Ligand 2-oxoisovalerate

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Basic Ligand Information

Molecular Structure
Picture of 2-oxoisovalerate (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
C5H8O3
2-oxoisovalerate
QHKABHOOEWYVLI-UHFFFAOYSA-N
Synonyms:
2-ketoisopentanoate, 2-ketoisovalerate, 2-oxo-3-methylbutanoate, 2-oxo-3-methylbutanoic acid, 2-oxo-3-methylbutyric acid, 2-oxo-iso-valerate, 2-oxo-isopentanoate, 2-oxo-isovalerate, 2-oxoiso-valerate, 2-oxoisopentanoate, 2-oxoisopentanoic acid, 2-oxoisovaleric acid, 3,3-dimethyl-2-oxo-propionate, 3-methyl-2-ketobutyrate, 3-methyl-2-oxo-butanoate, 3-methyl-2-oxobutanoate, 3-methyl-2-oxobutanoic acid, 3-methyl-2-oxobutyrate, 3-methyl-2-oxobutyric acid, alpha-ketoisovaleric acid, ketovaline


Show all pahtways known for Show all BRENDA pathways known for 2-oxoisovalerate

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (17 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
PROVEN IN VIVO REACTION
ENZYME 3D STRUCTURE
show the reaction diagram
2-oxoisovalerate = isobutyraldehyde + CO2
-
show the reaction diagram
3-methyl-2-oxobutyrate + L-glutamate = L-valine + 2-oxoglutarate

In Vivo Product in Enzyme-catalyzed Reactions (13 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
PROVEN IN VIVO REACTION
ENZYME 3D STRUCTURE
show the reaction diagram
(R)-3,3-dimethylmalate + NAD+ = 3-methyl-2-oxobutanoate + CO2 + NADH
-
show the reaction diagram
DL-2-hydroxyisovalerate + O2 = 2-oxoisovalerate + H2O2
-
show the reaction diagram
L-valine + NAD(P)+ + H2O = 2-oxoisovalerate + NH3 + NAD(P)H
-

Substrate in Enzyme-catalyzed Reactions (135 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
REACTION
ENZYME 3D STRUCTURE
show the reaction diagram
2-ketoisopentanoate + NAD(P)H = 2-hydroxyisopentanoate + NAD(P)+
-
show the reaction diagram
2-oxoisovalerate + NADPH = 2-hydroxyvalerate + NADP+
-
show the reaction diagram
3-methyl-2-oxobutanoate + NADH = 2-hydroxy-3-methylbutanoate + NAD+
-
show the reaction diagram
2-oxoisovalerate + NADH + H+ = 2-hydroxyisovalerate + NAD+
-
show the reaction diagram
2-ketoisovalerate + NADPH + H+ = ?
-
show the reaction diagram
2-oxoisovalerate + CoA + NAD+ = isobutanoyl-CoA + CO2 + NADH
-
show the reaction diagram
3-methyl-2-oxobutanoate + CoA + NAD+ = 2-methylpropanoyl-CoA + CO2 + NADH
-
show the reaction diagram
2-oxoisovalerate + NAD+ + CoA-SH = ?
-
show the reaction diagram
2-oxoisovalerate + oxidized 2,6-dichlorophenolindophenol = 2-methylpropanal + CO2 + reduced 2,6-dichlorophenolindophenol
-
show the reaction diagram
3-methyl-2-oxobutanoate + H2O + oxidized methyl viologen = S-(2-methylpropanoyl)-CoA + reduced methyl viologen + H+
-
show the reaction diagram
2-oxo-3-methylbutanoate + NH3 + NADH = L-Val + NAD+ + H2O
-
show the reaction diagram
3-methyl-2-oxobutanoate + NH3 + NADPH + H+ = ?
-
show the reaction diagram
2-oxo-iso-valerate + NADPH + NH3 = L-leucine + NADP+ + H2O
-
show the reaction diagram
2-oxo-3-methylbutyric acid + NH3 + NADPH + H+ = D-valine + H2O + NADP+
-
show the reaction diagram
2-oxoisovalerate = isobutyraldehyde + CO2
-
show the reaction diagram
acetyl-CoA + 2-oxoisovalerate + H2O = ?
-
show the reaction diagram
2-oxoisovalerate + acetyl-CoA = isopropylmalate + CoA
-
show the reaction diagram
acetyl-CoA + H2O + 2-ketoisovalerate = ?
-
show the reaction diagram
L-alanine + 2-oxoisopentanoate = pyruvate + L-valine
-
show the reaction diagram
beta-alanine + 2-oxoisopentanoate = malonic semialdehyde + L-valine
-
show the reaction diagram
D-alanine + 2-oxoisovalerate = pyruvate + D-valine
-
show the reaction diagram
histidine + 2-oxoisovalerate = imidazol-5-yl-pyruvate + L-valine
-
show the reaction diagram
2-oxoisovalerate + L-glutamate = L-valine + 2-oxoglutarate
-
show the reaction diagram
L-glutamine + 2-oxoisovalerate = 2-oxoglutaramate + L-valine
-
show the reaction diagram
(R)-alpha-methylbenzylamine + 3-methyl-2-oxobutyrate = acetophenone + L-valine
-
show the reaction diagram
3-methyl-2-oxobutanoic acid = ?
-
show the reaction diagram
2-oxoisovalerate = ?
-
show the reaction diagram
2-Oxo-3-methylbutanoate + formaldehyde = 2-Dehydropantoate
-

