophenolindophenol

pyruvate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
L-lactate + 2,6-dichlorophenolindophenol
pyruvate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
L-lactate + 2,6-dichlorophenolindophenol
pyruvate + reduced 2,6-dichlorophenolindophenol
-
lower activity for preparation from "heavy" mitochondria
-
?
L-lactate + 2,6-dichlorophenolindophenol
pyruvate + reduced 2,6-dichlorophenolindophenol
-
very low activity
-
?
L-lactate + O2

pyruvate + H2O2
-
-
-
-
?
L-lactate + O2
pyruvate + H2O2
-
-
-
?
L-lactate + O2
pyruvate + H2O2
-
28% of the activity compared to glycolate
-
?
L-lactate + O2
pyruvate + H2O2
-
yoghurt mixed and homogenized in water, filtered (20-25 microm), this sample injected into the luminometer measuring cell containing the lactate biosensor-system
-
-
?
L-lactate + O2
pyruvate + H2O2
-
-
-
?
L-lactate + O2
pyruvate + H2O2
-
-
-
?
L-lactate + O2
pyruvate + H2O2
-
-
-
?
L-lactate + O2
pyruvate + H2O2
-
-
-
?
L-lactate + O2
pyruvate + H2O2
-
very low activity
-
?
L-lactate + O2
pyruvate + H2O2
-
high activity, does not act on D-lactate
-
?
L-leucine + O2

? + H2O2
-
-
-
?
L-leucine + O2
? + H2O2
-
-
-
?
L-leucine + O2
? + H2O2
-
highest activity
-
?
L-mandelate + 2,6-dichlorophenolindophenol

oxo(phenyl)acetic acid + reduced 2,6-dichlorophenolindophenol
-
-
-
?
L-mandelate + 2,6-dichlorophenolindophenol
oxo(phenyl)acetic acid + reduced 2,6-dichlorophenolindophenol
-
-
-
?
L-mandelate + O2

?
-
A95G-mutant is also reactive
-
-
?
L-mandelate + O2
?
-
the step involving the removal of the alpha-hydrogen is rate-limiting, A95G-mutant is also reactive
-
-
?
L-methionine + O2

? + H2O2
-
-
-
?
L-methionine + O2
? + H2O2
-
-
-
?
L-phenyllactate + 2,6-dichlorophenolindophenol

phenylpyruvate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
L-phenyllactate + 2,6-dichlorophenolindophenol
phenylpyruvate + reduced 2,6-dichlorophenolindophenol
-
-
-
-
-
L-tryptophan + O2

? + H2O2
-
-
-
?
L-tryptophan + O2
? + H2O2
-
-
-
?
L-tryptophan + O2
? + H2O2
-
-
-
?
lactate + O2

pyruvate + H2O2
-
-
-
?
lactate + O2
pyruvate + H2O2
-
-
-
?
lactate + O2
pyruvate + H2O2
-
lactate detection in beer samples
H2O2 oxidizes Prussian Blue on an electrode, the concomitant electron flow is measured
-
?
lactate + O2
pyruvate + H2O2
-
-
-
?
lactate + O2
pyruvate + H2O2
-
-
-
?
additional information

