Ligand Phenylglyoxal

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Basic Ligand Information

Molecular Structure
Picture of Phenylglyoxal (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
C8H6O2
Phenylglyoxal
HEGSGKPQLMEBJL-RKQHYHRCSA-N
Synonyms:
alpha-deuteriophenylglyoxal, oxo(phenyl)acetaldehyde, Phenylglyoxan

Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (29 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
phenylglyoxal + NADPH = ?
show the reaction diagram
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phenylglyoxal + NADPH = ?
show the reaction diagram
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phenylglyoxal + NADPH = ?
show the reaction diagram
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phenylglyoxal + NADPH = ?
show the reaction diagram
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phenylglyoxal + NADPH = ? + NADP+
show the reaction diagram
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phenylglyoxal + NADPH = ? + NADP+
show the reaction diagram
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phenylglyoxal + NADPH = hydroxyphenylacetaldehyde + NADP+
show the reaction diagram
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phenylglyoxal + NADPH + H+ = ?
show the reaction diagram
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phenylglyoxal + NADPH = ?
show the reaction diagram
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phenylglyoxal + NADH = hydroxyphenylacetaldehyde + NAD+
show the reaction diagram
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phenylglyoxal + NADP+ + H2O = ?
show the reaction diagram
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phenylglyoxal + ferricyanide = oxo(phenyl) acetic acid + ferrocyanide + H+
show the reaction diagram
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phenylglyoxal + NADPH = ?
show the reaction diagram
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phenylglyoxal + H2O = ?
show the reaction diagram
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Product in Enzyme-catalyzed Reactions (2 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE

Activator in Enzyme-catalyzed Reactions (5 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
activation at pH 7
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1 mM, 46% inhibition
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Inhibitor in Enzyme-catalyzed Reactions (164 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
5.3 mM, 70% inhibition in borate buffer, 92% inhibition in NaHCO3 buffer within 10 min, complete inactivation after prolonged incubation with phenylglyoxal, NAD+ and D-pantoate increase half-inactivation time from 6 min without substrates to 40 and 17 min respectively
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in absence of NADPH
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pseudo-first-order loss of oxidative decarboxylase activity
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40 mM, pH 8.5, t1/2: 0.33 h
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2 equivalents per subunit are required for total inactivation, in presence of competitive inhibitors inactivation is markedly reduced
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NADPH protects against inactivation of aklavinone-11-hydroxylase by phenylglyoxal
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pseudo-first order kinetics, incorporation into the substrate-binding site
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25% activity remaining after 3 h for native and recombinant wild-type and recombinant mutant H30A, complete inactivation of recombinant mutant K179R after 7 min
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10 mM, biphasic kinetic, complete inactivation after 30 min
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47% residual activity at 1 mM with feruloyl-CoA as substrate
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concentration-dependent inhibition, complete inactivation at 50 mM
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at 3 mM pyridoxal 5'-phosphate glutamine-dependent glutamate synthase is inactivated by about 50% within 10 min. This inactivation is not prevented by 2-oxoglutarate
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4 mM, 75% inhibition, uncompetitive vs. 2-oxoglutarate, noncompetitive vs. NADH
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5 mM, 60% loss of activity
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pyridoxal 5'-phosphate protects
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total inactivation
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100 mM, 46% inhibition
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in 0.1 M phosphate, pH 7.3, 4 mM, inactivation after 15 min to 40% and to 20% after 60 min
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76fold excess, approx. 60% and 20% loss of ferredoxin dependent and methylviologen dependent activity after 2 h, respectively
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inhibition of the ferredoxin-linked activity and the methyl viologen-linked activity
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74% inhibition, inhibition increases with the alkanity of the preincubation medium, S-adenosyl-L-methionine protects against inhibition
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complete inactivation after 1 h incubation
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prevents reconstitution of apotransketolase
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concentration-dependent inhibition of liver enzyme with 65% inhibition at 5 mM
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inactivation, 50% protection by pyridoxal 5'-phosphate or CoA (glycine or threonine to some extent), kinetics
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at 10 mM, in bicarbonate buffer, pH 9.0
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33% inhibition after preincubation with phenylglyoxal
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12 mM, 50% inhibition
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92% of inhibition at 10 mM
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concentration and time-dependent
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10 mM, 90% inhibition
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irreversible, complete inactivation, alkylation of Arg155, GMP protects, no alkylation of mutant R155K
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inactivation
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N-acetylmannosamine or phosphoenolpyruvate protect
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80% loss of activity, inactivation of inhibition in the presence of geranylgeranyl diphosphate
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loss of activity with lysine, no effect on activity with L-alanine
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inhibition levels of wild-type and mutant enzymes, overview
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2.5 mM, 10% residual activity
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complete inactivation, reacts on arginine residues
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the enzyme loses 84.7% of its initial activity after incubation for 90 min with 0.0009 mM phenyllyoxal
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in the presence of 3-phosphoglycerate
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3 mM, irreversible inactivation of wild-type enzyme and mutant enzyme del396-573, t1/2: 5 min for both forms
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incomplete inactivation
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1.0 mM, complete irreversible inactivation after 30 min in bicarbonate buffer, pH 9.0, at 25°C
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Arg-343 and Arg-350 were found to be covalently modified; irreversible, substrates and 2,3-bisphosphoglycerate protect against inactivation
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97% residual activity in the presence of 5 mM phenylglyoxal, after 30 min at 30°C
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5 mM, complete inhibition
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3 mM, 27% inhibition
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1 mM, 20% inhibition
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preincubation with captopril protects enzyme from inactivation
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synergism with DTNB
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protection by substrate
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20 mM, 82% loss of activity, benzylpenicillin or phenylacetate protects
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57.4% residual activity
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55% inhibition at 1 mM, 98% inhibition at 10 mM
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6 mM: inhibition, inhibition partially removed by 35 mM phosphate
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inactivation follows pseudo-first-order kinetics
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phosphoenolpyruvate, ADP and Mn2+, alone or in combination protect against inactivation. Modification of only two of the three to four reactive arginine residues per enzyme subunit is responsible for inactivation
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inactivation
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inactivation, coincubation with substrate and metal-ion cofactor reduces the rate of inactivation by 10-fold
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50 mM, complete inactivation, dimethylally diphosphate and Mg2+ protect the isozyme partially
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protection by histidinol phosphate
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inhibition of Phe activation. Both ATP and Phe prevent the inactivation. ATP is competitive with phenylglyoxal, whereas Phe is not. A single arginine residue of GS 1 is essential for Phe activation in binding the phosphate moiety of ATP
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1 mM, 33% inhibition
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protection by substrates and competitive inhibitors
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cytosolic enzyme form
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inactivation by modification of arginine residues, ATP protects
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GTP or IMP partially protect
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pseudo-first order kinetics, inhibition is prevented either by MgADP- and MgATP2-
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Enzyme Kinetic Parameters

kcat Value (Turnover Number) (11 results)

EC NUMBER
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
COMMENTARY
LITERATURE
39.3
-
pH 7.0, 25°C
9.49
-
pH 7.5, 25°C
0.0272
-
pH and temperature not specified in the publication

KM Value (32 results)

EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
2.366
-
-
0.59
-
-
5.67
-
pH 7.5, 25°C
0.3
-
-
13
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pH and temperature not specified in the publication

Ki Value (4 results)

EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.002
0.0023
-
0.4
-
-

IC50 Value (3 results)

EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
4.5
-
29°C

References & Links

Links to other databases for Phenylglyoxal

ChEBI
PubChem
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PubChem