Ligand L-valine

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Basic Ligand Information

Molecular Structure
Picture of L-valine (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
C5H11NO2
L-valine
KZSNJWFQEVHDMF-BYPYZUCNSA-N
Synonyms:
(2S)-2-amino-3-methylbutanoic acid, L-Val, L-valine[side 2], Val, valine


Show all pahtways known for Show all BRENDA pathways known for L-valine

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (14 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
PROVEN IN VIVO REACTION
ENZYME 3D STRUCTURE
show the reaction diagram
L-valine + O2 = ? + H2O2
-
show the reaction diagram
L-valine + O2 + NADPH + H+ = (Z)-2-methylpropanal oxime + NADP+ + CO2 + H2O
-
show the reaction diagram
L-valine + NAD(P)+ + H2O = 2-oxoisovalerate + NH3 + NAD(P)H
-
show the reaction diagram
ATP + L-valine + tRNAMetG34C36 = AMP + diphosphate + L-valyl-tRNAMetG34C36
-
show the reaction diagram
ATP + L-valine + tRNAVal = AMP + diphosphate + L-valyl-tRNAVal
-

In Vivo Product in Enzyme-catalyzed Reactions (5 results)

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

Substrate in Enzyme-catalyzed Reactions (137 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
REACTION
ENZYME 3D STRUCTURE
show the reaction diagram
L-valine + O2 = ? + H2O2
-
show the reaction diagram
L-valine + 2-oxoglutarate + O2 = 4-hydroxy-L-valine + succinate + CO2
-
show the reaction diagram
L-valine + 2 [reduced NADPH-hemoprotein reductase] + 2 O2 = (E)-2-methylpropanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
-
show the reaction diagram
valine + H2O + NADP+ = 2-oxovalerate + NH3 + NADPH
-
show the reaction diagram
L-Val + pyruvate + NADH = ?
-
show the reaction diagram
Val + pyruvate + NADH = ?
-
show the reaction diagram
L-Val + pyruvate + NADH = N-[1-(R)-(Carboxy)ethyl]-(S)-Val + NAD+
-
show the reaction diagram
L-valine + 2,6-dichlorophenolindophenol + H2O = ? + reduced 2,6-dichlorophenolindophenol
-
show the reaction diagram
acetyl-CoA + L-valine = CoA + N-acetyl-L-valine
-
show the reaction diagram
pyruvate + L-valine = L-alanine + 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
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
-
show the reaction diagram
L-valine = i-butylamine + CO2
-
show the reaction diagram
L-Val = 2-Methylpropylamine + CO2
-
show the reaction diagram
L-valine = 2-methylpropanamine + CO2
-
show the reaction diagram
L-valine = D-valine
-
show the reaction diagram
ATP + L-valine + tRNAMetG34C36 = AMP + diphosphate + L-valyl-tRNAMetG34C36
-
show the reaction diagram
ATP + L-valine + tRNAIle = AMP + diphosphate + L-valyl-tRNAIle
-
show the reaction diagram
ATP + L-valine + [CmaA-protein-T-domain]-4'-phosphopantetheine = AMP + diphosphate + S-L-valyl-[CmaA-protein-T-domain]-4'-phosphopantetheine
-
show the reaction diagram
ATP + L-Glu + L-valine = ADP + phosphate + gamma-L-Glu-L-valine
-
show the reaction diagram
ATP + (-)-jasmonate + L-Val = AMP + diphosphate + jasmonoyl-L-Val
-
show the reaction diagram
ATP + UDP-N-acetylmuramate + L-Val = ADP + phosphate + UDP-N-acetylmuramoyl-L-Val
-
show the reaction diagram
ATP + H2O + L-valine/out = ADP + phosphate + L-valine/in
-

Product in Enzyme-catalyzed Reactions (173 results)