?
-
isozyme lHAOX1 displays the highest activity with the long-chain fatty acid 2-hydroxyhexadecanoic acid (2-hydroxypalmitic acid) and has intermediate activity with 2-hydroxyhexanoic acid (2-hydroxycaproic acid), 2-hydroxyoctanoic acid (2-hydroxycaprylic acid), and the short-chain hydroxyacid L-lactate. With much lower activity, it can also use glycolate, leucic acid, valic acid, and isoleucic acid as substrates. No activity with 2-hydroxyhexadecanoic acid and D-lactate
-
-
-
additional information
?
-
isozyme lHAOX1 displays the highest activity with the long-chain fatty acid 2-hydroxyhexadecanoic acid (2-hydroxypalmitic acid) and has intermediate activity with 2-hydroxyhexanoic acid (2-hydroxycaproic acid), 2-hydroxyoctanoic acid (2-hydroxycaprylic acid), and the short-chain hydroxyacid L-lactate. With much lower activity, it can also use glycolate, leucic acid, valic acid, and isoleucic acid as substrates. No activity with 2-hydroxyhexadecanoic acid and D-lactate
-
-
-
additional information
?
-
isozyme lHAOX1 displays the highest activity with the long-chain fatty acid 2-hydroxyhexadecanoic acid (2-hydroxypalmitic acid) and has intermediate activity with 2-hydroxyhexanoic acid (2-hydroxycaproic acid), 2-hydroxyoctanoic acid (2-hydroxycaprylic acid), and the short-chain hydroxyacid L-lactate. With much lower activity, it can also use glycolate, leucic acid, valic acid, and isoleucic acid as substrates. No activity with 2-hydroxyhexadecanoic acid and D-lactate
-
-
-
additional information
?
-
isozyme lHAOX2 exhibits the highest activity with leucic acid. It shows intermediate activity with 2-hydroxyhexanoic acid and 2-hydroxyoctanoic acid. lHAOX2 displays lower activity with 2-hydroxydodecanoic acid, valic acid, and isoleucic acid and poor activity with glycolate and L-lactate. No activity with 2-hydroxyhexadecanoic acid and D-lactate
-
-
-
additional information
?
-
isozyme lHAOX2 exhibits the highest activity with leucic acid. It shows intermediate activity with 2-hydroxyhexanoic acid and 2-hydroxyoctanoic acid. lHAOX2 displays lower activity with 2-hydroxydodecanoic acid, valic acid, and isoleucic acid and poor activity with glycolate and L-lactate. No activity with 2-hydroxyhexadecanoic acid and D-lactate
-
-
-
additional information
?
-
isozyme lHAOX2 exhibits the highest activity with leucic acid. It shows intermediate activity with 2-hydroxyhexanoic acid and 2-hydroxyoctanoic acid. lHAOX2 displays lower activity with 2-hydroxydodecanoic acid, valic acid, and isoleucic acid and poor activity with glycolate and L-lactate. No activity with 2-hydroxyhexadecanoic acid and D-lactate
-
-
-
additional information
?
-
-
no substrate: oxalate, acetate, pyruvate, glycerol, propionate, succinate, fumarate, malate, maleate, tartrate, oxaloacetate, 2-oxoglutarate, glycocol,L-alanine, serine, glutamate, ascorbate, glucose, and fructose
-
-
-
additional information
?
-
-
interaction of Rice dwarf virus, RDV, outer capsid P8 protein with rice glycolate oxidase mediates relocalization of P8, GOX may play important roles in RDV targeting into the replication site of host cells, overview
-
-
-
additional information
?
-
-
GLO is a typical photorespiratory enzyme and it exerts a strong regulation over photosynthesis, possibly through a feed-back inhibition on Rubisco activase, the glyoxylate cycle may be partially activated to compensate for the photorespiratory glyoxylate when GLO is suppressed in rice
-
-
-
additional information
?
-
GLO is a typical photorespiratory enzyme and it exerts a strong regulation over photosynthesis, possibly through a feed-back inhibition on Rubisco activase, the glyoxylate cycle may be partially activated to compensate for the photorespiratory glyoxylate when GLO is suppressed in rice
-
-
-
additional information
?
-
the enzyme is involved in the photorespiration process
-
-
-
additional information
?
-
B7FUG8
the enzyme is not able to metabolize D-lactate
-
-
-
additional information
?
-
-
long-chain L-alpha-hydroxy acid oxidase (LCHAO) is a FMN-dependent oxidase that dehydrogenates L-alpha-hydroxy acids to oxo acids
-
-
-
additional information
?
-
-
the enzyme is involved in the photorespiration process
-
-
-
additional information
?
-
-
energy-yielding metabolism can be described as follows: as long as glucose is available, approximatelyone-fourth of the pyruvate formed is converted to acetate by the sequential action of pyruvate oxidase and acetate kinase with acquisition of additional ATP. The rest of the pyruvate is reduced by lactate dehydrogenase to form lactate, with partial achievement of redox balance. The lactate is oxidized by lactate oxidase back to pyruvate, which is converted to acetate as described above; and the sequential reactions mentioned above continue to occur as long as lactate is present
-
-
-
additional information
?
-
-
energy-yielding metabolism can be described as follows: as long as glucose is available, approximatelyone-fourth of the pyruvate formed is converted to acetate by the sequential action of pyruvate oxidase and acetate kinase with acquisition of additional ATP. The rest of the pyruvate is reduced by lactate dehydrogenase to form lactate, with partial achievement of redox balance. The lactate is oxidized by lactate oxidase back to pyruvate, which is converted to acetate as described above; and the sequential reactions mentioned above continue to occur as long as lactate is present
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(S)-lactate + O2
acetate + CO2 + H2O
(S)-lactate + O2
pyruvate + H2O2
2-hydroxycaproate + O2
2-oxocaproate + H2O2
Q24JJ8, Q9LJH5, Q9LRR9
-
-
-
?
2-hydroxycaprylate + O2
2-oxocaprylate + H2O2
Q24JJ8, Q9LJH5, Q9LRR9
-
-
-
?
2-hydroxyoctanoate + O2
2-oxooctanoate + H2O2
-
substrates for isoenzymes HAOX1, HAOX2, preferred substrate for isoenzyme HAOX3
-
?
2-hydroxypalmitate + O2
2-oxopalmitate + H2O2
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
D-2 -hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
D-lactate + O2
pyruvate + H2O2
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
DL-2-hydroxycaproate + O2
2-oxocaproate + H2O2
DL-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
DL-2-hydroxyisovalerate + O2
2-oxoisovalerate + H2O2
DL-2-hydroxyvalerate + O2
2-oxovalerate + H2O2
DL-glycerate + O2
? + H2O2
-
-
-
?
DL-lactate + O2
pyruvate + H2O2
-
-
-
?
DL-methionine + O2
? + H2O2
-
-
-
?
glycolate + acceptor
glyoxylate + reduced acceptor
B7FUG8
-
-
-
?
glycolate + O2
glyoxylate + H2O2
glyoxylate thiohemiacetals + O2
? + H2O2
-
possible natural substrates, i.e. glyoxylate thiohemiacetals of coemzyme A, D-phosphopantetheine, D-pantetheine, N-acetylcysteamine, 2-mercaptoethanol, DL-dihydrolipoate, propane-1,3-dithiol
-
?
homoserine + O2
? + H2O2
-
traces of activity
-
?
L-2-hydroxy-4-methylthiobutanoic acid + O2
3-(methylthio)propanoate + HCO3-
-
oxidative decarboxylation
-
?
L-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
L-alanine + O2
? + H2O2
-
low activity
-
?
L-isoleucine + O2
? + H2O2
-
low activity
-
?
L-lactate + O2
pyruvate + H2O2
L-lysine + O2
? + H2O2
-
-
-
?
L-mandelate + O2
? + H2O2
-
-
-
?
L-methionine + O2
? + H2O2
L-phenylalanine + O2
? + H2O2
-
-
-
?
L-tryptophan + O2
? + H2O2
L-tyrosine + O2
? + H2O2
-
-
-
?
L-valine + O2
? + H2O2
-
low activity
-
?
lactate + O2
pyruvate + H2O2
thiol-glyoxylate adducts + O2
an oxalyl thioester + H2O2
-
may be the physiological substrates
-
?
additional information
?
-
(S)-lactate + O2

acetate + CO2 + H2O
-
-
-
-
?
(S)-lactate + O2
acetate + CO2 + H2O
-
-
-
-
?
(S)-lactate + O2

pyruvate + H2O2
-
no decarboxylation
-
?
(S)-lactate + O2
pyruvate + H2O2
-
no decarboxylation
-
?
(S)-lactate + O2
pyruvate + H2O2
-
-
-
?
(S)-lactate + O2
pyruvate + H2O2
-
-
-
-
?
(S)-lactate + O2
pyruvate + H2O2
-
-
-
-
?
2-hydroxypalmitate + O2