Product in Enzyme-catalyzed Reactions (82 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
REACTION
ENZYME 3D STRUCTURE
-
show the reaction diagram
2-hydroxyisovalerate + NAD+ = 2-oxoisovalerate + NADH + H+
-
show the reaction diagram
(R)-3,3-dimethylmalate + NAD+ = 3-methyl-2-oxobutanoate + CO2 + NADH
-
-
show the reaction diagram
(R,S)-2-hydroxyisovalerate + acceptor = 2-oxo-isovalerate + reduced acceptor
-
-
show the reaction diagram
isobutyryl-CoA + CO2 + reduced benzyl viologen = 2-oxoisopentanoate + CoA + benzyl viologen
-
-
show the reaction diagram
D-valine + oxidized 2,6-dichloroindophenol + H2O = 2-oxoisopentanoate + NH3 + reduced 2,6-dichloroindophenol
-
-
show the reaction diagram
S-adenosyl-L-methionine + 2-oxobutyrate = S-adenosyl-L-homocysteine + 3-methyl-2-oxobutyrate
-
show the reaction diagram
pyruvate + L-valine = L-alanine + 3-methyl-2-oxobutanoate
-
-
show the reaction diagram
phenylpyruvate + DL-valine = phenylalanine + 3-methyl-2-oxobutanoate
-
show the reaction diagram
L-valine + (S)-3-methyl-2-oxopentanoate = 3-methyl-2-oxobutanoate + L-isoleucine
-
-
show the reaction diagram
L-valine + glyoxylate = 3-methyl-2-oxobutanoate + glycine
-
-
show the reaction diagram
valine + pyruvate = 3-methyl-2-oxobutanoate + alanine
-
show the reaction diagram
L-valine + alpha-ketomethiobutyrate = 3-methyl-2-oxo-butanoate + L-methionine
-
-
show the reaction diagram
valine + glyoxylate = 3-methyl-2-oxobutanoate + glycine
-
-
show the reaction diagram
D-valine + 2-oxoadipate = 3-methyl-2-oxobutanoate + 2-aminoadipate
-
-
show the reaction diagram
2-oxo-4-methylthiobutanoate + L-valine = L-methionine + 2-oxo-isovalerate
-
-
show the reaction diagram
L-valine + indole-3-pyruvic acid = 3-methyl-2-oxobutanoate + L-tryptophan
-
-
show the reaction diagram
L-valine + 2-oxoglutarate = 3-methyl-2-oxobutanoate + L-glutamate
-