EC NUMBER
LITERATURE
REACTION DIAGRAM
REACTION
ENZYME 3D STRUCTURE
-
show the reaction diagram
2-oxovalerate + NH3 + NADH + H+ = L-valine + H2O + NAD+
-
-
show the reaction diagram
2-oxovalerate + NH3 + NADPH + H+ = L-valine + H2O + NADP+
-
show the reaction diagram
N-methyl-L-valine + acceptor + H2O = L-valine + formaldehyde + reduced acceptor
-
-
show the reaction diagram
5-L-glutamyl-L-Val + Gly-Gly = L-Val + 5-L-glutamyl-Gly-Gly
-
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
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
(R)-alpha-methylbenzylamine + 3-methyl-2-oxobutyrate = acetophenone + L-valine
-
show the reaction diagram
Val-Gly-Gly + H2O = Val + Gly-Gly
-
show the reaction diagram
Arg-Val + H2O = Arg + Val
-
show the reaction diagram
Val-Trp + H2O = Val + Trp
-
-
show the reaction diagram
Met-Val + H2O = Met + Val
-
-
show the reaction diagram
L-Val-p-nitroanilide + H2O = L-Val + p-nitroaniline
-
show the reaction diagram
Val-Leu + H2O = Val + Leu
-
-
show the reaction diagram
Val-4-nitroanilide + H2O = L-valine + p-nitroaniline
-
-
show the reaction diagram
L-Val-7-amido-4-methylcoumarin + H2O = L-Val + 7-amino-4-methylcoumarin
-
-
show the reaction diagram
L-Val-7-amido-4-methylcoumarin + H2O = L-Val + 7-amino-4-methylcoumarin
-
-
show the reaction diagram
Met-Val + H2O = Met + Val
-
-
show the reaction diagram
L-Asp-L-Val + H2O = L-Asp + L-Val
-
-
show the reaction diagram
L-Val-L-Lys + H2O = L-valine + L-lysine
-
-
show the reaction diagram
His-Pro-Val + H2O = His-Pro + Val
-
-
show the reaction diagram
N-benzyloxycarbonyl-Pro-Val + H2O = N-benzyloxycarbonyl-Pro + Val
-
-
show the reaction diagram
Carbobenzoxy-Gly-Val + H2O = Carbobenzoxy-Gly + Val
-
-
show the reaction diagram
2-aminobenzoyl-Phe-Arg-Val + H2O = 2-aminobenzoyl-Phe-Arg + Val
-
-
show the reaction diagram
pyroglutamyl-Val + H2O = pyroglutamate + Val
-
show the reaction diagram
beta-Asp-Val + H2O = Asp + Val
-
show the reaction diagram
N-Formyl-Met-Val + H2O = N-Formyl-Met + Val
-
-
show the reaction diagram
alpha-melanocyte-stimulating hormone + H2O = acetyl-SYSMEHFRWGKP + L-Val
-
-
show the reaction diagram
GRGVVVGRG + H2O = GRGV + Val + Val + GRG
-
-
show the reaction diagram
Benzyloxycarbonyl-Gly-Val + H2O = Benzyloxycarbonyl-Gly + Val
-
-
show the reaction diagram
PFU-093 + H2O = FITC(Ahx)-L-Val + L-Val + L-Lys-Dbc
-
-
show the reaction diagram
jasmonoyl-L-valine + H2O = jasmonic acid + L-valine
-
-
show the reaction diagram
L-valineamide + H2O = L-valine + NH3
-
show the reaction diagram
L-valinamide + H2O = L-valine + NH3
-
-
show the reaction diagram
N-Benzoyl-Val + H2O = Benzoate + Val
-
show the reaction diagram
DL-alpha-aminoisovaleronitrile + H2O = L-valine + NH3
-
show the reaction diagram
5-L-glutamyl-L-valine = 5-oxoproline + L-valine
-
-
show the reaction diagram
D-valine = L-Val
-

Activator in Enzyme-catalyzed Reactions (22 results)

COMMENTARY
EC NUMBER
LITERATURE
ENZYME 3D STRUCTURE

Inhibitor in Enzyme-catalyzed Reactions (85 results)