2-oxopalmitate + H2O2
Q24JJ8, Q9LJH5, Q9LRR9
-
-
-
?
2-hydroxypalmitate + O2
2-oxopalmitate + H2O2
-
substrates for isoenzymes HAOX1, HAOX2
-
?
an (S)-2-hydroxy carboxylate + O2

a 2-oxo carboxylate + H2O2
Q24JJ8, Q9LJH5, Q9LRR9
-
-
-
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
Q9NYQ3
-
-
-
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
-
-
-
-
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
Q9NYQ2
-
-
-
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
Q9NYQ2
-
-
-
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
Q9WU19
-
-
-
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
-
-
-
-
?
an (S)-2-hydroxy carboxylate + O2
a 2-oxo carboxylate + H2O2
Q07523
-
-
-
?
D-2 -hydroxyisocaproate + O2

2-oxoisocaproate + H2O2
-
48% of the activity compared to glycolate
-
?
D-2 -hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
liver enzyme is much less active with C4 or C5 alpha-hydroxy acids but as active as with glycolate
-
?
D-lactate + O2

pyruvate + H2O2
-
traces of activity
-
?
D-lactate + O2
pyruvate + H2O2
-
traces of activity
-
?
D-lactate + O2
pyruvate + H2O2
-
traces of activity
-
?
DL-2-hydroxybutyrate + O2

2-oxobutyrate + H2O2
-
68% of the activity compared to glycolate
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
-
-
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
-
-
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
-
-
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
-
-
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
-
-
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
-
-
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
-
-
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
-
best substrate tested
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
-
higher affinity with C5 and C6 hydroxy acids
-
?
DL-2-hydroxybutyrate + O2
2-oxobutyrate + H2O2
-
best substrate tested
-
?
DL-2-hydroxycaproate + O2

2-oxocaproate + H2O2
-
-
-
?
DL-2-hydroxycaproate + O2
2-oxocaproate + H2O2
-
-
-
?
DL-2-hydroxycaproate + O2
2-oxocaproate + H2O2
-
-
-
?
DL-2-hydroxycaproate + O2
2-oxocaproate + H2O2
-
-
-
?
DL-2-hydroxycaproate + O2
2-oxocaproate + H2O2
-
-
-
?
DL-2-hydroxycaproate + O2
2-oxocaproate + H2O2
-
low activity
-
?
DL-2-hydroxyisocaproate + O2

2-oxoisocaproate + H2O2
-
-
-
?
DL-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
-
-
?
DL-2-hydroxyisovalerate + O2

2-oxoisovalerate + H2O2
-
-
-
?
DL-2-hydroxyisovalerate + O2
2-oxoisovalerate + H2O2
-
low activity
-
?
DL-2-hydroxyisovalerate + O2
2-oxoisovalerate + H2O2
-
low activity
-
?
DL-2-hydroxyisovalerate + O2
2-oxoisovalerate + H2O2
-
low activity
-
?
DL-2-hydroxyisovalerate + O2
2-oxoisovalerate + H2O2
-
low activity
-
?
DL-2-hydroxyvalerate + O2

2-oxovalerate + H2O2
-
39% of the activity compared to glycolate
-
?
DL-2-hydroxyvalerate + O2
2-oxovalerate + H2O2
-
-
-
?
DL-2-hydroxyvalerate + O2
2-oxovalerate + H2O2
-
-
-
?
DL-2-hydroxyvalerate + O2
2-oxovalerate + H2O2
-
-
-
?
DL-2-hydroxyvalerate + O2
2-oxovalerate + H2O2
-
-
-
?
DL-2-hydroxyvalerate + O2
2-oxovalerate + H2O2
-
-
-
?
DL-2-hydroxyvalerate + O2
2-oxovalerate + H2O2
-
low activity
-
?
glycolate + O2

glyoxylate + H2O2
-
-
-
-
?
glycolate + O2
glyoxylate + H2O2
Q56ZN0
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
highest activity for isoenzyme HAOX1, no activity for isoenzymes HAOX2, HAOX3
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
Q9WU19
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
substrate for isoenzyme A
-
?
glycolate + O2
glyoxylate + H2O2
Q9WU19
-
-
-
?
glycolate + O2
glyoxylate + H2O2
Q10CE4
-
-
-
?
glycolate + O2
glyoxylate + H2O2
plant
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
substrate for isoenzyme A
-
?
glycolate + O2
glyoxylate + H2O2
-
isoenzyme A utilizes short chain aliphatic hydroxy acids, isoenzyme B utilizes long-chain and aromatic hydroxyacids, that may also utilize L-amino acids
-
?
glycolate + O2
glyoxylate + H2O2
-
preference for long chain substrates, more efficient hydroxy acid oxidase than an amino acid oxidase
-
-
-
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
?
glycolate + O2
glyoxylate + H2O2
-
-
-
-
?
glyoxylate + O2