Activator in Enzyme-catalyzed Reactions (3 results)

COMMENTARY
EC NUMBER
LITERATURE
ENZYME 3D STRUCTURE

Inhibitor in Enzyme-catalyzed Reactions (16 results)

COMMENTARY
EC NUMBER
LITERATURE
ENZYME 3D STRUCTURE
10 mM, 43.1% inhibition
-
0.01 M, 21% inhibition
-
non-competitive inhibition at 5 mM
-
2-oxoglutarate dehydrogenase complex
-
competitive
-
substrate inhibition
-
65 mM, 50% loss of specific activity
-
competitive
-
transamination between glutamine and glyoxylate
-
measured in the forward reaction, concentrations higher than 1.0 mM inhibits the enzyme
less effective than 2-oxoisohexanoate and 2-oxo-3-methylpentanoate
-

3D Structure of Enzyme-Ligand-Complex (PDB) (68 results)

EC NUMBER
ENZYME 3D STRUCTURE

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (112 results)

COMMENTARY
EC NUMBER
LITERATURE
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
30°C, pH 5.5, mutant enzyme Y52L
11.7
-
30°C, pH 5.5, wild-type enzyme
27
-
mutant Y51F, pH 5.5, 30°C
179
-
mutant Y51L, pH 5.5, 30°C
90.2
-
mutant Y51M, pH 5.5, 30°C
76.2
-
pH 7.0, 30°C, recombinant enzyme
120
-
wild-type, pH 5.5, 30°C
33.9
-
pH 8.0, 37°C
0.182
-
E1b component mutant S292Dalpha
0.58
-
E1b component mutant S292Nalpha
3.92
-
E1b component mutant S302Aalpha
2.18
-
hE1b-Tyr113Phe mutant
2.85
-
recombinant component E1b mutant D295Aalpha, pH 7.5, 22°C
0.485
-
recombinant component E1b mutant R287Aalpha, pH 7.5, 22°C
0.38
-
recombinant component E1b mutant R301Aalpha, pH 7.5, 22°C
0.41
-
recombinant component E1b mutant Y300Aalpha, pH 7.5, 22°C
0.36
-
recombinant component E1b mutant Y300Falpha, pH 7.5, 22°C
0.57
-
recombinant E1b component mutant H291Aalpha, pH 7.5, 22°C
0.58
-
recombinant E1b component mutant H291Nalpha, pH 7.5, 22°C
0.67
-
recombinant E1b component mutant H291Qalpha, pH 7.5, 22°C
0.49
-
recombinant wild-type component E1b, pH 7.5, 22°C
0.195
-
recombinant wild-type E1b component, pH 7.5, 22°C
8.65
-
wild type enzyme
9.4
-
wild-type
0.1983
-
wild-type E1b component
3.3
-
pH 6.9, 85°C, under argon
pH 9.5, 21°C
226
-
K79A mutant
7.22
-
K91A mutant
13
-
L104V mutant
0.03
-
L81A mutant
0.018
-
Y144L mutant
0.023
-
Y144V mutant
0.062
-
alpha-IPMS-14CR
0.52
-
alpha-IPMS-2CR
1.17
-
at pH 7.8 and 37°C
330
-
full-length enzyme, in 50 mM HEPES (pH 7.5), at 25°C
isoform IPMS1, pH and temperature not specified in the publication
1.08
-
isoform IPMS3, pH and temperature not specified in the publication
0.49
-
isoform Leu4, at pH 7.5 and 30°C
13.79
-
isoform Leu9, at pH 7.5 and 30°C
7.28
-
mutant enzyme D444A, at pH 7.5 and 25°C
3.1
-