COMMENTARY
EC NUMBER
LITERATURE
ENZYME 3D STRUCTURE
no inhibition
-
less than 45% inhibition
-
10 mM, 23% inhibition
-
substrate inhibition, noncompetitive
-
10 mM, about 50% loss of specific activity
-
substrate inhibition at higher concentrations than 20 mM
-
VDH2: 20 mM instead of 10 mM in reaction mixture caused 22% loss of activity, 50 mM 40% loss of activity
-
6% inhibition at 6.67 mM
-
5 mM, 23% inhibition
-
feedback inhibition, reversible by MgATP2-
-
enzyme form AHS I is inhibited. Enzyme form AHS II is not inhibited
-
isoenzyme I is more resistant to inhibition than isoenzyme III
-
isoenzyme I and III inhibited
-
binding site structure, inhibition mechanism
-
isoenzyme AHS I is sensitive to feed-back inhibition, isoenzyme AHS II is insensitive
-
competitive
-
inhibits to a maximal activity of approximately 50% at concentrations higher than 0.5 mM
-
inhibition of the enzyme from Arabidopsis thaliana, no inhibition of the enzyme expressed in E. coli
-
feedback inhibition; feedback inhibition; feedback inhibition
-
feedback inhibition of wild-type enzyme about 50% at 10 mM, M8 and M13 mutants are resistant
-
feedback inhibition
-
feedback inhibition, the inhibition by valine is uniquely in fungi reversed by MgATP
-
competitive; feed-back inhibition
-
cooperative effective with Leu
-
feed-back inhibition; noncompetitive
-
feed-back inhibition
-
5 mM, 89% inhibition; feed-back inhibition; noncompetitive
-
two enzyme forms: one is very sensitive to inhibition by Val, the second is not subject to feedback inhibition
-
not inhibitory for catalytic subunit alone, inhibitory for catalytic subunit plus small subunit
-
noncompetitive; pH-dependent inhibition
-
no inhibition
-
0.1 mM, 50% inhibition
-
1 mM, about 70%% residual activity in sulfonylurea-susceptible and 80% in sulfonylurea-resistant biotype
-
isozyme AHAS I, feedback inhibition
-
isozyme AHAS I, cooperative feedback inhibition
-
isoenzymes I and II are inhibited, isoenzyme II is not inhibited
-
50% inhibition at 20 mM, crude enzyme preparation
-
10 mM, at pH 6.5
-
fully reversed by addition of pyridoxal phosphate, 35% inhibition at 10 mM after 20 min
-
competitive with L-ornithine
-
competitive with L-ornithine; inhibitory action largely depends on the branched structure of the hydrophobic residue
-
33% inhibition at 50 mM
-
with 1 mM tyrosine as the substrate, 10 mM valine inhibits activity by 78%
-
competitive inhibition of enzyme activity with leucine
-
growing this microorganism in the presence of valine diminishes transaminase C activity but does not repress avtA
-
competitive inhibitor
-
16 mM, 86% inhibition
-
fructose 1,6-diphosphate protects
-
allosteric inhibition
-
branched chain alpha-amino acids bind at the active site, competitive inhibition mechanism against substrates phosphocreatine and ADP, inhibition kinetics
-
23.7% residual activity at 5 mM
-
strong inhibition of prolinase activity against Pro-Gly regardless wether MnCl2 is present or not
-
inhibitory to enzyme isoform prolidase I, activating isoform prolidase II
-
slight inhibition at 20 mM
-
competitive inhibitor
-
weak, liver enzyme
-
slight inhibition
-
competitive
-
weak
-
less effective inhibitor, Ki-value above 150 mM
-
inhibition of biosynthetic and transferase activity
-
-
-
uncompetitive
-
competitive to L-citrulline
-
13% cell growth, 10% viability of cells
-
77% residual activity at 5 mM with L-methionine as substrate, 81% residual activity at 50 mM with D-methionine as substrate
-

Metals and Ions (1 result)

COMMENTARY
EC NUMBER
LITERATURE
ENZYME 3D STRUCTURE
about 430% activity at 1 mM
-

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (57 results)