? + H2O2
-
substrate for isoenzyme HAOX1
-
?
glyoxylate + O2
? + H2O2
-
26% of the activity compared to glycolate
-
?
glyoxylate + O2
? + H2O2
-
-
-
?
glyoxylate + O2
? + H2O2
-
in the absence of any nucleophile less than 2% of the activity compared to glycolate
-
?
glyoxylate + O2
? + H2O2
-
40% of the activity compared to glycolate
-
?
glyoxylate + O2
? + H2O2
-
-
-
?
L-2-hydroxyisocaproate + O2

2-oxoisocaproate + H2O2
-
substrate for isoenzyme B
-
?
L-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
-
-
?
L-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
-
-
?
L-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
-
-
?
L-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
best substrate tested
-
?
L-2-hydroxyisocaproate + O2
2-oxoisocaproate + H2O2
-
substrate for isoenzyme B
-
?
L-lactate + O2

pyruvate + H2O2
Q24JJ8, Q9LJH5, Q9LRR9
-
-
-
?
L-lactate + O2
pyruvate + H2O2
-
28% of the activity compared to glycolate
-
?
L-lactate + O2
pyruvate + H2O2
-
yoghurt mixed and homogenized in water, filtered (20-25 microm), this sample injected into the luminometer measuring cell containing the lactate biosensor-system
-
-
?
L-lactate + O2
pyruvate + H2O2
-
-
-
?
L-lactate + O2
pyruvate + H2O2
-
-
-
?
L-lactate + O2
pyruvate + H2O2
-
-
-
?
L-lactate + O2
pyruvate + H2O2
-
very low activity
-
?
L-lactate + O2
pyruvate + H2O2
-
high activity, does not act on D-lactate
-
?
L-leucine + O2

? + H2O2
-
-
-
?
L-leucine + O2
? + H2O2
-
-
-
?
L-leucine + O2
? + H2O2
-
highest activity
-
?
L-methionine + O2

? + H2O2
-
-
-
?
L-methionine + O2
? + H2O2
-
-
-
?
L-tryptophan + O2

? + H2O2
-
-
-
?
L-tryptophan + O2
? + H2O2
-
-
-
?
L-tryptophan + O2
? + H2O2
-
-
-
?
lactate + O2

pyruvate + H2O2
Q9CG58
-
-
-
?
lactate + O2
pyruvate + H2O2
Q9CG58
-
-
-
?
lactate + O2
pyruvate + H2O2
-
lactate detection in beer samples
H2O2 oxidizes Prussian Blue on an electrode, the concomitant electron flow is measured
-
?
lactate + O2
pyruvate + H2O2
A9QH69, A9QH71
-
-
-
?
lactate + O2
pyruvate + H2O2
A9QH71
-
-
-
?
additional information