mutant enzyme D444R, at pH 7.5 and 25°C
5.7
-
mutant enzyme D444Y, at pH 7.5 and 25°C
3.4
-
mutant enzyme R97A, at pH 7.5 and 25°C
7
-
pH 7.4, 25°C
3.5
-
pH 7.4, 25°C, presence of Co2+
0.77
-
pH 7.4, 25°C, presence of K+
3.2
-
pH 7.4, 25°C, presence of Mg2+
3.5
-
pH 7.4, 25°C, presence of Mn2+
1.69
-
pH 7.4, 25°C, presence of Rb+
2.9
-
pH 7.8, 37°C
330
-
pH 7.8, 55°C
450
-
pH 8.0, 50°C
1.2
-
pH 8.0, isoform IPMS1
2.4
-
pH 8.0, isoform IPMS2
2.3
-
wild type enzyme, at pH 7.5 and 25°C
3.7
-
at pH 8.0 and 32°C
0.18
-
pH 7.5, 45°C
2.1
-
half transamination reaction, pH 8.0, 90°C
270
-
pH 8.0, 25°C
0.2
-
pH 8.0, 37°C
pH not specified in the publication, 25°C
SlBCAT1, pH not specified in the publication, 25°C
23
-
SlBCAT2, pH not specified in the publication, 25°C
84.3
-
SlBCAT3, pH not specified in the publication, 25°C
46.5
-
SlBCAT4, pH not specified in the publication, 25°C
60.6
-
SlBCAT5, pH not specified in the publication, 25°C
22.1
-
SlBCAT6, pH not specified in the publication, 25°C
109.8
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
0.92
-
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
19
-
mutant enzyme T377L/A460Y, at pH 6.0 and 30°C
12
-
-
28.35
-
mutant A290M/Q252N/D306G/E316R/F388Y/L434C, pH 6.5, 30°C
95
-
mutant D295A, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction
0.48
-
mutant D295A, pH 7.5, 30°C, overall reaction
0.48
-
mutant Q487A, pH 7.0, 37°C
1.1
-
mutant Q487G, pH 7.0, 37°C
0.8
-
mutant Q487I, pH 7.0, 37°C
4.8
-
mutant Q487L, pH 7.0, 37°C
5.4
-
mutant Q487S, pH 7.0, 37°C
0.8
-
mutant R301A, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction
0.41
-
mutant R301A, pH 7.5, 30°C, overall reaction
0.41
-
mutant V461I, pH 6.5, 30°C
120
-
mutant V461I/A290M, pH 6.5, 30°C
118
-
mutant V461I/A290M/Q252N/D306G/E316R/F388Y, pH 6.5, 30°C
149
-
mutant V461I/A290M/Q252N/D306G/E316R/F388Y/I404C, pH 6.5, 30°C
5.2
-
mutant V461I/A290M/Q252N/D306G/E316R/F388Y/L434C/M290C, pH 6.5, 30°C
69
-
mutant V461I/A290M/Q252N/D306G/E316R/F388Y/L434C/M290V, pH 6.5, 30°C
43
-
mutant Y300A, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction
0.38
-
mutant Y300A, pH 7.5, 30°C, overall reaction
0.38
-
mutant Y300F, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction
0.57
-
mutant Y300F, pH 7.5, 30°C, overall reaction
0.57
-
pH 7.0, 55°C
0.3
-
pH and temperature not specified in the publication
wild-type, pH 6.5, 30°C
145
-
wild-type, pH 7.0, 37°C
8.9
-
wild-type, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction
0.19
-
wild-type, pH 7.5, 30°C, overall reaction
0.19
-

KM Value (175 results)