COMMENTARY
EC NUMBER
LITERATURE
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
pH 7.5, 28°C
pH 7.9, 30°C
28°C, pH 7.5
25°C, pH 10.4
0.91
-
pH 10.0, 21°C
28.3
-
in 100 mM glycine-KCl-KOH buffer (pH 10.4)
4.95
-
-
28.3
-
K91A mutant
0.0252
-
K79A mutant
0.000483
-
-
47.5
-
A124G mutant
5.7
-
-
5.08
-
pH not specified in the publication, 25°C
28.1
-
pH 10.0, 40°C
0.29
-
wild type enzyme, in 25 mM potassium phosphate buffer at pH 7.8, at 37°C
1236
-
wild type enzyme
277
-
pH 8.0, 25°C
19
-
pH 8.0, 65°C
2.1
-
SlBCAT4, pH not specified in the publication, 25°C
20.6
-
pH not specified in the publication, 25°C
39.1
-
SlBCAT1, pH not specified in the publication, 25°C
50.5
-
SlBCAT2, pH not specified in the publication, 25°C
3.8
-
SpBCAT1, pH not specified in the publication, 25°C
55
-
SlBCAT6, pH not specified in the publication, 25°C
24
-
SlBCAT5, pH not specified in the publication, 25°C
123
-
SlBCAT3, pH not specified in the publication, 25°C
111
-
mutant enzyme C338S, in 25 mM potassium phosphate buffer at pH 7.8, at 37°C
597
-
half transamination reaction, pH 8.0, 90°C
31
-
mutant enzyme C221S, in 25 mM potassium phosphate buffer at pH 7.8, at 37°C
443
-
mutant enzyme C235S, in 25 mM potassium phosphate buffer at pH 7.8, at 37°C
838
-
mutant enzyme C242S, in 25 mM potassium phosphate buffer at pH 7.8, at 37°C
688
-
mutant enzyme C293S, in 25 mM potassium phosphate buffer at pH 7.8, at 37°C
1111
-
mutant enzyme C315A
188
-
mutant enzyme C315A/C318A
197
-
mutant enzyme C318A
230
-
mutant enzyme C335S, in 25 mM potassium phosphate buffer at pH 7.8, at 37°C
170
-
mutant enzyme C335S/C338S, in 25 mM potassium phosphate buffer at pH 7.8, at 37°C
292
-
pH 7.5, 37°C, recombinant enzyme
0.214
-
with mutant tRNAVal with 3'-terminal purine riboside base analogue, pH 7.5, 37°C
14.4
-
with wild-type tRNAVal, pH 7.5, 37°C
13.9
-
with mutant tRNAVal with 3'-terminal isoguanosine base analogue, pH 7.5, 37°C
with mutant tRNAVal with 3'-terminal inosine base analogue, pH 7.5, 37°C
with mutant tRNAVal with 3'-terminal 2-aminopurine base analogue, pH 7.5, 37°C
-
2.9
-
aminoacylation reaction, His-tagged K277A mutant enzyme, pH 7.5, 25°C
0.064
-
aminoacylation reaction, His-tagged wild-type enzyme, pH 7.5, 25°C
1.5
-
at pH and °C
0.074
-
enzyme expressed in E. coli
5.65
-
pH 7.5, 25°C, the assay measures the release of diphosphate by means of a coupled enzyme system in which diphosphate drives the reduction of NAD+ to NADH
0.023
-
-
21.7
-
pH 8.0, 22°C
0.135
-

KM Value (117 results)

COMMENTARY
EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
LITERATURE
pH 7.5, 28°C
pH 7.9, 30°C
2.2
-
28°C, pH 7.5
25°C, pH 10.4
2
-
-
2.5
-
pH 10.0, 21°C
1.3
-
pH 10.4, 30°C
pH 10.4, temperature not specified in the publication
0.75
-
pH 10.6, 30°C
1
-
-
25
-
in 100 mM glycine-KCl-KOH buffer (pH 10.4)
0.044
-
A124G mutant
55.06
-
K79A mutant
714
-
K91A mutant
2.08
-
pH 10.5, mutant enzyme C251S
1.6
-
pH 10.5, mutant enzyme C30S
0.8
-
pH 10.5, mutant enzyme V305L
100
-
pH 10.5, wild-type enzyme
1.686
-
shoots
1.1
-
mutant enzyme LeuDEL4
25
-
native enzyme
3.8
-
pH 9.5, 30°C, in presence of 4 M NaCL
0.71
-
-
0.27
-
pH 7.5, 0.9% NaCl, at 25°C
13.92
-
pH 7.6, 30°C
3.73
-
pyruvate and NADH as cosubstrates
3
-
with phenylpyruvate, pH 8.0, 30°C
4.5
-
-
0.29
-
cosubstrate 2-oxoglutarate, pH 7.4, 37°C
5.79
-
cosubstrate 4-methylthio-2-oxo-butanoate, pH 7.4, 37°C
1.77
-
half transamination reaction, pH 8.0, 90°C
0.83
-
mitochondria of AS-30D cell, pH 7.8, 37°C
2.1
-
pH 10.0, 40°C
6.5
-
pH 8.0, 25°C
2.7
-
pH 8.0, 37°C
pH 8.0, 37°C, 2-oxoglutarate as amino group acceptor
pH 8.0, 37°C, isoenzyme I, 2-oxoglutarate as amino group acceptor
pH 8.0, 37°C, isoenzyme III, 2-oxoglutarate as amino group acceptor
pH 8.0, 65°C
1.17
-
pH 8.2, 37°C
4.3
-
pH 8.3, 337°C
4.41
-
pH 8.4, 25°C, 2-oxoglutarate as amino group acceptor
2.96
-
pH 8.6, 25°C
11
-
pH and temperature not specified in the publication
2.8
-
pH not specified in the publication, 25°C
pH8.2, 37°C, brain enzyme
1.4
-
SlBCAT1, pH not specified in the publication, 25°C
1
-
SlBCAT2, pH not specified in the publication, 25°C
1.4
-
SlBCAT3, pH not specified in the publication, 25°C
2
-
SlBCAT4, pH not specified in the publication, 25°C
1.4
-
SlBCAT5, pH not specified in the publication, 25°C
2.6
-
SlBCAT6, pH not specified in the publication, 25°C
1.2
-
SpBCAT1, pH not specified in the publication, 25°C
1.32
-
apparent Km value, at pH 7.4, 37°C
1.77
-
-
1100
-
pH 7.5, 37°C, recombinant enzyme
5.77
-
pH 7.0, 80°C
3.41
-
pH 7.0, 80°C, recombinant enzyme
3.41
-
aminoacylation reaction, His-tagged K277A mutant enzyme, pH 7.5, 25°C
0.0019
-
aminoacylation reaction, His-tagged wild-type enzyme, pH 7.5, 25°C
0.047
-
ATP, cytoplasmic enzyme
0.05
-
ATP-diphosphate exchange reaction, His-tagged K277A mutant enzyme, pH 7.5, 25°C
0.072
-
ATP-diphosphate exchange reaction, His-tagged wild-type enzyme, pH 7.5, 25°C
0.07
-
ATP-diphosphate exchange reaction, native wild-type enzyme, pH 7.5, 25°C
0.062
-
chloroplastic enzyme
0.015
-
cytoplasmic enzyme
0.05
-
enzyme expressed on E. coli
0.023
-
in 100 mM HEPES (pH 7.2), 20 mM KCl, 30 mM MgCl2, at 30°C
0.1926
-
monomeric enzyme form
0.0082
-
pH 7.5, 37°C
0.0395
-
tetrameric enzyme form
0.01
-
tRNA
0.001
-
with mutant tRNAVal with 3'-terminal 2-aminopurine base analogue, pH 7.5, 37°C
0.005
-
with mutant tRNAVal with 3'-terminal inosine base analogue, pH 7.5, 37°C
0.0048
-
with mutant tRNAVal with 3'-terminal isoguanosine base analogue, pH 7.5, 37°C
0.002
-
with mutant tRNAVal with 3'-terminal purine riboside base analogue, pH 7.5, 37°C
0.0088
-
with wild-type tRNAVal, pH 7.5, 37°C
0.0043
-
pH 7.5, 25°C, the assay measures the release of diphosphate by means of a coupled enzyme system in which diphosphate drives the reduction of NAD+ to NADH
1.2
-
pH 8.0, 22°C
0.26
-
at pH 8.6 and 25°C
2.49
-
-
70
-
pH 8.0, 22°C
0.26
-