?
-
-
interaction of Rice dwarf virus, RDV, outer capsid P8 protein with rice glycolate oxidase mediates relocalization of P8, GOX may play important roles in RDV targeting into the replication site of host cells, overview
-
-
-
additional information
?
-
-
GLO is a typical photorespiratory enzyme and it exerts a strong regulation over photosynthesis, possibly through a feed-back inhibition on Rubisco activase, the glyoxylate cycle may be partially activated to compensate for the photorespiratory glyoxylate when GLO is suppressed in rice
-
-
-
additional information
?
-
Q10CE4
GLO is a typical photorespiratory enzyme and it exerts a strong regulation over photosynthesis, possibly through a feed-back inhibition on Rubisco activase, the glyoxylate cycle may be partially activated to compensate for the photorespiratory glyoxylate when GLO is suppressed in rice
-
-
-
additional information
?
-
Q19U05
the enzyme is involved in the photorespiration process
-
-
-
additional information
?
-
-
long-chain L-alpha-hydroxy acid oxidase (LCHAO) is a FMN-dependent oxidase that dehydrogenates L-alpha-hydroxy acids to oxo acids
-
-
-
additional information
?
-
-
the enzyme is involved in the photorespiration process
-
-
-
additional information
?
-
-
energy-yielding metabolism can be described as follows: as long as glucose is available, approximatelyone-fourth of the pyruvate formed is converted to acetate by the sequential action of pyruvate oxidase and acetate kinase with acquisition of additional ATP. The rest of the pyruvate is reduced by lactate dehydrogenase to form lactate, with partial achievement of redox balance. The lactate is oxidized by lactate oxidase back to pyruvate, which is converted to acetate as described above; and the sequential reactions mentioned above continue to occur as long as lactate is present
-
-
-
additional information
?
-
-
energy-yielding metabolism can be described as follows: as long as glucose is available, approximatelyone-fourth of the pyruvate formed is converted to acetate by the sequential action of pyruvate oxidase and acetate kinase with acquisition of additional ATP. The rest of the pyruvate is reduced by lactate dehydrogenase to form lactate, with partial achievement of redox balance. The lactate is oxidized by lactate oxidase back to pyruvate, which is converted to acetate as described above; and the sequential reactions mentioned above continue to occur as long as lactate is present
-
-
-
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2,6-dichlorophenolindophenol
-
inhibition by excess substrate
2-hydroxybutynoate
-
inhibition of transhydrogenation reaction
2-oxobutyrate
-
non-competitive inhibition at 5 mM
2-oxoisocaproate
-
non-competitive inhibition at 5 mM, most active inhibitor of 2-keto acids, oxidation of 2-hydroxybutyrate most sensitive
2-oxoisovalerate
-
non-competitive inhibition at 5 mM
2-oxovalerate
-
non-competitive inhibition at 5 mM
2-pyridylhydroxymethanesulfonate
-
strong inhibition between 0.1-1 mM
3-benzyl-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
3-decyl-2,5-dioxo-4-hydroxy-3-pyrroline
-
bound to the active site in the three-dimensional structure
3-ethoxy-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
3-ethyl-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
3-methyl-4-(2-phenoxybenzyl)-1H-pyrazole-5-carboxylic acid
3-methyl-4-(2-phenylethyl)-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-(3-phenoxybenzyl)-1H-pyrazole-5-carboxylic acid
3-methyl-4-(4-phenoxybenzyl)-1H-pyrazole-5-carboxylic acid
3-methyl-4-(naphthalen-1-ylmethyl)-1H-pyrazole-5-carboxylic acid
3-methyl-4-(naphthalen-2-ylmethyl)-1H-pyrazole-5-carboxylic acid
3-methyl-4-(quinolin-2-ylmethyl)-1H-pyrazole-5-carboxylic acid
3-methyl-4-[2-(trifluoromethoxy)benzyl]-1H-pyrazole-5-carboxylic acid
3-methyl-4-[2-(trifluoromethyl)benzyl]-1H-pyrazole-5-carboxylic acid
3-methyl-4-[3-(pyridin-3-yl)benzyl]-1H-pyrazole-5-carboxylic acid
3-methyl-4-[3-(pyridin-4-yl)benzyl]-1H-pyrazole-5-carboxylic acid
3-methyl-4-[3-(trifluoromethyl)benzyl]-1H-pyrazole-5-carboxylic acid
3-methyl-4-[4-(trifluoromethoxy)benzyl]-1H-pyrazole-5-carboxylic acid
3-methyl-4-[4-(trifluoromethyl)benzyl]-1H-pyrazole-5-carboxylic acid
3-methyl-4-[[4'-(trifluoromethoxy)biphenyl-3-yl]methyl]-1H-pyrazole-5-carboxylic acid
3-methyl-4-[[4'-(trifluoromethoxy)biphenyl-4-yl]methyl]-1H-pyrazole-5-carboxylic acid
3-methyl-4-[[4'-(trifluoromethyl)biphenyl-3-yl]methyl]-1H-pyrazole-5-carboxylic acid
3-methyl-4-[[4'-(trifluoromethyl)biphenyl-4-yl]methyl]-1H-pyrazole-5-carboxylic acid
4-(1-benzofuran-2-ylmethyl)-3-methyl-1H-pyrazole-5-carboxylic acid
4-(1-benzothiophen-2-ylmethyl)-3-methyl-1H-pyrazole-5-carboxylic acid
4-(3-carbamoylbenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
4-(3-carboxybenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
4-(3-cyanobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
4-(3-fluorobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
4-(4'-fluorobiphenyl-3-yl)-3-methyl-1H-pyrazole-5-carboxylic acid
4-(4'-fluorobiphenyl-4-yl)-3-methyl-1H-pyrazole-5-carboxylic acid
4-(4-carbamoylbenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
4-(4-carboxybenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
4-(4-cyanobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
4-(4-fluorobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
4-(4-fluorophenyl)-3-methyl-1H-pyrazole-5-carboxylic acid
4-(biphenyl-3-ylmethyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-carboxy-5-(1-pentyl)hexylsulfanyl-1,2,3-triazole
-
bound to the active site in the three-dimensional structure
4-carboxy-5-dodecylsulfanyl-1,2,3-triazole
-
-
4-carboxy-5-[(4-chlorophenyl)sulfanyl]-1,2,3-thiadiazole
-
CCPST
-
4-[(2'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
4-[(3'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
4-[(4'-carbamoylbiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
4-[(4'-carboxybiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
4-[(4'-cyanobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
4-[(4'-fluorobiphenyl-2-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
4-[(4'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
4-[(4'-fluorobiphenyl-4-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
4-[2-(4'-fluorobiphenyl-3-yl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
4-[2-(4'-fluorobiphenyl-4-yl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
4-[2-(4-fluorophenyl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
4-[2-(biphenyl-4-yl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[[4'-(2-amino-2-oxoethyl)biphenyl-3-yl]methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-(2-phenylethyl)-1H-pyrazole-5-carboxylic acid
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-(propan-2-yl)-1H-pyrazole-5-carboxylic acid
4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-phenyl-1H-pyrazole-5-carboxylic acid
arsenate
-
inhibition of glycolate-ferricyanide or glyoxylate-ferricyanide assay above 0.1 M
Atebrin
-
long chain oxidase, 72-76% inhibition at 1 mM, short chain oxidase: 68-76% inhibition at 1 mM
benzaldehyde
-
50% inhibition at 2 mM
bipyridine
-
strong inhibition
caproate
-
mixed-type non-competitive inhibition
chloride
-
inhibits the enzyme at high concentrations
Cibacron blue 3GA
-
at a concentration higher than 0.001 mM is a normal competitive inhibitor, at concentrations below 0.001 mM the inhibition is time-, dye- and pH-dependent
cysteine
-
28-38% inhibition of glycolate oxidation at 1 mM
dihydrolipoate
-
competitive inhibition of 2-hydroxybutyrate oxidation
Dithionite
-
reduction of FMN
DL-2-hydroxy-3-butynoate
-
irreversible inactivation after 25 turnovers, covalent addition to the coenzyme
DL-2-hydroxy-3-heptynoate
-
inactivation after18000 turnovers
DL-2-hydroxy-3-hexynoate
-
inactivation after 8500 turnovers
DL-2-hydroxy-3-octynoate
-
inactivation after 15000 turnovers
DL-2-hydroxy-3-pentynoate
-
inactivation after 4800 turnovers
DL-2-hydroxyisocaproate
-
marked inhibition above 50 mM
DL-2-hydroxyvalerate
-
marked inhibition above 50 mM
DL-beta-Phenyllactate
-
short chain oxidase: 10% inhibition of glycolate oxidation, 81% inhibition of L-2-hydroxisocaproate oxidation at 10 mM
DL-Lipoate
-
long chain oxidase, 35% inhibition at 0.24 mM, short chain oxidase: 46-52% inhibition at 0.01 mM
DL-vinylglycolate
-
slight inactivation after 10000 turnovers
hydoxylamine
-
66-67% inhibition at 5 mM
hydroxylamine
-
50% inhibition at 5 mM, competitive
iodoacetamide
-
inhibition at 50 mM
L-phenylalanine
-
long chain oxidase, 43% inhibition at 33 mM
oxamate
-
mixed-type non-competitive inhibition
Quinacrine
-
6% inhibition at 1 mM
rotenone
-
50% inhibition at 0.1 mM
sodium sulfite
-
reduces FMN
trans-cinnamate
-
competitive inhibition
2-Hydroxybutyrate