COMMENTARY
EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
LITERATURE
pH 7.5, 25°C, recombinant enzyme
8.7
-
30°C, pH 5.5, mutant enzyme Y52L
18.6
-
30°C, pH 5.5, wild-type enzyme
5.5
-
mutant Y51F, pH 5.5, 30°C
7.7
-
mutant Y51L, pH 5.5, 30°C
12
-
mutant Y51M, pH 5.5, 30°C
8.6
-
pH 7.0, 30°C, recombinant enzyme
3.5
-
wild-type, pH 5.5, 30°C
38
-
pH 7.0, 30°C
0.065
-
at pH 7.0 and 37°C
0.29
-
in 100 mM Tris-HC1 buffer, pH 8.0, at 30°C
46
-
pH 7.0, 37°C
0.29
-
pH 7.5, 30°C
0.18
-
pH 7.5, 30°C, D-mandelate dehydrogenase D-ManDH2
0.15
-
pH 8.0, 37°C, wild-type enzyme
6.91
-
pH 7.0, 30°C
1.27
-
E1b component mutant S292Dalpha
4.38
-
E1b component mutant S292Nalpha
0.193
-
E1b component mutant S302Aalpha
0.028
-
mutant enzyme G290A and S298A
0.059
-
mutant enzyme I289A and H291A
0.062
-
mutant enzyme S293A
0.568
-
mutant enzyme S295A
0.064
-
mutant enzyme T294A
0.058
-
recombinant component E1b mutant R287Aalpha, pH 7.5, 22°C
2.33
-
recombinant component E1b mutant R301Aalpha, pH 7.5, 22°C
0.23
-
recombinant component E1b mutant Y300Aalpha, pH 7.5, 22°C
0.34
-
recombinant component E1b mutant Y300Falpha, pH 7.5, 22°C
0.25
-
recombinant E1b component mutant H291Aalpha, pH 7.5, 22°C
0.206
-
recombinant E1b component mutant H291Nalpha, pH 7.5, 22°C
0.118
-
recombinant E1b component mutant H291Qalpha, pH 7.5, 22°C
0.203
-
recombinant wild-type component E1b, and mutant D295Aalpha, pH 7.5, 22°C
0.05
-
recombinant wild-type E1b component, pH 7.5, 22°C
0.059
-
wild type enzyme
0.119
-
wild-type E1b component
0.048
-
wild-type enzyme and mutant enzyme D297A
0.056
-
-
0.17
-
pH 6.9, 85°C, under argon
pH 8.0, 65°C, anaerobic
1.3
-
pH 10.4, 30°C
pH 10.4, temperature not specified in the publication
0.46
-
pH 8.8, 30°C
0.8
-
pH 9.5, 21°C
0.81
-
K79A mutant
50
-
K91A mutant
4.5
-
shoots
0.538
-
L104V mutant
0.253
-
L81A mutant
0.098
-
Y144L mutant
0.151
-
Y144V mutant
52.85
-
alpha-IPMS-14CR
0.035
-
alpha-IPMS-2CR
0.261
-
apparent value, full-length enzyme, in 50 mM HEPES (pH 7.5), at 25°C
at pH 7.8 and 37°C
0.09
-
isoform IPMS1, pH and temperature not specified in the publication
0.143
-
isoform IPMS3, pH and temperature not specified in the publication
0.215
-
mutant enzyme D444A, at pH 7.5 and 25°C
0.005
-
mutant enzyme D444R, at pH 7.5 and 25°C
0.009
-
mutant enzyme D444Y, at pH 7.5 and 25°C
0.016
-
mutant enzyme R97A, at pH 7.5 and 25°C
0.008
-
pH 7.4, 25°C
0.012
-
pH 7.4, 25°C, presence of Co2+
0.0022
-
pH 7.4, 25°C, presence of K+
0.016
-
pH 7.4, 25°C, presence of Mg2+
0.012
-
pH 7.4, 25°C, presence of Mn2+
0.0017
-
pH 7.4, 25°C, presence of Rb+
0.019
-
pH 7.8, 37°C
0.09
-
pH 8.0, 50°C
0.054
-
pH 8.0, isoform IPMS1
0.304
-
pH 8.0, isoform IPMS2
0.279
-