Ki Value (29 results)

COMMENTARY
EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
LITERATURE
-
36.8
-
at pH 7.0
140
-
pH 7.0, 30°C, mutant K218A
0.006
-
pH 7.5, 37°C
0.105
-
pH 7.0, 37°C, holoenzyme
16.3
-
pH 7.0, 30°C, wild-type enzyme
0.177
-
pH 7.0, 30°C, mutant S212A
0.0156
-
pH 7.0, 30°C, mutant R216A
0.0245
-
pH 7.0, 30°C, mutant P206A
0.039
-
pH 7.0, 30°C, mutant L222A
0.003
-
pH 7.0, 30°C, mutant L177A
0.0162
-
pH 7.0, 30°C, mutant H205A
0.02
-
pH 7.0, 30°C, mutant H181A
0.058
-
pH 7.0, 30°C, mutant F204A
0.026
-
holoenzyme, pH 8.0, 60°C
0.018
-
catalytic subunit plus small subunit, pH 7.0, 30°C
0.16
-
at pH 6.5 and 37°C
0.00273
-
forward reaction, 37°C, pH 8
2
-
-
9.5
-
reverse reaction, 37°C, pH 8
20
-
pH 7.8, 37°C
10
-
pH 8.5
0.9
-
versus ADP, pH 7.5, 37°C
23
-
versus phosphocreatine, pH 7.5, 37°C
14
-
pH 7.5, 37°C
5
-

IC50 Value (8 results)

COMMENTARY
EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
LITERATURE
L89A, pH 7.5, 37°C
0.012
-
mutant S27A, pH 7.5, 37°C
0.0075
-
R101A, pH 7.5, 37°C
0.004
-
wild-type, pH 7.5, 37°C
0.005
-
-
2
-
IC50 above 70 mM
70
-
pH 7.5, 37°C
13
-
pH 7.0, 30°C
131
-

References & Links

Links to other databases for L-valine

ChEBI
PubChem
ChEBI
PubChem