-
at pH 7.0
2-Hydroxybutyrate
-
long chain oxidase, 13-17% inhibition at 17 mM
3-benzyl-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid

-
-
3-benzyl-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
3-ethoxy-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid

-
-
3-ethoxy-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
3-ethyl-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid

-
-
3-ethyl-4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-(2-phenoxybenzyl)-1H-pyrazole-5-carboxylic acid

-
-
3-methyl-4-(2-phenoxybenzyl)-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-(3-phenoxybenzyl)-1H-pyrazole-5-carboxylic acid

-
-
3-methyl-4-(3-phenoxybenzyl)-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-(4-phenoxybenzyl)-1H-pyrazole-5-carboxylic acid

-
-
3-methyl-4-(4-phenoxybenzyl)-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-(naphthalen-1-ylmethyl)-1H-pyrazole-5-carboxylic acid

-
-
3-methyl-4-(naphthalen-1-ylmethyl)-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-(naphthalen-2-ylmethyl)-1H-pyrazole-5-carboxylic acid

-
-
3-methyl-4-(naphthalen-2-ylmethyl)-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-(quinolin-2-ylmethyl)-1H-pyrazole-5-carboxylic acid

-
-
3-methyl-4-(quinolin-2-ylmethyl)-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[2-(trifluoromethoxy)benzyl]-1H-pyrazole-5-carboxylic acid

-
-
3-methyl-4-[2-(trifluoromethoxy)benzyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[2-(trifluoromethyl)benzyl]-1H-pyrazole-5-carboxylic acid

-
-
3-methyl-4-[2-(trifluoromethyl)benzyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[3-(pyridin-3-yl)benzyl]-1H-pyrazole-5-carboxylic acid

-
-
3-methyl-4-[3-(pyridin-3-yl)benzyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[3-(pyridin-4-yl)benzyl]-1H-pyrazole-5-carboxylic acid

-
-
3-methyl-4-[3-(pyridin-4-yl)benzyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[3-(trifluoromethyl)benzyl]-1H-pyrazole-5-carboxylic acid

-
-
3-methyl-4-[3-(trifluoromethyl)benzyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[4-(trifluoromethoxy)benzyl]-1H-pyrazole-5-carboxylic acid

-
-
3-methyl-4-[4-(trifluoromethoxy)benzyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[4-(trifluoromethyl)benzyl]-1H-pyrazole-5-carboxylic acid

-
-
3-methyl-4-[4-(trifluoromethyl)benzyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[[4'-(trifluoromethoxy)biphenyl-3-yl]methyl]-1H-pyrazole-5-carboxylic acid

-
-
3-methyl-4-[[4'-(trifluoromethoxy)biphenyl-3-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[[4'-(trifluoromethoxy)biphenyl-4-yl]methyl]-1H-pyrazole-5-carboxylic acid

-
-
3-methyl-4-[[4'-(trifluoromethoxy)biphenyl-4-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[[4'-(trifluoromethyl)biphenyl-3-yl]methyl]-1H-pyrazole-5-carboxylic acid

-
-
3-methyl-4-[[4'-(trifluoromethyl)biphenyl-3-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
3-methyl-4-[[4'-(trifluoromethyl)biphenyl-4-yl]methyl]-1H-pyrazole-5-carboxylic acid

-
-
3-methyl-4-[[4'-(trifluoromethyl)biphenyl-4-yl]methyl]-1H-pyrazole-5-carboxylic acid
-
-
4-(1-benzofuran-2-ylmethyl)-3-methyl-1H-pyrazole-5-carboxylic acid

-
-
4-(1-benzofuran-2-ylmethyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(1-benzothiophen-2-ylmethyl)-3-methyl-1H-pyrazole-5-carboxylic acid

-
-
4-(1-benzothiophen-2-ylmethyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(3-carbamoylbenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid

-
-
4-(3-carbamoylbenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(3-carboxybenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid

-
-
4-(3-carboxybenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(3-cyanobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid

-
-
4-(3-cyanobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(3-fluorobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid

-
-
4-(3-fluorobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(4'-fluorobiphenyl-3-yl)-3-methyl-1H-pyrazole-5-carboxylic acid

-
-
4-(4'-fluorobiphenyl-3-yl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(4'-fluorobiphenyl-4-yl)-3-methyl-1H-pyrazole-5-carboxylic acid

-
-
4-(4'-fluorobiphenyl-4-yl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(4-carbamoylbenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid

-
-
4-(4-carbamoylbenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(4-carboxybenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid

-
-
4-(4-carboxybenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(4-cyanobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid

-
-
4-(4-cyanobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(4-fluorobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid

-
-
4-(4-fluorobenzyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-(4-fluorophenyl)-3-methyl-1H-pyrazole-5-carboxylic acid

-
-
4-(4-fluorophenyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
35% inhibition at 0.010 mM
4-(4-fluorophenyl)-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-chloromercuribenzoate