wild type enzyme, at pH 7.5 and 25°C
0.015
-
with acetyl-CoA as cosubstrate
0.06
-
at pH 8.0 and 32°C
1
-
pH 8.5, 50°C, K35A mutant enzyme
32.2
-
pH 8.5, 50°C, V33A mutant enzyme
15.5
-
pH 8.5, 50°C, wild-type enzyme
28
-
with L-tryptophan, pH 8.0, 30°C
0.11
-
pH 7.5, 45°C
0.0133
-
half transamination reaction, pH 8.0, 90°C
0.18
-
pH 7.5, 25°C
0.34
-
pH 8.0, 25°C, substrate L-isoleucine
0.61
-
pH 8.0, 37°C
pH 8.3, 25°C
0.11
-
pH 8.3, 337°C
2.69
-
pH 8.3, 37°C, leucine as amino group donor
0.37
-
pH 8.4, 30°C
0.4
-
pH not specified in the publication, 25°C
SlBCAT1, pH not specified in the publication, 25°C
5.57
-
SlBCAT2, pH not specified in the publication, 25°C
5.5
-
SlBCAT3, pH not specified in the publication, 25°C
0.65
-
SlBCAT4, pH not specified in the publication, 25°C
0.37
-
SlBCAT5, pH not specified in the publication, 25°C
1.2
-
SlBCAT6, pH not specified in the publication, 25°C
0.15
-
in 100 mM potassium phosphate buffer (pH 7.4), at 37°C
-
1.27
-
pH 6.5, 37°C
1.9
-
pH 7.0, 30°C
7.73
-
wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C
8.5
-
mutant enzyme T377L/A460Y, at pH 6.0 and 30°C
0.77
-
Hill coefficient 0.9, pH 7.0, 30°C
8.31
-
in 50 mM potassium phosphate buffer, pH 6.8 in the presence of 2.5 mM MgSO4 and 0.1 mM thiamine diphosphate
5.02
-
mutant A290M/Q252N/D306G/E316R/F388Y/L434C, pH 6.5, 30°C
8.6
-
mutant D295A, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction
0.05
-
mutant D295A, pH 7.5, 30°C, overall reaction
0.05
-
mutant Q487A, pH 7.0, 37°C
186
-
mutant Q487G, pH 7.0, 37°C
175
-
mutant Q487I, pH 7.0, 37°C
323
-
mutant Q487L, pH 7.0, 37°C
342
-
mutant Q487S, pH 7.0, 37°C
154
-
mutant R301A, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction
0.225
-
mutant R301A, pH 7.5, 30°C, overall reaction
0.255
-
mutant V461I, pH 6.5, 30°C
5.6
-
mutant V461I/A290M, pH 6.5, 30°C
9.3
-
mutant V461I/A290M/Q252N/D306G/E316R/F388Y, pH 6.5, 30°C
14.6
-
mutant V461I/A290M/Q252N/D306G/E316R/F388Y/I404C, pH 6.5, 30°C
2.6
-
mutant V461I/A290M/Q252N/D306G/E316R/F388Y/L434C/M290C, pH 6.5, 30°C
5.2
-
mutant V461I/A290M/Q252N/D306G/E316R/F388Y/L434C/M290V, pH 6.5, 30°C
6.6
-
mutant Y300A, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction
0.337
-
mutant Y300A, pH 7.5, 30°C, overall reaction
0.14
-
mutant Y300F, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction
0.252
-
mutant Y300F, pH 7.5, 30°C, overall reaction
0.39
-
pH 6.5, 37°C
1.9
-
pH 7.0, 55°C
0.027
-
wild-type, pH 6.5, 30°C
5.1
-
wild-type, pH 7.0, 37°C
300
-
wild-type, pH 7.5, 30°C, E1b-catalyzed decarboxylation reaction
0.05
-
wild-type, pH 7.5, 30°C, overall reaction
0.05
-

References & Links

Links to other databases for 2-oxoisovalerate

ChEBI
PubChem
-
PubChem