-
strong inhibition at 0.01 mM
4-chloromercuribenzoate
-
inhibition at 50 mM
4-chloromercuribenzoate
-
long chain oxidase, 29-42% inhibition at 0.001 mM, short chain oxidase: 70-75% inhibition at 0.001 mM
4-[(2'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid

-
-
4-[(2'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[(3'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid

-
-
4-[(3'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[(4'-carbamoylbiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid

-
-
4-[(4'-carbamoylbiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[(4'-carboxybiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid

-
-
4-[(4'-carboxybiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[(4'-cyanobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid

-
-
4-[(4'-cyanobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[(4'-fluorobiphenyl-2-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid

-
-
4-[(4'-fluorobiphenyl-2-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[(4'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid

-
-
4-[(4'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[(4'-fluorobiphenyl-4-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid

-
-
4-[(4'-fluorobiphenyl-4-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[2-(4'-fluorobiphenyl-3-yl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid

-
-
4-[2-(4'-fluorobiphenyl-3-yl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
-
-
4-[2-(4'-fluorobiphenyl-4-yl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid

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4-[2-(4'-fluorobiphenyl-4-yl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
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4-[2-(4-fluorophenyl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid

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4-[2-(4-fluorophenyl)ethyl]-3-methyl-1H-pyrazole-5-carboxylic acid
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4-[[4'-(2-amino-2-oxoethyl)biphenyl-3-yl]methyl]-3-methyl-1H-pyrazole-5-carboxylic acid

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4-[[4'-(2-amino-2-oxoethyl)biphenyl-3-yl]methyl]-3-methyl-1H-pyrazole-5-carboxylic acid
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4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-(2-phenylethyl)-1H-pyrazole-5-carboxylic acid

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4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-(2-phenylethyl)-1H-pyrazole-5-carboxylic acid
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4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-(propan-2-yl)-1H-pyrazole-5-carboxylic acid

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4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-(propan-2-yl)-1H-pyrazole-5-carboxylic acid
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4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-phenyl-1H-pyrazole-5-carboxylic acid

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4-[[4-(4-fluorophenyl)pyridin-2-yl]methyl]-3-phenyl-1H-pyrazole-5-carboxylic acid
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8-hydroxyquinoline

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50% inhibition at 0.05 mM
8-hydroxyquinoline
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5-17% inhibition at 1 mM
8-hydroxyquinoline
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8-17% inhibition at 1 mM
acetate

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mixed-type non-competitive inhibition
Cu2+

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nearly complete inhibition at 0.025 mM
Cu2+
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complete inhibition at 0.025 mM
Cu2+
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50% inhibition at 0.2 mM
Cu2+
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short chain oxidase: 86% inhibition at 0.1 mM
diethyldithiocarbamate

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competitive inhibition
diethyldithiocarbamate
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51-55% inhibition at 1 mM
diphenylglycolic acid

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11-17% inhibition at 52 mM
diphenylglycolic acid
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50% inhibition at 52 mM, competitive
glycolate

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glycolate
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inhibition by excess substrate
glycolate
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inhibition above 1.7 mM
glyoxylate

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inhibition by excess substrate
glyoxylate
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substrate inhibition at concentrations above 4 mM
iodoacetate

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inhibition at 50 mM
iodoacetate
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long chain oxidase, 31-36% inhibition at 0.1 mM, short chain oxidase: no inhibition
KCN

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mixed-type inhibitor
KCN
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30% inhibition of L-2-hydroxyisocaproate oxidation at 1 mM, 91% inhibition of glycolate oxidation at 1 mM
L-leucine

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competitive inhibition
L-leucine
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9-12% inhibition at 33 mM
L-Mandelate

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at pH 7.0
L-Mandelate
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inhibition by excess substrate
o-Iodosobenzoate

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46-62% inhibition at 0.1 mM
o-Iodosobenzoate
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46% inhibition at 0.1 mM
o-Iodosobenzoate
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long chain oxidase, 95-100% inhibition at 0.1 mM, short chain oxidase: no inhibition
o-phenanthroline

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strong inhibition between 0.1-1.0 mM
o-phenanthroline
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5-23% inhibition at 1 mM
o-phenanthroline
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5-14% inhibition at 1 mM
oxalate

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at pH 7.0
oxalate
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mixed-type non-competitive inhibition, increasing inhibitory effects as the number of carbons in aliphatic chains decreases
oxalate
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competitive inhibition
oxalate
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18% inhibition of glycolate oxidation, 71% inhibition of glyoxylate oxidation at 0.03 mM
oxalate
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34% inhibition at 5 mM, competitive
phosphate

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competitive
phosphate
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50% inhibition at 0.1 M
phosphate
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inhibition of glycolate-ferricyanide or glyoxylate-ferricyanide assay above 0.1 M
propionate

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mixed-type non-competitive inhibition
pyruvate

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competitive inhibition
pyruvate
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26% inhibition at 5 mM
succinate

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succinate
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mesophyll isoform
additional information

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development of selective inhibitors of Hao2 from screening of a compound library, overview
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additional information
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treatment with 4-[(4'-fluorobiphenyl-3-yl)methyl]-3-methyl-1H-pyrazole-5-carboxylic acid or 4-(1-benzothiophen-2-ylmethyl)-3-methyl-1H-pyrazole-5-carboxylic acid results in a significant reduction or attenuation of blood pressure in an established or developing model of hypertension, deoxycorticosterone acetate-treated rats
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additional information
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development of selective inhibitors of Hao2 from screening of a compound library, overview
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Adenocarcinoma
Cellular mechanism of resistance of human colorectal adenocarcinoma cells against apoptosis-induction by Russell's Viper venom l-amino acid oxidase (Rusvinoxidase).
Adenocarcinoma
In vitro cytotoxicity of L-amino acid oxidase from the venom of Crotalus mitchellii pyrrhus.
Adenocarcinoma
The toxin BjussuLAAO-II induces oxidative stress and DNA damage, upregulates the inflammatory cytokine genes TNF and IL6, and downregulates the apoptotic-related genes BAX, BCL2 and RELA in human Caco-2 cells.
Breast Neoplasms
Apoptosis induction in human breast cancer (MCF-7) cells by a novel venom L-amino acid oxidase (Rusvinoxidase) is independent of its enzymatic activity and is accompanied by caspase-7 activation and reactive oxygen species production.
Carcinoma
Electrochemical immunosensor based on chitosan-gold nanoparticle/carbon nanotube as a ?platform and lactate oxidase as a ?label for detection of CA125 oncomarker?.
Colonic Neoplasms
Cytotoxic, Anti-Proliferative and Apoptosis Activity of l-Amino Acid Oxidase from Malaysian Cryptelytrops purpureomaculatus (CP-LAAO) Venom on Human Colon Cancer Cells.
Colonic Neoplasms
Cytotoxic, Antiproliferative and Apoptosis-inducing Activity of L-Amino Acid Oxidase from Malaysian Calloselasma rhodostoma on Human Colon Cancer Cells.
Colorectal Neoplasms
Characterization and cytotoxicity of L-amino acid oxidase from the venom of king cobra (Ophiophagus hannah).
Edema, Cardiac
Aristolochic acid and its derivatives as inhibitors of snake venom L-amino acid oxidase.
Fibrosarcoma
Characterization and cytotoxicity of L-amino acid oxidase from the venom of king cobra (Ophiophagus hannah).
Glioma
L-amino acid oxidase (LOX) modulation of melphalan activity against intracranial glioma.
Hyperglycinemia, Nonketotic
A missense mutation (His42Arg) in the T-protein gene from a large Israeli-Arab kindred with nonketotic hyperglycinemia.
Hyperglycinemia, Nonketotic
A one-base deletion (183delC) and a missense mutation (D276H) in the T-protein gene from a Japanese family with nonketotic hyperglycinemia.
Hyperglycinemia, Nonketotic
Crystal structure of human T-protein of glycine cleavage system at 2.0 A resolution and its implication for understanding non-ketotic hyperglycinemia.
Hyperglycinemia, Nonketotic
Crystal structure of T-protein of the glycine cleavage system. Cofactor binding, insights into H-protein recognition, and molecular basis for understanding nonketotic hyperglycinemia.
Hyperglycinemia, Nonketotic
Identification of the mutations in the T-protein gene causing typical and atypical nonketotic hyperglycinemia.
Hyperglycinemia, Nonketotic
Molecular genetic and potential biochemical characteristics of patients with T-protein deficiency as a cause of glycine encephalopathy (NKH).
Hyperglycinemia, Nonketotic
Nonketotic hyperglycinemia: two patients with primary defects of P-protein and T-protein, respectively, in the glycine cleavage system.
Hyperglycinemia, Nonketotic
Recurrent mutations in P- and T-proteins of the glycine cleavage complex and a novel T-protein mutation (N145I): a strategy for the molecular investigation of patients with nonketotic hyperglycinemia (NKH).
Infection
l-amino acid oxidase expression profile and biochemical responses of rabbitfish (Siganus oramin) after exposure to a high dose of Cryptocaryon irritans.
Kidney Failure, Chronic
High resolution crystal structure of rat long chain hydroxy acid oxidase in complex with the inhibitor 4-carboxy-5-[(4-chlorophenyl)sulfanyl]-1, 2, 3-thiadiazole. Implications for inhibitor specificity and drug design.
Leukemia
Cytotoxic proteins of Amanita virosa Secr. mushroom: purification, characteristics and action towards mammalian cells.
Melanoma
Characterization and cytotoxicity of L-amino acid oxidase from the venom of king cobra (Ophiophagus hannah).
Neoplasms
Antiproliferative Activity of King Cobra (Ophiophagus hannah) Venom l-Amino Acid Oxidase.
Neoplasms
CR-LAAO, an L-amino acid oxidase from Calloselasma rhodostoma venom, as a potential tool for developing novel immunotherapeutic strategies against cancer.
Neoplasms
Isolation, characterization and screening of the in vitro cytotoxic activity of a novel L-amino acid oxidase (LAAOcdt) from Crotalus durissus terrificus venom on human cancer cell lines.
Neoplasms
King cobra (Ophiophagus hannah) venom L-amino acid oxidase induces apoptosis in PC-3 cells and suppresses PC-3 solid tumor growth in a tumor xenograft mouse model.
Neoplasms
l-Amino acid oxidase from Cerastes vipera snake venom: Isolation, characterization and biological effects on bacteria and tumor cell lines.
Neoplasms
l-Amino acid oxidase isolated from Calloselasma rhodostoma snake venom induces cytotoxicity and apoptosis in JAK2V617F-positive cell lines.
Neoplasms
Oxidoreductase activities in normal rat liver, tumor-bearing rat liver, and hepatoma HC-252.
Neoplasms
Targeting Tumor Microenvironment by Bioreduction-Activated Nanoparticles for Light-Triggered Virotherapy.
prephenate dehydrogenase deficiency
Molecular genetic and potential biochemical characteristics of patients with T-protein deficiency as a cause of glycine encephalopathy (NKH).
Pulmonary Edema
Aristolochic acid and its derivatives as inhibitors of snake venom L-amino acid oxidase.
Stomach Neoplasms
Characterization and cytotoxicity of L-amino acid oxidase from the venom of king cobra (Ophiophagus hannah).
Uterine Cervical Neoplasms
ACTX-8, a cytotoxic L-amino acid oxidase isolated from Agkistrodon acutus snake venom, induces apoptosis in Hela cervical cancer cells.
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